Updated on 2024/05/15

写真a

 
SENJU Yosuke
 
Organization
Research Institute for Interdisciplinary Science Special-Appointment Lecturer
Position
Special-Appointment Lecturer
External link

Degree

  • Doctor of Science, Ph.D. ( Tohoku University )

  • Master of Science ( Tohoku University )

  • Bachelor of Science ( Tohoku University )

Research Interests

  • Biophysics

  • Structural biology

  • Actin

  • Lipid

  • Self-assembly

  • Biomembranes

  • Cytoskeleton/Cell motility

  • Liposome

  • Thermodynamics

  • Rheology

  • Drug discovery

  • Microbiology

  • BAR domain

Research Areas

  • Life Science / Biophysics

  • Natural Science / Biophysics, chemical physics and soft matter physics

Education

  • Aichi Prefectural Okazaki High School    

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  • Tohoku University   理学部   物理学科

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    Country: Japan

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  • Tohoku University   大学院理学研究科   物理学専攻

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    Country: Japan

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Research History

  • Okayama University   Research Institute for Interdisciplinary Science (RIIS)   Lecturer

    2021.4

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    Country:Japan

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  • Okayama University   Research Institute for Interdisciplinary Science (RIIS)   Assistant Professor

    2019.4 - 2021.3

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    Country:Japan

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  • Tohoku University   Department of Physics, Graduate School of Science   RA

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  • The University of Tokyo   The Institute for Quantitative Biosciences (IQB)   Assistant Professor

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  • Tohoku University   Department of Physics, Graduate School of Science   TA

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  • University of Helsinki   Institute of Biotechnology   postdoctoral fellow

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  • The University of Tokyo   The Institute for Quantitative Biosciences (IQB)   postdoctoral fellow

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Professional Memberships

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Committee Memberships

  • PeerJ   Editorial Board of Academic Editors  

    2023.10   

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    Committee type:Academic society

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  • BMC journal (Springer Nature)   Editorial Board Member  

    2023.8   

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  • The Biophysical Society of Japan   分野別専門委員  

    2023.1 - 2024.12   

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  • United Japanese researchers Around the world   ワーキンググループメンバー  

    2021.12   

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Papers

  • Activated I-BAR IRSp53 clustering controls the formation of VASP-actin-based membrane protrusions. Reviewed International coauthorship International journal

    Feng-Ching Tsai, J Michael Henderson, Zack Jarin, Elena Kremneva, Yosuke Senju, Julien Pernier, Oleg Mikhajlov, John Manzi, Konstantin Kogan, Christophe Le Clainche, Gregory A Voth, Pekka Lappalainen, Patricia Bassereau

    Science advances   8 ( 41 )   eabp8677   2022.10

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    Filopodia are actin-rich membrane protrusions essential for cell morphogenesis, motility, and cancer invasion. How cells control filopodium initiation on the plasma membrane remains elusive. We performed experiments in cellulo, in vitro, and in silico to unravel the mechanism of filopodium initiation driven by the membrane curvature sensor IRSp53 (insulin receptor substrate protein of 53 kDa). We showed that full-length IRSp53 self-assembles into clusters on membranes depending on PIP2. Using well-controlled in vitro reconstitution systems, we demonstrated that IRSp53 clusters recruit the actin polymerase VASP (vasodilator-stimulated phosphoprotein) to assemble actin filaments locally on membranes, leading to the generation of actin-filled membrane protrusions reminiscent of filopodia. By pulling membrane nanotubes from live cells, we observed that IRSp53 can only be enriched and trigger actin assembly in nanotubes at highly dynamic membrane regions. Our work supports a regulation mechanism of IRSp53 in its attributes of curvature sensation and partner recruitment to ensure a precise spatial-temporal control of filopodium initiation.

    DOI: 10.1126/sciadv.abp8677

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  • A biophysical perspective of the regulatory mechanisms of ezrin/radixin/moesin proteins. Invited Reviewed International coauthorship International journal

    Yosuke Senju, Feng-Ching Tsai

    Biophysical reviews   14 ( 1 )   199 - 208   2022.2

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    Many signal transductions resulting from ligand-receptor interactions occur at the cell surface. These signaling pathways play essential roles in cell polarization, membrane morphogenesis, and the modulation of membrane tension at the cell surface. However, due to the large number of membrane-binding proteins, including actin-membrane linkers, and transmembrane proteins present at the cell surface, the molecular mechanisms underlying the regulation at the cell surface are yet unclear. Here, we describe the molecular functions of one of the key players at the cell surface, ezrin/radixin/moesin (ERM) proteins from a biophysical point of view. We focus our discussion on biophysical properties of ERM proteins revealed by using biophysical tools in live cells and in vitro reconstitution systems. We first describe the structural properties of ERM proteins and then discuss the interactions of ERM proteins with PI(4,5)P2 and the actin cytoskeleton. These properties of ERM proteins revealed by using biophysical approaches have led to a better understanding of their physiological functions in cells and tissues. Supplementary Information: The online version contains supplementary material available at 10.1007/s12551-021-00928-0.

    DOI: 10.1007/s12551-021-00928-0

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  • Liposome Co-sedimentation and Co-flotation Assays to Study Lipid–Protein Interactions Reviewed International coauthorship International journal

    Yosuke Senju, Pekka Lappalainen, Hongxia Zhao

    Methods in Molecular Biology   195 - 204   2021

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    Authorship:Lead author, Corresponding author   Language:English   Publishing type:Part of collection (book)   Publisher:Springer US  

    DOI: 10.1007/978-1-0716-1142-5_14

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  • Fluorescence Assays to Study Membrane Penetration of Proteins Reviewed International coauthorship International journal

    Yosuke Senju, Hongxia Zhao

    Methods in Molecular Biology   215 - 223   2021

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    DOI: 10.1007/978-1-0716-1142-5_16

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  • Spatiotemporal Analysis of Caveolae Dynamics Using Total Internal Reflection Fluorescence Microscopy. Reviewed International journal

    Yosuke Senju, Shiro Suetsugu

    Methods in molecular biology (Clifton, N.J.)   2169   63 - 70   2020

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    Total internal reflection fluorescence microscopy enables to analyze the localizations and dynamics of cellular events that occur at or near the plasma membrane. Total internal reflection fluorescence microscopy exclusively illuminates molecules in the close vicinity of the glass surface, thereby reducing background fluorescence and enabling observation of the plasma membrane in the glass-attached cells with a high signal-to-noise ratio. Here, we describe the application of total internal reflection fluorescence microscopy to analyze the dynamics of caveolae, which play essential physiological functions, including membrane tension buffering, endocytosis, and signaling at the plasma membrane.

    DOI: 10.1007/978-1-0716-0732-9_6

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  • Regulation of actin dynamics by PI(4,5)P2 in cell migration and endocytosis. Invited Reviewed International journal

    Yosuke Senju, Pekka Lappalainen

    Current opinion in cell biology   56   7 - 13   2019.2

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    The actin cytoskeleton is indispensable for several cellular processes, including migration, morphogenesis, polarized growth, endocytosis, and phagocytosis. The organization and dynamics of the actin cytoskeleton in these processes are regulated by Rho family small GTPases and kinase-phosphatase pathways. Moreover, membrane phospholipids, especially the phosphatidylinositol phosphates have emerged as important regulators of actin dynamics. From these, PI(4,5)P2 is the most abundant at the plasma membrane, and directly regulates the activities and subcellular localizations of numerous actin-binding proteins. Here, we discuss recent studies demonstrating that actin-binding proteins interact with PI(4,5)P2-rich membranes through drastically different affinities and dynamics correlating with their roles in cytoskeletal dynamics. Moreover, by using mesenchymal cell migration and clathrin-mediated endocytosis as examples, we present a model for how interplay between PI(4,5)P2 and actin-binding proteins control the actin cytoskeleton in cells.

    DOI: 10.1016/j.ceb.2018.08.003

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  • Mechanistic principles underlying regulation of the actin cytoskeleton by phosphoinositides. Reviewed International journal

    Yosuke Senju, Maria Kalimeri, Essi V Koskela, Pentti Somerharju, Hongxia Zhao, Ilpo Vattulainen, Pekka Lappalainen

    Proceedings of the National Academy of Sciences of the United States of America   114 ( 43 )   E8977-E8986 - E8986   2017.10

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    Authorship:Lead author   Language:English   Publishing type:Research paper (scientific journal)   Publisher:NATL ACAD SCIENCES  

    The actin cytoskeleton powers membrane deformation during many cellular processes, such as migration, morphogenesis, and endocytosis. Membrane phosphoinositides, especially phosphatidylinositol 4,5-bisphosphate [PI(4,5)P2], regulate the activities of many actin-binding proteins (ABPs), including profilin, cofilin, Dia2, N-WASP, ezrin, and moesin, but the underlying molecular mechanisms have remained elusive. Moreover, because of a lack of available methodology, the dynamics of membrane interactions have not been experimentally determined for any ABP. Here, we applied a combination of biochemical assays, photobleaching/activation approaches, and atomistic molecular dynamics simulations to uncover the molecular principles by which ABPs interact with phosphoinositide-rich membranes. We show that, despite using different domains for lipid binding, these proteins associate with membranes through similar multivalent electrostatic interactions, without specific binding pockets or penetration into the lipid bilayer. Strikingly, our experiments reveal that these proteins display enormous differences in the dynamics of membrane interactions and in the ranges of phosphoinositide densities that they sense. Profilin and cofilin display transient, low-affinity interactions with phosphoinositide-rich membranes, whereas F-actin assembly factors Dia2 and N-WASP reside on phosphoinositide-rich membranes for longer periods to perform their functions. Ezrin and moesin, which link the actin cytoskeleton to the plasma membrane, bind membranes with very high affinity and slow dissociation dynamics. Unlike profilin, cofilin, Dia2, and N-WASP, they do not require high "stimulus-responsive" phosphoinositide density for membrane binding. Moreover, ezrin can limit the lateral diffusion of PI(4,5)P2 along the lipid bilayer. Together, these findings demonstrate that membrane-interaction mechanisms of ABPs evolved to precisely fulfill their specific functions in cytoskeletal dynamics.

    DOI: 10.1073/pnas.1705032114

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  • Phosphorylation of PACSIN2 by protein kinase C triggers the removal of caveolae from the plasma membrane. Reviewed International journal

    Yosuke Senju, Eva Rosenbaum, Claudio Shah, Sayaka Hamada-Nakahara, Yuzuru Itoh, Kimiko Yamamoto, Kyoko Hanawa-Suetsugu, Oliver Daumke, Shiro Suetsugu

    Journal of cell science   128 ( 15 )   2766 - 80   2015.8

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    PACSIN2, a membrane-sculpting BAR domain protein, localizes to caveolae. Here, we found that protein kinase C (PKC) phosphorylates PACSIN2 at serine 313, thereby decreasing its membrane binding and tubulation capacities. Concomitantly, phosphorylation decreased the time span for which caveolae could be tracked at the plasma membrane (the 'tracking duration'). Analyses of the phospho-mimetic S313E mutant suggested that PACSIN2 phosphorylation was sufficient to reduce caveolar-tracking durations. Both hypotonic treatment and isotonic drug-induced PKC activation increased PACSIN2 phosphorylation at serine 313 and shortened caveolar-tracking durations. Caveolar-tracking durations were also reduced upon the expression of other membrane-binding-deficient PACSIN2 mutants or upon RNA interference (RNAi)-mediated PACSIN2 depletion, pointing to a role for PACSIN2 levels in modulating the lifetime of caveolae. Interestingly, the decrease in membrane-bound PACSIN2 was inversely correlated with the recruitment and activity of dynamin 2, a GTPase that mediates membrane scission. Furthermore, expression of EHD2, which stabilizes caveolae and binds to PACSIN2, restored the tracking durations of cells with reduced PACSIN2 levels. These findings suggest that the PACSIN2 phosphorylation decreases its membrane-binding activity, thereby decreasing its stabilizing effect on caveolae and triggering dynamin-mediated removal of caveolae.

    DOI: 10.1242/jcs.167775

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  • Possible regulation of caveolar endocytosis and flattening by phosphorylation of F-BAR domain protein PACSIN2/Syndapin II. Reviewed International journal

    Yosuke Senju, Shiro Suetsugu

    Bioarchitecture   5 ( 5-6 )   70 - 7   2015

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    Caveolae are flask-shaped invaginations of the plasma membrane. The BAR domain proteins form crescent-shaped dimers, and their oligomeric filaments are considered to form spirals at the necks of invaginations, such as clathrin-coated pits and caveolae. PACSIN2/Syndapin II is one of the BAR domain-containing proteins, and is localized at the necks of caveolae. PACSIN2 is thought to function in the scission and stabilization of caveolae, through binding to dynamin-2 and EHD2, respectively. These two functions are considered to be switched by PACSIN2 phosphorylation by protein kinase C (PKC) upon hypotonic stress and sheer stress. The phosphorylation decreases the membrane binding affinity of PACSIN2, leading to its removal from caveolae. The removal of the putative oligomeric spiral of PACSIN2 from caveolar membrane invaginations could lead to the deformation of caveolae. Indeed, PACSIN2 removal from caveolae is accompanied by the recruitment of dynamin-2, suggesting that the removal provides space for the function of dynamin-2. Otherwise, the removal of PACSIN2 decreases the stability of caveolae, which could result in the flattening of caveolae. In contrast, an increase in the amount of EHD2 restored caveolar stability. Therefore, PACSIN2 at caveolae stabilizes caveolae, but its removal by phosphorylation could induce both caveolar endocytosis and flattening.

    DOI: 10.1080/19490992.2015.1128604

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  • Direct interaction of actin filaments with F-BAR protein pacsin2. Reviewed International journal

    Julius Kostan, Ulrich Salzer, Albina Orlova, Imre Törö, Vesna Hodnik, Yosuke Senju, Juan Zou, Claudia Schreiner, Julia Steiner, Jari Meriläinen, Marko Nikki, Ismo Virtanen, Oliviero Carugo, Juri Rappsilber, Pekka Lappalainen, Veli-Pekka Lehto, Gregor Anderluh, Edward H Egelman, Kristina Djinović-Carugo

    EMBO reports   15 ( 11 )   1154 - 62   2014.11

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    Two mechanisms have emerged as major regulators of membrane shape: BAR domain-containing proteins, which induce invaginations and protrusions, and nuclear promoting factors, which cause generation of branched actin filaments that exert mechanical forces on membranes. While a large body of information exists on interactions of BAR proteins with membranes and regulatory proteins of the cytoskeleton, little is known about connections between these two processes. Here, we show that the F-BAR domain protein pacsin2 is able to associate with actin filaments using the same concave surface employed to bind to membranes, while some other tested N-BAR and F-BAR proteins (endophilin, CIP4 and FCHO2) do not associate with actin. This finding reveals a new level of complexity in membrane remodeling processes.

    DOI: 10.15252/embr.201439267

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  • Essential role of PACSIN2/syndapin-II in caveolae membrane sculpting. Reviewed International journal

    Yosuke Senju, Yuzuru Itoh, Kazunori Takano, Sayaka Hamada, Shiro Suetsugu

    Journal of cell science   124 ( Pt 12 )   2032 - 40   2011.6

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    Caveolae are flask-shaped invaginations of the plasma membrane that are associated with tumor formation, pathogen entry and muscular dystrophy, through the regulation of lipids, signal transduction and endocytosis. Caveolae are generated by the fusion of caveolin-1-containing vesicles with the plasma membrane, which then participate in endocytosis via dynamin. Proteins containing membrane-sculpting F-BAR (or EFC) domains organize the membrane in clathrin-mediated endocytosis. Here, we show that the F-BAR protein PACSIN2 sculpts the plasma membrane of the caveola. The PACSIN2 F-BAR domain interacts directly with caveolin-1 by unmasking autoinhibition of PACSIN2. Furthermore, the membrane invaginations induced by the PACSIN2 F-BAR domain contained caveolin-1. Knockdown of PACSIN2 resulted in abnormal morphology of caveolin-1-associated plasma membranes, presumably as a result of decreased recruitment of dynamin-2 to caveolin-1. These results indicate that PACSIN2 mediates membrane sculpting by caveolin-1 in caveola morphology and recruits dynamin-2 for caveola fission.

    DOI: 10.1242/jcs.086264

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  • Subcellular membrane curvature mediated by the BAR domain superfamily proteins. Reviewed International journal

    Shiro Suetsugu, Kiminori Toyooka, Yosuke Senju

    Seminars in cell & developmental biology   21 ( 4 )   340 - 9   2010.6

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    The Bin-Amphiphysin-Rvs167 (BAR) domain superfamily consists of proteins containing the BAR domain, the extended FCH (EFC)/FCH-BAR (F-BAR) domain, or the IRSp53-MIM homology domain (IMD)/inverse BAR (I-BAR) domain. These domains bind membranes through electrostatic interactions between the negative charges of the membranes and the positive charges on the structural surface of homo-dimeric BAR domain superfamily members. Some BAR superfamily members have membrane-penetrating insertion loops, which also contribute to the membrane binding by the proteins. The membrane-binding surface of each BAR domain superfamily member has its own unique curvature that governs or senses the curvature of the membrane for BAR-domain binding. The wide range of BAR-domain surface curvatures correlates with the various invaginations and protrusions of cells. Therefore, each BAR domain superfamily member may generate and recognize the curvature of the membrane of each subcellular structure, such as clathrin-coated pits or filopodia. The BAR domain superfamily proteins may regulate their own catalytic activity or that of their binding proteins, depending on the membrane curvature of their corresponding subcellular structures.

    DOI: 10.1016/j.semcdb.2009.12.002

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  • The eukaryotic-like characteristics of small GTPase, roadblock and TRAPPC3 proteins from Asgard archaea. International journal

    Linh T Tran, Caner Akıl, Yosuke Senju, Robert C Robinson

    Communications biology   7 ( 1 )   273 - 273   2024.3

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    Membrane-enclosed organelles are defining features of eukaryotes in distinguishing these organisms from prokaryotes. Specification of distinct membranes is critical to assemble and maintain discrete compartments. Small GTPases and their regulators are the signaling molecules that drive membrane-modifying machineries to the desired location. These signaling molecules include Rab and Rag GTPases, roadblock and longin domain proteins, and TRAPPC3-like proteins. Here, we take a structural approach to assess the relatedness of these eukaryotic-like proteins in Asgard archaea, the closest known prokaryotic relatives to eukaryotes. We find that the Asgard archaea GTPase core domains closely resemble eukaryotic Rabs and Rags. Asgard archaea roadblock, longin and TRAPPC3 domain-containing proteins form dimers similar to those found in the eukaryotic TRAPP and Ragulator complexes. We conclude that the emergence of these protein architectures predated eukaryogenesis, however further adaptations occurred in proto-eukaryotes to allow these proteins to regulate distinct internal membranes.

    DOI: 10.1038/s42003-024-05888-1

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  • Membrane Proteins: Function, Structure, and Dynamics. Invited International journal

    Yosuke Senju, Shiro Suetsugu

    Membranes   13 ( 12 )   2023.12

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    Plasma and intracellular membranes are characterized by different lipid compositions that enable proteins to localize to distinct subcellular compartments [...].

    DOI: 10.3390/membranes13120904

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  • Actin-rich lamellipodia-like protrusions contribute to the integrity of epithelial cell-cell junctions. Reviewed International coauthorship International journal

    Yosuke Senju, Toiba Mushtaq, Helena Vihinen, Aki Manninen, Juha Saarikangas, Katharina Ven, Ulrike Engel, Markku Varjosalo, Eija Jokitalo, Pekka Lappalainen

    The Journal of biological chemistry   104571 - 104571   2023.3

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    Metastasis-suppressor 1 (MTSS1) is a membrane-interacting scaffolding protein that regulates the integrity of epithelial cell-cell junctions and functions as a tumor suppressor in a wide range of carcinomas. MTSS1 binds phosphoinositide-rich membranes through its I-BAR domain, and is capable of sensing and generating negative membrane curvature in vitro. However, the mechanisms by which MTSS1 localizes to intercellular junctions in epithelial cells, and contributes to their integrity and maintenance have remained elusive. By carrying out electron microscopy and live-cell imaging on cultured Madin-Darby canine kidney (MDCK) cell monolayers, we provide evidence that adherens junctions of epithelial cells harbor lamellipodia-like, dynamic actin-driven membrane folds, which exhibit high negative membrane curvature at their distal edges. BioID proteomics and imaging experiments demonstrated that MTSS1 associates with an Arp2/3 complex activator, the WAVE-2 complex, in dynamic actin-rich protrusions at cell-cell junctions. Inhibition of Arp2/3 or WAVE-2 suppressed actin filament assembly at adherens junctions, decreased the dynamics of junctional membrane protrusions, and led to defects in epithelial integrity. Together, these results support a model in which membrane-associated MTSS1, together with the WAVE-2 and Arp2/3 complexes, promotes the formation of dynamic lamellipodia-like actin protrusions that contribute to the integrity of cell-cell junctions in epithelial monolayers.

    DOI: 10.1016/j.jbc.2023.104571

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  • Moesin-ezrin-radixin-like protein merlin: Its conserved and distinct functions from those of ERM proteins. Invited Reviewed International journal

    Yosuke Senju, Emi Hibino

    Biochimica et biophysica acta. Biomembranes   1865 ( 2 )   184076 - 184076   2022.10

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    DOI: 10.1016/j.bbamem.2022.184076

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  • Structural and biochemical evidence for the emergence of a calcium-regulated actin cytoskeleton prior to eukaryogenesis. Reviewed International coauthorship International journal

    Caner Akıl, Linh T Tran, Magali Orhant-Prioux, Yohendran Baskaran, Yosuke Senju, Shuichi Takeda, Phatcharin Chotchuang, Duangkamon Muengsaen, Albert Schulte, Edward Manser, Laurent Blanchoin, Robert C Robinson

    Communications biology   5 ( 1 )   890 - 890   2022.8

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    Charting the emergence of eukaryotic traits is important for understanding the characteristics of organisms that contributed to eukaryogenesis. Asgard archaea and eukaryotes are the only organisms known to possess regulated actin cytoskeletons. Here, we determined that gelsolins (2DGels) from Lokiarchaeota (Loki) and Heimdallarchaeota (Heim) are capable of regulating eukaryotic actin dynamics in vitro and when expressed in eukaryotic cells. The actin filament severing and capping, and actin monomer sequestering, functionalities of 2DGels are strictly calcium controlled. We determined the X-ray structures of Heim and Loki 2DGels bound actin monomers. Each structure possesses common and distinct calcium-binding sites. Loki2DGel has an unusual WH2-like motif (LVDV) between its two gelsolin domains, in which the aspartic acid coordinates a calcium ion at the interface with actin. We conclude that the calcium-regulated actin cytoskeleton predates eukaryogenesis and emerged in the predecessors of the last common ancestor of Loki, Heim and Thorarchaeota.

    DOI: 10.1038/s42003-022-03783-1

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  • Bex1 is essential for ciliogenesis and harbours biomolecular condensate-forming capacity. Reviewed International journal

    Emi Hibino, Yusuke Ichiyama, Atsushi Tsukamura, Yosuke Senju, Takao Morimune, Masahito Ohji, Yoshihiro Maruo, Masaki Nishimura, Masaki Mori

    BMC biology   20 ( 1 )   42 - 42   2022.2

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    BACKGROUND: Primary cilia are sensory organelles crucial for organ development. The pivotal structure of the primary cilia is a microtubule that is generated via tubulin polymerization reaction that occurs in the basal body. It remains to be elucidated how molecules with distinct physicochemical properties contribute to the formation of the primary cilia. RESULTS: Here we show that brain expressed X-linked 1 (Bex1) plays an essential role in tubulin polymerization and primary cilia formation. The Bex1 protein shows the physicochemical property of being an intrinsically disordered protein (IDP). Bex1 shows cell density-dependent accumulation as a condensate either in nucleoli at a low cell density or at the apical cell surface at a high cell density. The apical Bex1 localizes to the basal body. Bex1 knockout mice present ciliopathy phenotypes and exhibit ciliary defects in the retina and striatum. Bex1 recombinant protein shows binding capacity to guanosine triphosphate (GTP) and forms the condensate that facilitates tubulin polymerization in the reconstituted system. CONCLUSIONS: Our data reveals that Bex1 plays an essential role for the primary cilia formation through providing the reaction field for the tubulin polymerization.

    DOI: 10.1186/s12915-022-01246-x

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  • Interaction of Proteins with Biomembranes. International journal

    Yosuke Senju, Shiro Suetsugu

    Membranes   12 ( 2 )   2022.2

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    Many proteins interact with cell and subcellular membranes [...].

    DOI: 10.3390/membranes12020181

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  • Dynamin 2 and BAR domain protein pacsin 2 cooperatively regulate formation and maturation of podosomes. Reviewed International journal

    Jianzhen Li, Kenshiro Fujise, Haymar Wint, Yosuke Senju, Shiro Suetsugu, Hiroshi Yamada, Kohji Takei, Tetsuya Takeda

    Biochemical and biophysical research communications   571   145 - 151   2021.9

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    Podosomes are actin-rich adhesion structures formed in a variety of cell types, such as monocytic cells or cancer cells, to facilitate attachment to and degradation of the extracellular matrix (ECM). Previous studies showed that dynamin 2, a large GTPase involved in membrane remodeling and actin organization, is required for podosome function. However, precise roles of dynamin 2 at the podosomes remain to be elucidated. In this study, we identified a BAR (Bin-Amphiphysin-Rvs167) domain protein pacsin 2 as a functional partner of dynamin 2 at podosomes. Dynamin 2 and pacsin 2 interact and co-localize to podosomes in Src-transformed NIH 3T3 (NIH-Src) cells. RNAi of either dynamin 2 or pacsin 2 in NIH-Src cells inhibited podosome formation and maturation, suggesting essential and related roles at podosomes. Consistently, RNAi of pacsin 2 prevented dynamin 2 localization to podosomes, and reciprocal RNAi of dynamin 2 prevented pacsin 2 localization to podosomes. Taking these results together, we conclude that dynamin 2 and pacsin 2 co-operatively regulate organization of podosomes in NIH-Src cells.

    DOI: 10.1016/j.bbrc.2021.07.041

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  • Ezrin enrichment on curved membranes requires a specific conformation or interaction with a curvature-sensitive partner. Reviewed International journal

    Feng-Ching Tsai, Aurelie Bertin, Hugo Bousquet, John Manzi, Yosuke Senju, Meng-Chen Tsai, Laura Picas, Stephanie Miserey-Lenkei, Pekka Lappalainen, Emmanuel Lemichez, Evelyne Coudrier, Patricia Bassereau

    eLife   7   2018.9

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    One challenge in cell biology is to decipher the biophysical mechanisms governing protein enrichment on curved membranes and the resulting membrane deformation. The ERM protein ezrin is abundant and associated with cellular membranes that are flat, positively or negatively curved. Using in vitro and cell biology approaches, we assess mechanisms of ezrin's enrichment on curved membranes. We evidence that wild-type ezrin (ezrinWT) and its phosphomimetic mutant T567D (ezrinTD) do not deform membranes but self-assemble anti-parallelly, zipping adjacent membranes. EzrinTD's specific conformation reduces intermolecular interactions, allows binding to actin filaments, which reduces membrane tethering, and promotes ezrin binding to positively-curved membranes. While neither ezrinTD nor ezrinWT senses negative curvature alone, we demonstrate that interacting with curvature-sensing I-BAR-domain proteins facilitates ezrin enrichment in negatively-curved membrane protrusions. Overall, our work demonstrates that ezrin can tether membranes, or be targeted to curved membranes, depending on conformations and interactions with actin and curvature-sensing binding partners.

    DOI: 10.7554/eLife.37262

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  • Measurement of caveolin-1 densities in the cell membrane for quantification of caveolar deformation after exposure to hypotonic membrane tension. Reviewed International journal

    Masashi Tachikawa, Nobuhiro Morone, Yosuke Senju, Tadao Sugiura, Kyoko Hanawa-Suetsugu, Atsushi Mochizuki, Shiro Suetsugu

    Scientific reports   7 ( 1 )   7794 - 7794   2017.8

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    Caveolae are abundant flask-shaped invaginations of plasma membranes that buffer membrane tension through their deformation. Few quantitative studies on the deformation of caveolae have been reported. Each caveola contains approximately 150 caveolin-1 proteins. In this study, we estimated the extent of caveolar deformation by measuring the density of caveolin-1 projected onto a two-dimensional (2D) plane. The caveolin-1 in a flattened caveola is assumed to have approximately one-quarter of the density of the caveolin-1 in a flask-shaped caveola. The proportion of one-quarter-density caveolin-1 increased after increasing the tension of the plasma membrane through hypo-osmotic treatment. The one-quarter-density caveolin-1 was soluble in detergent and formed a continuous population with the caveolin-1 in the caveolae of cells under isotonic culture. The distinct, dispersed lower-density caveolin-1 was soluble in detergent and increased after the application of tension, suggesting that the hypo-osmotic tension induced the dispersion of caveolin-1 from the caveolae, possibly through flattened caveolar intermediates.

    DOI: 10.1038/s41598-017-08259-5

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  • ADF/Cofilin Accelerates Actin Dynamics by Severing Filaments and Promoting Their Depolymerization at Both Ends. Reviewed International journal

    Hugo Wioland, Berengere Guichard, Yosuke Senju, Sarah Myram, Pekka Lappalainen, Antoine Jégou, Guillaume Romet-Lemonne

    Current biology : CB   27 ( 13 )   1956 - 1967   2017.7

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    Actin-depolymerizing factor (ADF)/cofilins contribute to cytoskeletal dynamics by promoting rapid actin filament disassembly. In the classical view, ADF/cofilin sever filaments, and capping proteins block filament barbed ends whereas pointed ends depolymerize, at a rate that is still debated. Here, by monitoring the activity of the three mammalian ADF/cofilin isoforms on individual skeletal muscle and cytoplasmic actin filaments, we directly quantify the reactions underpinning filament severing and depolymerization from both ends. We find that, in the absence of monomeric actin, soluble ADF/cofilin can associate with bare filament barbed ends to accelerate their depolymerization. Compared to bare filaments, ADF/cofilin-saturated filaments depolymerize faster from their pointed ends and slower from their barbed ends, resulting in similar depolymerization rates at both ends. This effect is isoform specific because depolymerization is faster for ADF- than for cofilin-saturated filaments. We also show that, unexpectedly, ADF/cofilin-saturated filaments qualitatively differ from bare filaments: their barbed ends are very difficult to cap or elongate, and consequently undergo depolymerization even in the presence of capping protein and actin monomers. Such depolymerizing ADF/cofilin-decorated barbed ends are produced during 17% of severing events. They are also the dominant fate of filament barbed ends in the presence of capping protein, because capping allows growing ADF/cofilin domains to reach the barbed ends, thereby promoting their uncapping and subsequent depolymerization. Our experiments thus reveal how ADF/cofilin, together with capping protein, control the dynamics of actin filament barbed and pointed ends. Strikingly, our results propose that significant barbed-end depolymerization may take place in cells.

    DOI: 10.1016/j.cub.2017.05.048

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  • Ezrin enhances line tension along transcellular tunnel edges via NMIIa driven actomyosin cable formation. Reviewed International journal

    Caroline Stefani, David Gonzalez-Rodriguez, Yosuke Senju, Anne Doye, Nadia Efimova, Sébastien Janel, Justine Lipuma, Meng Chen Tsai, Daniel Hamaoui, Madhavi P Maddugoda, Olivier Cochet-Escartin, Coline Prévost, Frank Lafont, Tatyana Svitkina, Pekka Lappalainen, Patricia Bassereau, Emmanuel Lemichez

    Nature communications   8   15839 - 15839   2017.6

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    Transendothelial cell macroaperture (TEM) tunnels control endothelium barrier function and are triggered by several toxins from pathogenic bacteria that provoke vascular leakage. Cellular dewetting theory predicted that a line tension of uncharacterized origin works at TEM boundaries to limit their widening. Here, by conducting high-resolution microscopy approaches we unveil the presence of an actomyosin cable encircling TEMs. We develop a theoretical cellular dewetting framework to interpret TEM physical parameters that are quantitatively determined by laser ablation experiments. This establishes the critical role of ezrin and non-muscle myosin II (NMII) in the progressive implementation of line tension. Mechanistically, fluorescence-recovery-after-photobleaching experiments point for the upstream role of ezrin in stabilizing actin filaments at the edges of TEMs, thereby favouring their crosslinking by NMIIa. Collectively, our findings ascribe to ezrin and NMIIa a critical function of enhancing line tension at the cell boundary surrounding the TEMs by promoting the formation of an actomyosin ring.

    DOI: 10.1038/ncomms15839

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  • MIM-Induced Membrane Bending Promotes Dendritic Spine Initiation. Reviewed International journal

    Juha Saarikangas, Nazim Kourdougli, Yosuke Senju, Genevieve Chazal, Mikael Segerstråle, Rimante Minkeviciene, Jaakko Kuurne, Pieta K Mattila, Lillian Garrett, Sabine M Hölter, Lore Becker, Ildikó Racz, Wolfgang Hans, Thomas Klopstock, Wolfgang Wurst, Andreas Zimmer, Helmut Fuchs, Valérie Gailus-Durner, Martin Hrabě de Angelis, Lotta von Ossowski, Tomi Taira, Pekka Lappalainen, Claudio Rivera, Pirta Hotulainen

    Developmental cell   33 ( 6 )   644 - 59   2015.6

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    Proper morphogenesis of neuronal dendritic spines is essential for the formation of functional synaptic networks. However, it is not known how spines are initiated. Here, we identify the inverse-BAR (I-BAR) protein MIM/MTSS1 as a nucleator of dendritic spines. MIM accumulated to future spine initiation sites in a PIP2-dependent manner and deformed the plasma membrane outward into a proto-protrusion via its I-BAR domain. Unexpectedly, the initial protrusion formation did not involve actin polymerization. However, PIP2-dependent activation of Arp2/3-mediated actin assembly was required for protrusion elongation. Overexpression of MIM increased the density of dendritic protrusions and suppressed spine maturation. In contrast, MIM deficiency led to decreased density of dendritic protrusions and larger spine heads. Moreover, MIM-deficient mice displayed altered glutamatergic synaptic transmission and compatible behavioral defects. Collectively, our data identify an important morphogenetic pathway, which initiates spine protrusions by coupling phosphoinositide signaling, direct membrane bending, and actin assembly to ensure proper synaptogenesis.

    DOI: 10.1016/j.devcel.2015.04.014

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  • TRPV4 channel activity is modulated by direct interaction of the ankyrin domain to PI(4,5)P₂. Reviewed International journal

    Nobuaki Takahashi, Sayaka Hamada-Nakahara, Yuzuru Itoh, Kazuhiro Takemura, Atsushi Shimada, Yoshifumi Ueda, Manabu Kitamata, Rei Matsuoka, Kyoko Hanawa-Suetsugu, Yosuke Senju, Masayuki X Mori, Shigeki Kiyonaka, Daisuke Kohda, Akio Kitao, Yasuo Mori, Shiro Suetsugu

    Nature communications   5   4994 - 4994   2014.9

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    Mutations in the ankyrin repeat domain (ARD) of TRPV4 are responsible for several channelopathies, including Charcot-Marie-Tooth disease type 2C and congenital distal and scapuloperoneal spinal muscular atrophy. However, the molecular pathogenesis mediated by these mutations remains elusive, mainly due to limited understanding of the TRPV4 ARD function. Here we show that phosphoinositide binding to the TRPV4 ARD leads to suppression of the channel activity. Among the phosphoinositides, phosphatidylinositol-4,5-bisphosphate (PI(4,5)P2) most potently binds to the TRPV4 ARD. The crystal structure of the TRPV4 ARD in complex with inositol-1,4,5-trisphosphate, the head-group of PI(4,5)P2, and the molecular-dynamics simulations revealed the PI(4,5)P2-binding amino-acid residues. The TRPV4 channel activities were increased by titration or hydrolysis of membrane PI(4,5)P2. Notably, disease-associated TRPV4 mutations that cause a gain-of-function phenotype abolished PI(4,5)P2 binding and PI(4,5)P2 sensitivity. These findings identify TRPV4 ARD as a lipid-binding domain in which interactions with PI(4,5)P2 normalize the channel activity in TRPV4.

    DOI: 10.1038/ncomms5994

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  • IRSp53 mediates podosome formation via VASP in NIH-Src cells. Reviewed International coauthorship International journal

    Tsukasa Oikawa, Hitomi Okamura, Franziska Dietrich, Yosuke Senju, Tadaomi Takenawa, Shiro Suetsugu

    PloS one   8 ( 3 )   e60528   2013

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    Podosomes are cellular "feet," characterized by F-actin-rich membrane protrusions, which drive cell migration and invasion into the extracellular matrix. Small GTPases that regulate the actin cytoskeleton, such as Cdc42 and Rac are central regulators of podosome formation. The adaptor protein IRSp53 contains an I-BAR domain that deforms membranes into protrusions and binds to Rac, a CRIB motif that interacts with Cdc42, an SH3 domain that binds to many actin cytoskeletal regulators with proline-rich peptides including VASP, and the C-terminal variable region by splicing. However, the role of IRSp53 and VASP in podosome formation had been unclear. Here we found that the knockdown of IRSp53 by RNAi attenuates podosome formation and migration in Src-transformed NIH3T3 (NIH-Src) cells. Importantly, the differences in the IRSp53 C-terminal splicing isoforms did not affect podosome formation. Overexpression of IRSp53 deletion mutants suggested the importance of linking small GTPases to SH3 binding partners. Interestingly, VASP physically interacted with IRSp53 in NIH-Src cells and was essential for podosome formation. These data highlight the role of IRSp53 as a linker of small GTPases to VASP for podosome formation.

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  • The role of actomyosin contractility in the formation and dynamics of actin bundles during fibroblast spreading. Reviewed International journal

    Yosuke Senju, Hidetake Miyata

    Journal of biochemistry   145 ( 2 )   137 - 50   2009.2

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    We studied the process of formation of stress fibres and involvement of phosphorylation of myosin-II during spreading of Swiss 3T3 fibroblasts. In cells that were allowed to spread for 1 h on a glass surface, circular bundles of actin and myosin-II filament were present. At 2-3 h after the plating, cells showed a polygonal and polarized shape. The proportion of the cells having circular bundles was decreased, whereas that of the cells with straight bundles of actin filaments was increased. At 4 h after the plating, cells were completely polarized and stress fibres were present at the periphery and the dorsal and ventral surfaces of the cells. Thus, spreading cells possessed different forms of actomyosin bundles corresponding to the cell shape. In circular bundles and stress fibres, myosin regulatory light chains were diphosphorylated. Formation of circular bundles and stress fibres was suppressed after the treatment of the cells with Y-27632, a Rho-kinase inhibitor, or blebbistatin, a myosin-II inhibitor. In digitonin-extracted cells, circular bundles as well as stress fibres contracted following the addition of Mg-ATP. These results suggest that circular bundles are contractile structures containing actin and phosphorylated myosin-II filaments, and the formation of circular bundles is regulated by Rho-kinase.

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  • Studying in Finland Reviewed

    Yosuke Senju

    MEMBRANE   48 ( 5 )   244 - 247   2023.10

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    DOI: 10.5360/membrane.48.244

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  • 培養細胞 Invited

    2023.4

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  • 国際会議に出席してみて Invited

    千住洋介

    分生研ニュース : 東京大学分子細胞生物学研究所広報誌   2012.7

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  • BAR domain Invited

    Yosuke Senju, Shiro Suetsugu

    2012.3

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  • Arp2/3 complex and actin polymerization Invited

    Yosuke Senju, Shiro Suetsugu

    2012.3

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  • カベオラにおけるF-BAR/EFCドメインタンパク質pacsinの機能解析 Invited

    千住洋介

    分生研ニュース : 東京大学分子細胞生物学研究所広報誌   2010.12

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  • Dynamics of actin filament bundles during fibroblast spreading

    Yosuke Senju

    The science reports of the Tohoku University. Ser.8, Physics and astronomy   2008.3

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  • 繊維芽細胞におけるストレスファイバー形成過程の研究 Invited

    千住 洋介, 宮田 英威

    日本バイオレオロジー学会年会抄録集   28   53   2005.6

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Presentations

  • Molecular mechanisms linking actin cytoskeleton to the plasma membrane Invited International coauthorship

    The 58th Annual Meeting of the Biophysics Society of Japan  2020.9.17  The Biophysical Society of Japan

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    Language:English   Presentation type:Oral presentation (invited, special)  

    Venue:Gunma  

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  • Mechanistic principles underlying regulation of the actin-binding proteins by phosphoinositides International conference

    The 11th TOYOTA RIKEN International Workshop "Actin Filament: beyond the atomic resolution structures"  2019.11.25  Toyota Riken

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    Venue:Nagoya University  

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  • Mechanistic principles underlying regulation of the actin cytoskeleton by phosphoinositides International conference

    ASCB | EMBO 2017 Meeting  2017.12.2  ASCB

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    Venue:Philadelphia, USA  

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  • Mechanistic principles underlying regulation of the actin dynamics by phosphoinositides International conference

    FEBS Advanced Lecture course and ECF2017 meeting on “cytoskeleton: mechanical coupling from the plasma membrane to nucleus”  2017.6.4  FEBS

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    Venue:Helsinki, Finland  

    Mechanistic principles underlying regulation of the actin cytoskeleton by phosphoinositides.

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  • Regulation of cell-cell adhesions by I-BAR domain proteins International conference

    ASCB Annual Meeting  2016.12.3 

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  • Function of I-BAR domain proteins at the interface of the actin cytoskeleton and plasma membrane Invited International conference

    Physics of living matter  2016.1.26 

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    Venue:University of Nice Sophia Antipolis  

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  • Regulation of cell-cell adhesions by I-BAR domain proteins International conference

    ASCB Annual Meeting  2015.12.12 

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  • Molecular Mechanism of F-BAR Protein Pacsin2 in Caveolae Biogenesis. International conference

    ASCB Annual Meeting  2011.12.3 

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    Venue:Denver, CO  

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  • F-BAR ドメインタンパク質pacsin2の分子機構とカベオラにおける機能

    第11回東京大学生命科学シンポジウム  2011.6.4 

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    Venue:東京大学本郷キャンパス  

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  • カベオラ形成におけるpacsin2の役割

    第10回東京大学生命科学シンポジウム  2010.5.1 

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    Venue:東京大学本郷キャンパス  

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  • Mechanistic principles underlying regulation of the actin cytoskeleton by phosphoinositides International coauthorship International conference

    Actin Assembly for Intracellular Functions  2020.2.20  University of Freiburg

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    Language:English   Presentation type:Poster presentation  

    Venue:Freiburg  

    The actin cytoskeleton provides forces for vital cellular processes involving membrane dynamics. Membrane phosphoinositides regulate many actin-binding proteins including cofilin, profilin, mDia2, N-WASP, ezrin and moesin, but the underlying mechanisms have remained elusive. By applying a combination of biochemical assays, photobleaching/activation approaches, and atomistic molecular dynamics simulations, we revealed that these proteins interact with membranes through multivalent electrostatic interactions, without specific binding pockets or penetrations into the lipid bilayers. However, their membrane-binding kinetics differ drastically. Cofilin and profilin exhibit transient, low-affinity interactions with phosphoinositide-containing membranes, whereas F-actin assembly factors mDia2 and N-WASP reside on phosphoinositide-containing membranes for longer periods to perform their functions. Ezrin and moesin, which link actin cytoskeleton to the plasma membrane, bind membranes with very high affinities and slow dissociation dynamics, and do not require high stimulus-responsive phosphoinositide density for membrane binding. Thus, membrane-interaction mechanisms of actin-binding proteins evolved to precisely fulfill their specific functions in cytoskeletal dynamics.

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  • Regulation of actin dynamics by phosphoinositides Invited

    2019.6.7  Research Core for Interdisciplinary Sciences, Okayama University

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    Venue:Research Core for Interdisciplinary Sciences, Okayama University  

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  • Regulation of actin assembly at cell-cell junctions of epithelial cells by BAR domain proteins Invited International conference

    Centre of Excellence - Academy of Finland 2019 meeting  2019.2.4 

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    Venue:Tallinn, Estonia  

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  • Regulation of actin assembly at cell-cell junctions of epithelial cells by BAR domain proteins International conference

    Symposium  2018.12.5  Institute of Biotechnology, University of Helsinki

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    Venue:Institute of Biotechnology, University of Helsinki  

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  • Regulation of actin assembly at cell-cell junctions of epithelial cells by BAR domain proteins International conference

    BioCity Symposium  2018.8.23  BioCity Turku

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    Venue:Turku Centre for Biotechnology  

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  • Regulation of actin assembly at cell-cell junctions of epithelial cells by BAR domain proteins International conference

    IN­TER­NA­TIONAL WORK­SHOP ON BIO­LO­GICAL MEM­BRANES  2018.8.19  UNIVERSITY OF HELSINKI

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    Venue:University of Helsinki  

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  • Regulation of actin dynamics by phosphoinositides Invited

    2018.7.31  NAIST BS

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  • Mechanistic principles underlying regulation of the actin cytoskeleton by PI(4,5)P2 International conference

    Symposium  2017.12.20  Institute of Biotechnology, University of Helsinki

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    Venue:Institute of Biotechnology, University of Helsinki  

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  • Mechanistic principles underlying regulation of the actin cytoskeleton by PI(4,5)P2 International conference

    Symposium  2017.12.19  Institute of Biotechnology, University of Helsinki

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    Venue:Institute of Biotechnology, University of Helsinki  

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  • Mechanistic principles underlying regulation of the actin cytoskeleton by phosphoinositides International conference

    ASCB | EMBO 2017 Meeting  2017.12.4  ASCB

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    Venue:Philadelphia, USA  

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  • Regulation of cell-cell contacts by I-BAR domain proteins International conference

    MEMBREC 2017 - Membrane Contact Sites  2017.9.5  University of Helsinki

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    Venue:Helsinki, Finland  

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  • Molecular mechanisms underlying regulation of actin-binding proteins by phosphoinositides Invited International conference

    Centre of Excellence - Academy of Finland 2017 meeting  2017.2.3 

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    Venue:University of Helsinki  

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  • Interactions of actin-binding proteins with membranes: Their dynamics correlate with their cellular functions International conference

    International Workshop on Biomembranes: The consequences of complexity  2016.8.16 

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    Venue:CECAM-FI, Finnish IT Center for Science, Espoo, Finland.  

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  • Dynamics of actin-binding protein interactions with PI(4,5)P2 correlate with their cellular functions International conference

    THE 9th FINNISH CELL BIOLOGY SYMPOSIUM  2016.4.14 

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    Venue:Lammi, Finland  

    Dynamics of actin-binding protein interactions with membranes correlate with their cellular functions

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  • Regulation of I-BAR domain proteins at the intercellular junctions of epithelial cells International conference

    4th MEMBREC Symposium  2015.9.3 

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    Venue:University of Helsinki  

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  • Regulation of I-BAR domain proteins at the intercellular junctions of epithelial cells International conference

    Bridging Nordic Imaging seminar  2015.8.13 

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    Venue:Turku, Finland  

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  • Dynamics of actin-binding protein interactions with membranes correlate with their cellular functions Invited International conference

    THE 8th FINNISH CELL BIOLOGY SYMPOSIUM  2015.4.16 

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    Venue:Lammi, Finland  

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  • Interplay between plasma membrane and actin-binding proteins Invited International conference

    Centre of Excellence - Academy of Finland 2015 meeting  2015.2.5 

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    Venue:Tampere University of Technology  

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  • Regulation of I-BAR domain proteins at intercellular junctions of epithelial cells. International conference

    Molecular basis for membrane remodelling and organization  2014.11.15 

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    Venue:Roscoff, France  

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  • Regulation of I-BAR domain proteins at intercellular junctions of epithelial cells. Invited International conference

    Nordic Network For Dynamic Biomembrane Research  2014.5.15 

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    Venue:Åland Islands  

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  • Regulation of I-BAR domain proteins at intercellular junctions of epithelial cells. International conference

    THE 7th FINNISH CELL BIOLOGY SYMPOSIUM  2014.4.3 

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    Venue:Lammi, Finland  

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  • Regulation of I-BAR domain proteins at intercellular junctions of epithelial cells. International conference

    Centre of Excellence - Academy of Finland 2014 meeting  2014.2.5 

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    Venue:University of Helsinki  

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  • The function of MIM at intercellular junctions of epithelial cells. International conference

    ASCB Annual Meeting  2013.12.14 

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    Venue:New Orleans, LA  

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  • Regulation of the actin cytoskeleton – plasma membrane interplay. Invited International conference

    Nordic Network For Dynamic Biomembrane Research  2012.9.13 

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    Venue:Skokloster, Sweden  

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  • Molecular mechanism of caveolae formation mediated by the F-BAR protein pacsin2.

    The 63rd Annual Meeting of Japan Society for Cell Biology  2011.6.27 

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    Venue:Hokkaido University  

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  • Essential Role of Pacsin2/Syndapin II in Membrane Fusion for Caveolae Formation. International conference

    ASCB Annual Meeting  2010.12.11 

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    Venue:Philadelphia, PA  

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  • The role of F-BAR protein pacsin2 in the formation of caveolae.

    The 48th Annual Meeting of the Biophysical Society of Japan  2010.9.20 

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    Venue:東北大学川内キャンパス  

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  • Remodeling of actin filament bundles and focal adhesions during fibroblast spreading.

    45th Annual Meeting of the Biophysical Society of Japan  2007.12.21 

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    Venue:Pacifico Yokohama  

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  • Tension-dependent formation of focal adhesions during fibroblast spreading. International conference

    The 6th COE Symposium (The 21st Century Center-of Excellence Program “Exploring New Science by Bridging Particle-Matter Hierarchy”)  2007.12 

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    Venue:Sendai, Japan  

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  • Dynamics of actin filament bundles and focal adhesions during fibroblast spreading. International conference

    Asia Science Forum  2007.9 

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    Venue:Sendai International Center, Sendai, Japan  

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  • 繊維芽細胞伸展時における焦点接着の動態解析.

    第4回東北大学バイオサイエンスシンポジウム  2007.6 

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    Venue:仙台国際センター,  

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  • Formation and dynamics of focal adhesions in spreading fibroblasts.

    The 59th Annual Meeting of Japan Society for Cell Biology  2007.5 

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    Venue:Fukuoka Convention Center  

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  • Formation and dynamics of focal adhesions in spreading cells International conference

    The Fifth COE Symposium (The 21st Century Center-of Excellence Program “Exploring New Science by Bridging Particle-Matter Hierarchy”)  2007.2 

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    Venue:Sendai, Japan  

    Formation and dynamics of focal adhesions in spreading fibroblasts.

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  • Cell polarization accompanies stress fiber formation in spreading fibroblasts. International conference

    Fifth East Asian Biophysics Symposium & Forty-Fourth Annual Meeting of the Biophysical Society of Japan  2006.11 

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    Venue:Okinawa, Japan  

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  • Formation of stress fibers in spreading cells International conference

    20th IUBMB International Congress of Biochemistry and Molecular Biology and 11th FAOBMB Congress  2006.6.18 

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    Language:English   Presentation type:Poster presentation  

    Venue:Kyoto, Japan  

    Formation of stress fibers in spreading fibroblasts.

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  • 繊維芽細胞伸展時におけるストレスファイバー形成について.

    第3回東北大学バイオサイエンスシンポジウム  2006.5.29 

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    Language:Japanese   Presentation type:Poster presentation  

    Venue:仙台国際センター  

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  • Formation and contraction of stress fibers. International conference

    The 3rd COE Symposium (The 21st Century Center-of Excellence Program “Exploring New Science by Bridging Particle-Matter Hierarchy”)  2006.2.16 

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  • Formation of stress fibers in spreading fibroblasts.

    ANNOUNCEMENT OF THE 43rd ANNUAL MEETING OF THE BIOPHYSICAL SOCIETY OF JAPAN  2005.11.23 

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    Language:English   Presentation type:Poster presentation  

    Venue:Sapporo Convention Center  

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  • Formation of stress fibers in spreading fibroblasts. Invited

    Japanese Society of Biorheology  2005.7.7 

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    Language:Japanese   Presentation type:Oral presentation (general)  

    Venue:Tohoku University  

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  • Formation of stress fibers: existence of rho-kinase and myosin light kinase-dependent pathways.

    The 58th Annual Meeting of Japan Society for Cell Biology  2005.6 

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    Venue:Omiya Sonic City  

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  • ストレスファイバー形成過程の可視化: アクトミオシン相互作用の役割.

    第42回日本生物物理学会年会  2004.12.13 

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    Language:Japanese   Presentation type:Poster presentation  

    Venue:国立京都国際会館  

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  • Transformation of the actin filament bundles in spreading fibroblasts: elucidation of the mechanism of the formation of stress fibers.

    The 57th Annual Meeting of Japan Society for Cell Biology  2004.5.26 

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    Venue:Senri Life Science Center  

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Awards

  • EBSA Bursary (University College London, UCL)

    2019.1   European Biophysical Societies' Association  

    Senju Yosuke

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  • Short-Term Fellowships (Heidelberg University)

    2016.12   EMBO  

    Senju Yosuke

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  • Travelling Fellowships (Heidelberg University)

    2016.10   The Company of Biologists   Journal of Cell Science

    Senju Yosuke

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  • Bilateral Joint Research Projects (University of Helsinki)

    2015.4   JSPS, Academy of Finland  

    Senju Yosuke

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Research Projects

  • アスガルド古細菌から理解する細胞膜ダイナミクスの普遍的メカニズム

    Grant number:23K05718  2023.04 - 2026.03

    日本学術振興会  Grant-in-Aid for Scientific Research (C)  基盤研究(C)

    千住 洋介

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    Authorship:Principal investigator  Grant type:Competitive

    Grant amount:\4680000 ( Direct expense: \3600000 、 Indirect expense:\1080000 )

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  • アスガルド古細菌に見出されたアクチン細胞骨格のイノシトールリン脂質による制御機構

    Grant number:20K06589  2020.04 - 2023.03

    日本学術振興会  Grant-in-Aid for Scientific Research (C)  基盤研究(C)

    千住 洋介

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    Authorship:Principal investigator  Grant type:Competitive

    Grant amount:\4420000 ( Direct expense: \3400000 、 Indirect expense:\1020000 )

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  • Institutional Program for Young Researcher Overseas Visits

    2010.12

    The University of Tokyo 

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    Authorship:Principal investigator 

    Grant amount:\350000

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  • 特別研究奨励費

    2005.04 - 2008.03

    Department of Physics,Graduate School of Science,Tohoku University  COE for "Exploring New Science by Bridging Particle-Matter Hierarchy" 

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    Authorship:Principal investigator 

    Grant amount:\880000 ( Direct expense: \880000 )

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  • Chancellor's travel grant

    2016.12

    Institute of Biotechnology, University of Helsinki 

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    Authorship:Principal investigator  Grant type:Competitive

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  • Travelling Fellowships

    2016.10

    The Company of Biologist  Journal of Cell Science 

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    Authorship:Principal investigator  Grant type:Competitive

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  • Chancellor's travel grant

    2015.12

    Institute of Biotechnology, University of Helsinki 

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    Authorship:Principal investigator  Grant type:Competitive

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  • Travel grants

    2015.08

    Bridging Nordic Imaging seminar 

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    Authorship:Principal investigator  Grant type:Competitive

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  • Chancellor's travel grant

    2014.11

    Institute of Biotechnology, University of Helsinki 

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    Authorship:Principal investigator  Grant type:Competitive

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  • Chancellor's travel grant

    2013.12

    Institute of Biotechnology, University of Helsinki 

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    Authorship:Principal investigator  Grant type:Competitive

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Media Coverage

  • ヨーロッパへの留学と国際共同研究 Internet

    United Japanese researchers Around the world  2023.11.2

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  • Actin dynamics and function Promotional material

    Mol Biol Cell.  29(6):696-697.  2018.3.15

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    Author:Other 

    Speakers at the Minisymposium on “Actin Dynamics and Function” reported recent discoveries ranging from the structure and mechanics of actin filaments, mechanisms regulating filament polymerization, depolymerization, and interaction with actin-binding proteins (ABPs) to the regulation and function of actin in the contexts of diverse cellular physiologies such as nuclear movement, phagocytosis, autophagy, secretion, and axon turning.
    Yosuke Senju (Pekka Lappalainen lab, University of Helsinki, Helsinki, Finland) reported the molecular mechanisms by which ABPs such as profilin, cofilin, Dia2, N-WASP, ezrin, and moesin interact with PI(4,5)P2-rich membranes. A combination of biochemical, biophysical, and molecular dynamics simulation approaches showed that although these ABPs interact with PI(4,5)P2-rich membranes through multivalent electrostatic interactions, they exhibit differences in the affinities and dynamics of membrane interactions. These distinct membrane-interaction kinetics correlate with specific functions of these ABPs in cytoskeletal dynamics.

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  • PKC kicks PACSIN2 out of caveolae Internet

    The Company of Biologists Ltd  J Cell Sci  J Cell Sci (2015) 128 (15): e1501.  2015.8.1

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    Author:Other 

    Caveolae-localised PACSIN2 [protein kinase C (PKC) and casein kinase substrate in neurons] contains an F-BAR domain, which sculpts membranes into tubules, and SH3 and linker domains, which mediate binding to other proteins. Drosophila PACSIN and mammalian PASCIN1 and PACSIN2 can be phosphorylated at the linker region, but the kinase responsible and the effects of the phosphorylation on membrane binding are unknown. In this issue (p. 2766), Shiro Suetsugu and colleagues conducted a detailed investigation that uncovered a mechanistic link between PKC, PACSIN2 and caveolar dynamics. They found that PACSIN2 was phosphorylated by PKC at serine 313, and that this phosphorylation was increased during hypotonic and shear stresses. Although the phosphorylation did not affect PACSIN2 dimerization or its interaction with other known binding partners, it decreased PACSIN2-mediated membrane tubulation. Caveolae tracking revealed that a long-lived caveolae fraction was decreased upon hypotonic stress, PACSIN2 knockdown, PKC activation and when membrane binding or phospho-mimetic PACSIN2 mutants were expressed. Furthermore, the authors present data suggesting that dynamin promotes the removal of phosphorylated PACSIN2 from the caveolar membrane. In summary, this study presents novel findings that support a model in which activated PKC phosphorylates PACSIN2, which disrupts its membrane association, thereby facilitating dynamin-dependent scission and increasing caveolar dynamics.

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  • F-BARタンパク質PACSIN2によるカベオラの形態形成とエンドサイトーシスの制御 Promotional material

    分生研ニュース編集委員会  分生研ニュース : 東京大学分子細胞生物学研究所広報誌  2012.7

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Academic Activities

  • workshop International contribution

    Role(s):Planning, management, etc.

    ( University of Helsinki ) 2019.6.10 - 2019.6.13

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  • BBSRC International contribution

    Role(s):Peer review

    Biotechnology and Biological Sciences Research Council  2018.3

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    Type:Peer review 

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  • Symposium International contribution

    Role(s):Planning, management, etc.

    Centre of Excellence - Academy of Finland  ( University of Helsinki ) 2017.12.17

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    Type:Competition, symposium, etc. 

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  • Hokkaido University FSP (First Step Program) International contribution

    Role(s):Planning, management, etc.

    Hokkaido University  ( Institute of Biotechnology, University of Helsinki ) 2017.9.13 - 2017.9.26

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    Type:Academic research 

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  • EMBO Practical Course Protein–lipid interactions: Advanced experimental and computational tools International contribution

    Role(s):Planning, management, etc.

    EMBO  ( University of Helsinki ) 2017.7.2 - 2017.7.9

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  • Hokkaido University FSP (First Step Program)

    Role(s):Planning, management, etc.

    Hokkaido University  ( Institute of Biotechnology, University of Helsinki ) 2016.9.6 - 2016.9.20

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    Type:Academic research 

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  • iP-U (incubation Program for innovative students at Utsunomiya University) International contribution

    Role(s):Planning, management, etc.

    Utsunomiya University  ( Institute of Biotechnology, University of Helsinki ) 2016.3.7 - 2016.3.14

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    Type:Academic research 

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  • Spring School International contribution

    Role(s):Planning, management, etc.

    Centre of Excellence - Academy of Finland  ( University of Helsinki ) 2015.5.11 - 2015.5.19

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  • Nordic Network For Dynamic Biomembrane Research International contribution

    Role(s):Panel moderator, session chair, etc.

    Nordforsk  ( Åland ) 2014.5.14 - 2014.5.16

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    Type:Academic society, research group, etc. 

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