担当区分：筆頭著者   記述言語：英語   掲載種別：研究論文（学術雑誌）  

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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担当区分：筆頭著者   記述言語：英語   掲載種別：研究論文（学術雑誌）   出版者・発行元：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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担当区分：筆頭著者   記述言語：英語   掲載種別：研究論文（学術雑誌）   出版者・発行元：COMPANY OF BIOLOGISTS LTD  

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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担当区分：筆頭著者   記述言語：英語   掲載種別：研究論文（学術雑誌）  

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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記述言語：英語   掲載種別：研究論文（学術雑誌）   出版者・発行元：WILEY-BLACKWELL  

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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担当区分：筆頭著者   記述言語：英語   掲載種別：研究論文（学術雑誌）  

DOI： 10.1242/jcs.086264

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記述言語：英語   掲載種別：研究論文（学術雑誌）   出版者・発行元：ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD  

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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記述言語：英語   掲載種別：研究論文（学術雑誌）  

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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担当区分：筆頭著者,　責任著者   記述言語：英語  

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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担当区分：筆頭著者,　責任著者   記述言語：英語   掲載種別：研究論文（学術雑誌）  

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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担当区分：筆頭著者,　責任著者   記述言語：英語   掲載種別：研究論文（学術雑誌）  

DOI： 10.1016/j.bbamem.2022.184076

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記述言語：英語   掲載種別：研究論文（学術雑誌）  

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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記述言語：英語   掲載種別：研究論文（学術雑誌）  

DOI： 10.1186/s12915-022-01246-x

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担当区分：筆頭著者,　責任著者   記述言語：英語  

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

DOI： 10.3390/membranes12020181

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記述言語：英語   掲載種別：研究論文（学術雑誌）  

DOI： 10.1016/j.bbrc.2021.07.041

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記述言語：英語   掲載種別：研究論文（学術雑誌）  

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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記述言語：英語   掲載種別：研究論文（学術雑誌）   出版者・発行元：NATURE PUBLISHING GROUP  

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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その他リンク： http://www.nature.com/articles/s41598-017-08259-5

記述言語：英語   掲載種別：研究論文（学術雑誌）   出版者・発行元：CELL PRESS  

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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記述言語：英語   掲載種別：研究論文（学術雑誌）   出版者・発行元：NATURE PUBLISHING GROUP  

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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記述言語：英語   掲載種別：研究論文（学術雑誌）   出版者・発行元：CELL PRESS  

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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記述言語：英語   掲載種別：研究論文（学術雑誌）  

DOI： 10.1038/ncomms5994

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記述言語：英語   掲載種別：研究論文（学術雑誌）  

DOI： 10.1371/journal.pone.0060528

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担当区分：筆頭著者,　責任著者   記述言語：英語   掲載種別：研究論文（学術雑誌）  

DOI： 10.1093/jb/mvn151

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担当区分：筆頭著者   記述言語：日本語   掲載種別：記事・総説・解説・論説等（大学・研究所紀要）   出版者・発行元：分生研ニュース編集委員会  

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担当区分：筆頭著者   記述言語：英語   掲載種別：記事・総説・解説・論説等（大学・研究所紀要）  

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担当区分：筆頭著者   記述言語：日本語  

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記述言語：英語   会議種別：口頭発表（招待・特別）  

開催地：University of Nice Sophia Antipolis  

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記述言語：英語   会議種別：ポスター発表  

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記述言語：英語   会議種別：ポスター発表  

開催地：Denver, CO  

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記述言語：日本語   会議種別：ポスター発表  

開催地：東京大学本郷キャンパス  

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記述言語：日本語   会議種別：ポスター発表  

開催地：東京大学本郷キャンパス  

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開催年月日： 2020年2月20日 - 2020年2月21日

記述言語：英語   会議種別：ポスター発表  

開催地：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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記述言語：英語   会議種別：公開講演，セミナー，チュートリアル，講習，講義等  

開催地：岡山大学異分野融合先端研究コア  

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記述言語：英語   会議種別：口頭発表（招待・特別）  

開催地：Tallinn, Estonia  

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記述言語：英語   会議種別：ポスター発表  

開催地：ヘルシンキ大学バイオテクノロジー研究所  

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記述言語：英語   会議種別：ポスター発表  

開催地：Turku Centre for Biotechnology  

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記述言語：英語   会議種別：ポスター発表  

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記述言語：英語   会議種別：公開講演，セミナー，チュートリアル，講習，講義等  

開催地：〒630-0192 奈良県生駒市高山町8916番地の5  

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記述言語：英語   会議種別：ポスター発表  

開催地：ヘルシンキ大学バイオテクノロジー研究所  

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記述言語：英語   会議種別：口頭発表（一般）  

開催地：ヘルシンキ大学バイオテクノロジー研究所  

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記述言語：英語   会議種別：ポスター発表  

開催地：Philadelphia, USA  

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記述言語：英語   会議種別：ポスター発表  

開催地：ヘルシンキ, フィンランド  

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記述言語：英語   会議種別：口頭発表（招待・特別）  

開催地：University of Helsinki  

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記述言語：英語   会議種別：ポスター発表  

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

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記述言語：英語   会議種別：ポスター発表  

開催地：Lammi, Finland  

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記述言語：英語   会議種別：ポスター発表  

開催地：University of Helsinki  

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記述言語：英語   会議種別：ポスター発表  

開催地：Turku, Finland  

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記述言語：英語   会議種別：口頭発表（招待・特別）  

開催地：Lammi, Finland  

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記述言語：英語   会議種別：口頭発表（招待・特別）  

開催地：Tampere University of Technology  

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記述言語：英語   会議種別：ポスター発表  

開催地：Roscoff, France  

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記述言語：英語   会議種別：口頭発表（招待・特別）  

開催地：Åland Islands  

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記述言語：英語   会議種別：ポスター発表  

開催地：Lammi, Finland  

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記述言語：英語   会議種別：ポスター発表  

開催地：University of Helsinki  

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記述言語：英語   会議種別：ポスター発表  

開催地：New Orleans, LA  

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記述言語：英語   会議種別：口頭発表（招待・特別）  

開催地：Skokloster, Sweden  

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記述言語：英語   会議種別：口頭発表（一般）  

開催地：Hokkaido University  

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記述言語：英語   会議種別：ポスター発表  

開催地：Philadelphia, PA  

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記述言語：英語   会議種別：口頭発表（一般）  

開催地：東北大学川内キャンパス  

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記述言語：英語   会議種別：ポスター発表  

開催地：パシフィコ横浜  

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記述言語：英語   会議種別：ポスター発表  

開催地：Sendai, Japan  

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記述言語：英語   会議種別：ポスター発表  

開催地：Sendai International Center, Sendai, Japan  

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記述言語：日本語   会議種別：ポスター発表  

開催地：仙台国際センター,  

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記述言語：英語   会議種別：ポスター発表  

開催地：Fukuoka Convention Center  

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記述言語：英語   会議種別：ポスター発表  

開催地：Sendai, Japan  

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記述言語：英語   会議種別：ポスター発表  

開催地：Okinawa, Japan  

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記述言語：英語   会議種別：ポスター発表  

開催地：Kyoto, Japan  

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記述言語：日本語   会議種別：ポスター発表  

開催地：仙台国際センター  

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記述言語：英語   会議種別：ポスター発表  

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記述言語：英語   会議種別：ポスター発表  

開催地：札幌コンベンショ ンセンター,  

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記述言語：日本語   会議種別：口頭発表（一般）  

開催地：東北大学  

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記述言語：英語   会議種別：ポスター発表  

開催地：Omiya Sonic City  

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記述言語：日本語   会議種別：ポスター発表  

開催地：国立京都国際会館  

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記述言語：英語   会議種別：ポスター発表  

開催地：Senri Life Science Center  

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種別：学術調査 

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種別：学術調査 

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種別：学会・研究会等 

座長

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