2021/12/24 更新

写真a

タケダ シュウイチ
武田 修一
TAKEDA SHUICHI
所属
異分野基礎科学研究所 助教(特任)
職名
助教(特任)
連絡先
メールアドレス
外部リンク

学位

  • 博士(理学) ( 2010年11月   名古屋大学 )

  • キャッピング蛋白質によるアクチン線維B端キャッピング活性の調節機序 ( 2010年11月   名古屋大学 )

研究分野

  • ライフサイエンス / 構造生物化学

経歴

  • 名古屋大学 大学院理学研究科 附属構造生物学研究センター 名古屋大学大学院理学研究科附属構造生物学研究センター   その他

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所属学協会

  • 日本細胞生物学会

  • 日本結晶学会

  • 日本生物物理学会

 

論文

  • Structural Insights into the Regulation of Actin Capping Protein by Twinfilin C-terminal Tail. 国際誌

    Shuichi Takeda, Ryotaro Koike, Ikuko Fujiwara, Akihiro Narita, Makoto Miyata, Motonori Ota, Yuichiro Maéda

    Journal of molecular biology   433 ( 9 )   166891 - 166891   2021年4月

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    記述言語:英語   掲載種別:研究論文(学術雑誌)  

    Twinfilin is a conserved actin regulator that interacts with actin capping protein (CP) via C terminus residues (TWtail) that exhibits sequence similarity with the CP interaction (CPI) motif of CARMIL. Here we report the crystal structure of TWtail in complex with CP. Our structure showed that although TWtail and CARMIL CPI bind CP to an overlapping surface via their middle regions, they exhibit different CP-binding modes at both termini. Consequently, TWtail and CARMIL CPI restrict the CP in distinct conformations of open and closed forms, respectively. Interestingly, V-1, which targets CP away from the TWtail binding site, also favors the open-form CP. Consistently, TWtail forms a stable ternary complex with CP and V-1, a striking contrast to CARMIL CPI, which rapidly dissociates V-1 from CP. Our results demonstrate that TWtail is a unique CP-binding motif that regulates CP in a manner distinct from CARMIL CPI.

    DOI: 10.1016/j.jmb.2021.166891

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  • Crystal structure of human V-1 in the apo form. 国際誌

    Shuichi Takeda, Ryotaro Koike, Takayuki Nagae, Ikuko Fujiwara, Akihiro Narita, Yuichiro Maéda, Motonori Ota

    Acta crystallographica. Section F, Structural biology communications   77 ( Pt 1 )   13 - 21   2021年1月

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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:International Union of Crystallography ({IUCr})  

    V-1, also known as myotrophin, is a 13 kDa ankyrin-repeat protein that binds and inhibits the heterodimeric actin capping protein (CP), which is a key regulator of cytoskeletal actin dynamics. The crystal structure of V-1 in complex with CP revealed that V-1 recognizes CP via residues spanning several ankyrin repeats. Here, the crystal structure of human V-1 is reported in the absence of the specific ligand at 2.3 Å resolution. In the asymmetric unit, the crystal contains two V-1 monomers that exhibit nearly identical structures (Cα r.m.s.d. of 0.47 Å). The overall structures of the two apo V-1 chains are also highly similar to that of CP-bound V-1 (Cα r.m.s.d.s of <0.50 Å), indicating that CP does not induce a large conformational change in V-1. Detailed structural comparisons using the computational program All Atom Motion Tree revealed that CP binding can be accomplished by minor side-chain rearrangements of several residues. These findings are consistent with the known biological role of V-1, in which it globally inhibits CP in the cytoplasm.

    DOI: 10.1107/S2053230X20016829

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  • Novel inter-domain Ca2+-binding site in the gelsolin superfamily protein fragmin. 国際誌

    Shuichi Takeda, Ikuko Fujiwara, Yasunobu Sugimoto, Toshiro Oda, Akihiro Narita, Yuichiro Maéda

    Journal of muscle research and cell motility   41 ( 1 )   153 - 162   2020年3月

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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:Springer Science and Business Media {LLC}  

    Gelsolin superfamily proteins, consisting of multiple domains (usually six), sever actin filaments and cap the barbed ends in a Ca2+-dependent manner. Two types of evolutionally conserved Ca2+-binding sites have been identified in this family; type-1 (between gelsolin and actin) and type-2 (within the gelsolin domain). Fragmin, a member in the slime mold Physarum polycephalum, consists of three domains (F1-F3) that are highly similar to the N-terminal half of mammalian gelsolin (G1-G3). Despite their similarities, the two proteins exhibit a significant difference in the Ca2+ dependency; F1-F3 absolutely requires Ca2+ for the filament severing whereas G1-G3 does not. In this study, we examined the strong dependency of fragmin on Ca2+ using biochemical and structural approaches. Our co-sedimentation assay demonstrated that Ca2+ significantly enhanced the binding of F2-F3 to actin. We determined the crystal structure of F2-F3 in the presence of Ca2+. F2-F3 binds a total of three calcium ions; while two are located in type-2 sites within F2 or F3, the remaining one resides between the F2 long helix and the F3 short helix. The inter-domain Ca2+-coordination appears to stabilize F2-F3 in a closely packed configuration. Notably, the F3 long helix exhibits a bent conformation which is different from the straight G3 long helix in the presence of Ca2+. Our results provide the first structural evidence for the existence of an unconventional Ca2+-binding site in the gelsolin superfamily proteins.

    DOI: 10.1007/s10974-019-09571-5

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  • Structural Polymorphism of Actin. 国際誌

    Toshiro Oda, Shuichi Takeda, Akihiro Narita, Yuichiro Maéda

    Journal of molecular biology   431 ( 17 )   3217 - 3228   2019年8月

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    記述言語:英語   掲載種別:研究論文(学術雑誌)  

    Information on the structural polymorphism of a protein is essential to understand the mechanisms of how it functions at an atomic level. Numerous studies on actin have accumulated substantial amounts of information about its polymorphism, and there are over 200 published atomic structures of different forms of actin using crystallography, fiber diffraction, and electron microscopy. To characterize all the reported structures, we proposed simple parameters based on the discrete rigid bodies within the actin molecule and identified four conformation groups by cluster analysis: the F-form in naked F-actin, the C-form in cofilactin, the O-form in profilin-actin, and the G-form in the majority of actin-containing crystal structures. The G-form group included the most variations, but each conformational variation was convertible via a thermal fluctuation, whereas the F- and C-forms were not accessible from the G-form. The convertibility and accessibility of the structures were evaluated using molecular dynamics simulations. Information about conformational conversion among each group is useful for understanding the mechanisms of actin function.

    DOI: 10.1016/j.jmb.2019.05.048

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  • Polymerization and depolymerization of actin with nucleotide states at filament ends. 国際誌

    Ikuko Fujiwara, Shuichi Takeda, Toshiro Oda, Hajime Honda, Akihiro Narita, Yuichiro Maéda

    Biophysical reviews   10 ( 6 )   1513 - 1519   2018年12月

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    記述言語:英語   掲載種別:研究論文(学術雑誌)  

    Polymerization induces hydrolysis of ATP bound to actin, followed by γ-phosphate release, which helps advance the disassembly of actin filaments into ADP-G-actin. Mechanical understanding of this correlation between actin assembly and ATP hydrolysis has been an object of intensive studies in biochemistry and structural biology for many decades. Although actin polymerization and depolymerization occur only at either the barbed or pointed ends and the kinetic and equilibrium properties are substantially different from each other, characterizing their properties is difficult to do by bulk assays, as these assays report the average of all actin filaments in solution and are therefore not able to discern the properties of individual actin filaments. Biochemical studies of actin polymerization and hydrolysis were hampered by these inherent properties of actin filaments. Total internal reflection fluorescence (TIRF) microscopy overcame this problem by observing single actin filaments. With TIRF, we now know not only that each end has distinct properties, but also that the rate of γ-phosphate release is much faster from the terminals than from the interior of actin filaments. The rate of γ-phosphate release from actin filament ends is even more accelerated when latrunculin A is bound. These findings highlight the importance of resolving structural differences between actin molecules in the interior of the filament and those at either filament end. This review provides a history of observing actin filaments under light microscopy, an overview of dynamic properties of ATP hydrolysis at the end of actin filament, and structural views of γ-phosphate release.

    DOI: 10.1007/s12551-018-0483-7

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  • Structural basis for cofilin binding and actin filament disassembly. 国際誌

    Kotaro Tanaka, Shuichi Takeda, Kaoru Mitsuoka, Toshiro Oda, Chieko Kimura-Sakiyama, Yuichiro Maéda, Akihiro Narita

    Nature communications   9 ( 1 )   1860 - 1860   2018年5月

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    記述言語:英語   掲載種別:研究論文(学術雑誌)  

    Actin depolymerizing factor (ADF) and cofilin accelerate actin dynamics by severing and disassembling actin filaments. Here, we present the 3.8 Å resolution cryo-EM structure of cofilactin (cofilin-decorated actin filament). The actin subunit structure of cofilactin (C-form) is distinct from those of F-actin (F-form) and monomeric actin (G-form). During the transition between these three conformations, the inner domain of actin (subdomains 3 and 4) and the majority of subdomain 1 move as two separate rigid bodies. The cofilin-actin interface consists of three distinct parts. Based on the rigid body movements of actin and the three cofilin-actin interfaces, we propose models for the cooperative binding of cofilin to actin, preferential binding of cofilin to ADP-bound actin filaments and cofilin-mediated severing of actin filaments.

    DOI: 10.1038/s41467-018-04290-w

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  • Comprehensive analysis of motions in molecular dynamics trajectories of the actin capping protein and its inhibitor complexes. 国際誌

    Ryotaro Koike, Shuichi Takeda, Yuichiro Maéda, Motonori Ota

    Proteins   84 ( 7 )   948 - 56   2016年7月

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    記述言語:英語   掲載種別:研究論文(学術雑誌)  

    The actin capping protein (CP) binds to actin filaments to block further elongation. The capping activity is inhibited by proteins V-1 and CARMIL interacting with CP via steric and allosteric mechanisms, respectively. The crystal structures of free CP, CP/V-1, and CP/CARMIL complexes suggest that the binding of CARMIL alters the flexibility of CP rather than the overall structure of CP, and this is an allosteric inhibition mechanism. Here, we performed molecular dynamics (MD) simulations of CP in the free form, and in complex with CARMIL or V-1. The resulting trajectories were analyzed exhaustively using Motion Tree, which identifies various rigid-body motions ranging from small local motions to large domain motions. After enumerating all the motions, CP flexibilities with different ligands were characterized by a list of frequencies for 20 dominant rigid-body motions, some of which were not identified in previous studies. The comparative analysis highlights the influence of the binding of the CARMIL peptide to CP flexibility. In free CP and the CP/V-1 complex, domain motions around a large crevice between the N-stalk and the CP-S domain occur frequently. The CARMIL peptide binds the crevice and suppresses the motions effectively. In addition, the binding of the CARMIL peptide enhances and alters local motions around the pocket that participates in V-1 binding. These newly identified motions are likely to suppress the binding of V-1 to CP. The observed changes in CP motion provide insights that describe the mechanism of allosteric regulation by CARMIL through modulating CP flexibility. Proteins 2016; 84:948-956. © 2016 Wiley Periodicals, Inc.

    DOI: 10.1002/prot.25043

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  • Effects of lipid composition and solution conditions on the mechanical properties of membrane vesicles. 国際誌

    Nobuhiko Kato, Akihiko Ishijima, Takehiko Inaba, Fumimasa Nomura, Shuichi Takeda, Kingo Takiguchi

    Membranes   5 ( 1 )   22 - 47   2015年1月

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    記述言語:英語   掲載種別:研究論文(学術雑誌)  

    The mechanical properties of cell-sized giant unilamellar liposomes were studied by manipulating polystyrene beads encapsulated within the liposomes using double-beam laser tweezers. Mechanical forces were applied to the liposomes from within by moving the beads away from each other, which caused the liposomes to elongate. Subsequently, a tubular membrane projection was generated in the tip at either end of the liposome, or the bead moved out from the laser trap. The force required for liposome transformation reached maximum strength just before formation of the projection or the moving out of the bead. By employing this manipulation system, we investigated the effects of membrane lipid compositions and environment solutions on the mechanical properties. With increasing content of acidic phospholipids, such as phosphatidylglycerol or phosphatidic acid, a larger strength of force was required for the liposome transformation. Liposomes prepared with a synthetic dimyristoylphosphatidylcholine, which has uniform hydrocarbon chains, were transformed easily compared with liposomes prepared using natural phosphatidylcholine. Surprisingly, bovine serum albumin or fetuin (soluble proteins that do not bind to membranes) decreased liposomal membrane rigidity, whereas the same concentration of sucrose showed no particular effect. These results show that the mechanical properties of liposomes depend on their lipid composition and environment.

    DOI: 10.3390/membranes5010022

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  • Actin capping protein and its inhibitor CARMIL: how intrinsically disordered regions function. 国際誌

    Shuichi Takeda, Ryotaro Koike, Yasushi Nitanai, Shiho Minakata, Yuichiro Maéda, Motonori Ota

    Physical biology   8 ( 3 )   035005 - 035005   2011年6月

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    記述言語:英語   掲載種別:研究論文(学術雑誌)  

    The actin capping protein (CP) tightly binds to the barbed end of actin filaments to block further elongation. The β-tentacle in CP is an important region that ensures stable interaction with actin filaments. CARMIL inhibits the interaction of CP with actin filaments via the C-terminal portion containing the CP-binding motif, located in an intrinsically disordered region. We have proposed an allosteric inhibition model in which CARMIL suppresses CP by the population shift mechanism. Here, we solved a crystal structure of CP in complex with a CARMIL-derived peptide, CA32. The new structure clearly represents the α-helical form of the β-tentacle that was invisible in other CP/CARMIL peptide complex structures. In addition, we exhaustively performed a normal mode analysis with the elastic network model on all available crystal structures of the CP/CARMIL peptide complexes, including the new structure. We concluded that the CP-binding motif is necessary and sufficient for altering the fluctuation of CP, which is essential for attenuating the barbed-end-capping activity along the population shift mechanism. The roles and functions of the β-tentacle and the CP-binding motif are discussed in terms of their intrinsically disordered nature.

    DOI: 10.1088/1478-3975/8/3/035005

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  • Electron microscopic visualization of the filament binding mode of actin-binding proteins. 国際誌

    Takuto Ito, Tasuku Hirayama, Masayasu Taki, Shohei Iyoshi, Shuheng Dai, Shuichi Takeda, Chieko Kimura-Sakiyama, Toshiro Oda, Yukio Yamamoto, Yuichiro Maéda, Akihiro Narita

    Journal of molecular biology   408 ( 1 )   26 - 39   2011年4月

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    記述言語:英語   掲載種別:研究論文(学術雑誌)  

    A large number of actin-binding proteins (ABPs) regulate various kinds of cellular events in which the superstructure of the actin cytoskeleton is dynamically changed. Thus, to understand the actin dynamics in the cell, the mechanisms of actin regulation by ABPs must be elucidated. Moreover, it is particularly important to identify the side, barbed-end or pointed-end ABP binding sites on the actin filament. However, a simple, reliable method to determine the ABP binding sites on the actin filament is missing. Here, a novel electron microscopic method for determining the ABP binding sites is presented. This approach uses a gold nanoparticle that recognizes a histidine tag on an ABP and an image analysis procedure that can determine the polarity of the actin filament. This method will facilitate future study of ABPs.

    DOI: 10.1016/j.jmb.2011.01.054

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  • Two distinct mechanisms for actin capping protein regulation--steric and allosteric inhibition. 国際誌

    Shuichi Takeda, Shiho Minakata, Ryotaro Koike, Ichiro Kawahata, Akihiro Narita, Masashi Kitazawa, Motonori Ota, Tohru Yamakuni, Yuichiro Maéda, Yasushi Nitanai

    PLoS biology   8 ( 7 )   e1000416   2010年7月

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    記述言語:英語   掲載種別:研究論文(学術雑誌)  

    The actin capping protein (CP) tightly binds to the barbed end of actin filaments, thus playing a key role in actin-based lamellipodial dynamics. V-1 and CARMIL proteins directly bind to CP and inhibit the filament capping activity of CP. V-1 completely inhibits CP from interacting with the barbed end, whereas CARMIL proteins act on the barbed end-bound CP and facilitate its dissociation from the filament (called uncapping activity). Previous studies have revealed the striking functional differences between the two regulators. However, the molecular mechanisms describing how these proteins inhibit CP remains poorly understood. Here we present the crystal structures of CP complexed with V-1 and with peptides derived from the CP-binding motif of CARMIL proteins (CARMIL, CD2AP, and CKIP-1). V-1 directly interacts with the primary actin binding surface of CP, the C-terminal region of the alpha-subunit. Unexpectedly, the structures clearly revealed the conformational flexibility of CP, which can be attributed to a twisting movement between the two domains. CARMIL peptides in an extended conformation interact simultaneously with the two CP domains. In contrast to V-1, the peptides do not directly compete with the barbed end for the binding surface on CP. Biochemical assays revealed that the peptides suppress the interaction between CP and V-1, despite the two inhibitors not competing for the same binding site on CP. Furthermore, a computational analysis using the elastic network model indicates that the interaction of the peptides alters the intrinsic fluctuations of CP. Our results demonstrate that V-1 completely sequesters CP from the barbed end by simple steric hindrance. By contrast, CARMIL proteins allosterically inhibit CP, which appears to be a prerequisite for the uncapping activity. Our data suggest that CARMIL proteins down-regulate CP by affecting its conformational dynamics. This conceptually new mechanism of CP inhibition provides a structural basis for the regulation of the barbed end elongation in cells.

    DOI: 10.1371/journal.pbio.1000416

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  • Structural basis of actin filament capping at the barbed-end: a cryo-electron microscopy study. 国際誌

    Akihiro Narita, Shuichi Takeda, Atsuko Yamashita, Yuichiro Maéda

    The EMBO journal   25 ( 23 )   5626 - 33   2006年11月

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    記述言語:英語   掲載種別:研究論文(学術雑誌)  

    The intracellular distribution and migration of many protein complexes and organelles is regulated by the dynamics of the actin filament. Many actin filament end-binding proteins play crucial roles in actin dynamics, since polymerization and depolymerization of actin protomers occur only at the filament ends. We present here an EM structure of the complex of the actin filament and hetero-dimeric capping protein (CP) bound to the barbed-end at 23 A resolution, by applying a newly developed methods of image analysis to cryo-electron micrographs. This structure was fitted by the crystal structure of CP and the proposed actin filament structure, allowing us to construct a model that depicts two major binding regions between CP and the barbed-end. This binding scheme accounted for the results of newly performed and previously published mutation experiments, and led us to propose a two-step binding model. This is the first determination of an actin filament end structure.

    DOI: 10.1038/sj.emboj.7601395

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  • Opening of holes in liposomal membranes is induced by proteins possessing the FERM domain. 国際誌

    Shuichi Takeda, Akihiko Saitoh, Mayumi Furuta, Nao Satomi, Atsushi Ishino, Gakushi Nishida, Hiroaki Sudo, Hirokazu Hotani, Kingo Takiguchi

    Journal of molecular biology   362 ( 3 )   403 - 13   2006年9月

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    記述言語:英語   掲載種別:研究論文(学術雑誌)  

    The destabilization of vesicles caused by interactions between lipid bilayers and proteins was studied by direct, real-time observation using high-intensity dark-field microscopy. We previously reported that talin, a cytoskeletal submembranous protein, can reversibly open stable large holes in giant liposomes made of neutral and acidic phospholipids. Talin and other proteins belonging to the band 4.1 superfamily have the FERM domain at their N-terminal and interact with lipid membranes via that domain. Here, we observed that band 4.1, ezrin and moesin, members of the band 4.1 superfamily, are also able to open stable holes in liposomes. However, truncation of their C-terminal domains, which can interact with the N-terminal FERM domain, impaired their hole opening activities. Oligomeric states of ezrin affected the capability of the membrane hole formation. Phosphatidylinositol bisphosphate (PIP2), which binds to the FERM domain and disrupts the interaction between the N and C termini of the band 4.1 superfamily, down-regulates their membrane opening activity. These results suggest that the intermolecular interaction plays a key role in the observed membrane hole formation.

    DOI: 10.1016/j.jmb.2006.07.071

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  • Mechanical analyses of morphological and topological transformation of liposomes 査読

    Hirokazu Hotani, Takehiko Inaba, Fumimasa Nomura, Shuichi Takeda, Kingo Takiguchi, Tomohiko J. ltoh, Tamiki Umeda, Akihiko Ishijima

    Biosystems   71   93 - 100   2003年

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    記述言語:英語   掲載種別:研究論文(学術雑誌)  

  • Liposomes possess drastic capabilities for topological transformation. 国際誌

    Kingo Takiguchi, Fumimasa Nomura, Takehiko Inaba, Shuichi Takeda, Akihiko Saitoh, Hirokazu Hotani

    Chemphyschem : a European journal of chemical physics and physical chemistry   3 ( 7 )   571 - 4   2002年7月

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    記述言語:英語   掲載種別:研究論文(学術雑誌)  

    Morphological and topological changes of biological membranes play essential roles in cellular activities. It has been thought that these transformations are made possible through interactions with proteins. However, direct observation of giant liposomes by optical dark-field microscopy reveals that the lipid bilayer itself possesses the ability to undergo topological transformation.

    DOI: 10.1002/1439-7641(20020715)3:7<571::AID-CPHC571>3.0.CO;2-A

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  • Morphological and topological transformation of membrane vesicles

    Nomura, F., Honda, M., Takeda, S., Inaba, T., Takiguchi, K., Itoh, T.J., Ishijima, A., Umeda, T., Hotani, H.

    Journal of Biological Physics   28 ( 2 )   2002年

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    DOI: 10.1023/A:1019971429702

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  • Dynamic transformation of liposomes revealed by dark-field microscopy

    Nomura, F., Honda, M., Takeda, S., Takiguchi, K., Hotani, H.

    Studies in Surface Science and Catalysis   132   2001年

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    掲載種別:研究論文(学術雑誌)   出版者・発行元:Studies in Surface Science and Catalysis  

    DOI: 10.1016/s0167-2991(01)82138-8

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▼全件表示

MISC

  • F型アクチンのATP加水分解反応機構の理論解析

    兼松佑典, 武田修一, 小池亮太郎, 太田元規, 鷹野優, 前田雄一郎

    生体分子科学討論会講演要旨集   47th   2021年

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  • アクチン・フィラメント:原子分解能の構造解明で始まる世界

    武田修一, 兼松佑典, 成田哲博, 田中康太郎, 小池亮太郎, 太田元規, 鷹野優, 森次圭, 藤原郁子, 渡邉信久, 永江峰幸, 小田俊郎, 前田雄一郎, 前田雄一郎

    日本物理学会講演概要集(CD-ROM)   75 ( 1 )   2020年

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  • ラトランキュリンAはF型からG型へのコンフォメーション変化を誘起しアクチン脱重合を促進する

    武田修一, 藤原郁子, 小田俊郎, 成田哲博, 前田雄一郎

    日本結晶学会年会講演要旨集   2019   2019年

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  • 高分解能X線結晶構造から明らかとなったアクチン重合・ATP加水分解機構

    武田修一, 成田哲博, 小田俊郎, 田中康太郎, 小池亮太郎, 太田元規, 藤原郁子, 渡邉信久, 渡邉信久, 前田雄一郎

    日本結晶学会年会講演要旨集   2017   2017年

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  • 動的構造に着目したCARMIL蛋白質によるキャップ蛋白質の機能阻害メカニズムの解明

    小池亮太郎, 武田修一, 前田雄一郎, 太田元規

    日本蛋白質科学会年会プログラム・要旨集   15th   2015年

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  • 架橋型シクロヘキセニル核酸の機能性評価及び構造解析

    百相義大, 武田修一, 松本友治, 廣明秀一, 廣明秀一, 小比賀聡, 小比賀聡, 兒玉哲也

    日本薬学会年会要旨集(CD-ROM)   135th   2015年

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  • 架橋型シクロヘキセニル核酸の構造解析及び機能性評価

    百相義大, 武田修一, 松本友治, 廣明秀一, 廣明秀一, 廣明秀一, 小比賀聡, 小比賀聡, 兒玉哲也, 兒玉哲也

    アンチセンスシンポジウム講演要旨集   24th   2014年

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  • CARMIL蛋白質の天然変性領域によるアロステリックなキャップ蛋白質の機能制御

    小池亮太郎, 武田修一, 前田雄一郎, 太田元規

    日本蛋白質科学会年会プログラム・要旨集   13th   2013年

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  • ホスファチジル4,5-イノシトール-二リン酸によるアクチンキャッピング蛋白質の活性阻害機構の解明

    加藤文香, 宮ノ入洋平, 甲斐荘正恒, 甲斐荘正恒, 前田雄一郎, 武田修一

    日本分子生物学会年会プログラム・要旨集(Web)   35th   2012年

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  • 分子動力学法によるcapping protein(CP)の動的構造の解析

    小池亮太郎, 武田修一, 前田雄一郎, 太田元規

    日本蛋白質科学会年会プログラム・要旨集   12th   2012年

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講演・口頭発表等

  • ツインフィリン C末端尾部によるアクチンキャッピングタンパク質制御機構

    1. 武田 修一, 小池 亮太郎, 藤原 郁子, 成田 哲博, 宮田 真人, 太田元規, 前田 雄一郎

    令和3年度日本結晶学会年会  日本結晶学会

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    開催年月日: 2021年11月19日 - 2021年11月21日

    記述言語:日本語   会議種別:ポスター発表  

    開催地:北海道大学 (北海道札幌市)   国名:日本国  

共同研究・競争的資金等の研究

  • 時分割X線結晶構造解析によるアクチンATP加水分解反応の活写

    研究課題/領域番号:20K06522  2020年04月 - 現在

    日本学術振興会  科学研究費助成事業 基盤研究(C) 

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    担当区分:研究代表者  資金種別:競争的資金

    配分額:4420000円 ( 直接経費:3400000円 、 間接経費:1020000円 )

  • 時分割X線結晶構造解析によるアクチンATP加水分解反応の活写

    研究課題/領域番号:20K06522  2020年04月 - 2023年03月

    日本学術振興会  科学研究費助成事業 基盤研究(C)  基盤研究(C)

    武田 修一

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    配分額:4420000円 ( 直接経費:3400000円 、 間接経費:1020000円 )

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  • ゲルゾリン様タンパク質によるアクチン繊維切断機構の解明

    研究課題/領域番号:17K07373  2017年04月 - 2020年03月

    日本学術振興会  科学研究費助成事業   基盤研究(C)

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    担当区分:研究分担者  資金種別:競争的資金

    配分額:4940000円 ( 直接経費:3800000円 、 間接経費:1140000円 )

  • ゲルゾリン様タンパク質によるアクチン繊維切断機構の解明

    研究課題/領域番号:17K07373  2017年04月 - 2020年03月

    日本学術振興会  科学研究費助成事業 基盤研究(C)  基盤研究(C)

    小田 俊郎, 藤原 郁子, 武田 修一

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    配分額:4940000円 ( 直接経費:3800000円 、 間接経費:1140000円 )

    アクチンは、単量体と線維状重合体の2状態を転移しながら、多様な基本的な生命機能を担っている。本研究では、このアクチンがどのように機能するか、例えば、線維切断や線維同士の結合を構造レベルで解明するために、アクチン分子がとり得る構造空間を明らかにし、その空間に4つの代表的なコンフォメーション(G型、F型、C型、O型)が存在すること、そのコンフォメーション間の転移を議論した。また、線維状重合体を切断して制御するフラグミンの構造を解明した。

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  • F型アクチン結晶構造から解き明かすアクチン重合・ATP加水分解・繊維切断機構

    研究課題/領域番号:16K14708  2016年04月 - 2019年03月

    日本学術振興会  科学研究費助成事業  挑戦的萌芽研究

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    担当区分:研究代表者  資金種別:競争的資金

    配分額:3770000円 ( 直接経費:290000円 、 間接経費:870000円 )

  • F型アクチン結晶構造から解き明かすアクチン重合・ATP加水分解・繊維切断機構

    研究課題/領域番号:16K14708  2016年04月 - 2019年03月

    日本学術振興会  科学研究費助成事業 挑戦的萌芽研究  挑戦的萌芽研究

    武田 修一

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    配分額:3770000円 ( 直接経費:2900000円 、 間接経費:870000円 )

    繊維状に配置したアクチン四分子がゲルゾリンファミリータンパク質の一種であるフラグミンの全長タンパク質二分子によって固定された複合体の結晶構造を、2.3オングストローム分解能で決定した。AMPPNP, ADP-Pi, ADPが結合した繊維型コンフォメーションアクチン一分子とフラグミンのN末端側ドメインとの複合体結晶構造を1.2オングストローム分解能で決定した。これらのF型アクチン構造からアクチン繊維形成、ATP加水分解機構を原子分解能で議論することが可能となった。

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  • アクチン伸長端調節因子の協同作用による新規細胞骨格ターンオーバー制御機構の解明

    研究課題/領域番号:25650064  2013年04月 - 2016年03月

    日本学術振興会  科学研究費助成事業 挑戦的萌芽研究  挑戦的萌芽研究

    武田 修一, 成田 哲博

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    配分額:4030000円 ( 直接経費:3100000円 、 間接経費:930000円 )

    アクチンは、細胞運動の駆動力を産むタンパク質で、細胞内において単量体型と、それらが集まってできるアクチン繊維の二つの状態間をダイナミックに遷移している。アクチンキャッピングタンパク質(CP)は、アクチン繊維の端に強固に結合することで、その離散集合を阻害するため、細胞運動制御の重要な因子として知られている。本研究では、おもにX線結晶解析法という手法を用いて、CPのアクチン繊維への結合能を阻害する様々なタンパクとCPとの相互作用様式を明らかにした。その結果、細胞内にはCPを介してアクチン繊維の量を巧妙にコントロールする仕組みがあることが示唆された。

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  • アクチン伸長端調節因子の協同作用による新規細胞骨格ターンオーバー制御機構の解明

    研究課題/領域番号:25650064 

    日本学術振興会  科学研究費助成事業  挑戦的萌芽研究

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    担当区分:研究代表者  資金種別:競争的資金

    配分額:4030000円 ( 直接経費:3100000円 、 間接経費:930000円 )

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