大田原キャンパス

薬学科

教員紹介

松浦 能行

教授 松浦 能行

  • 担当科目

    <学部>
    物理学(1年)、基礎薬学実習I(物理)(1年)、薬品物理化学II(2年)、放射化学(2年)、薬学演習I(2年)、物理系薬学実習(2年)、関連職種連携ワーク(3年)、病院・薬局事前実習I(4年)、総合薬学演習II(6年)

  • 略歴

    <学歴・学位>
    東京大学理学部物理学科卒業
    東京大学大学院理学系研究科 修士(理学)
    東京大学大学院理学系研究科 博士(理学)

    <職歴>
    英国MRC Laboratory of Molecular Biology 博士研究員
    名古屋大学理学部 助手
    名古屋大学理学部 助教
    名古屋大学理学部 准教授

  • 研究分野/専門分野

    物理系薬学, 腫瘍生物学, 細胞生物学, 生物物理学, 機能生物化学, 構造生物化学

  • 研究テーマ

    ヒトの疾患(がんなど)に関する構造生物学研究

  • 研究業績

    【researchmap】
    https://researchmap.jp/read0132830



    【主な原著論文】

    1. *Matsuura, Y., Miyawaki, K., Structures of importin-α bound to the wild-type and an internal deletion mutant of the bipartite nuclear localization signal of HIF-1α. Biochem Biophys Res Commun, 652: 1-5 (2023).
    2. *Matsuura, Y. Crystallographic data of an importin-α3 dimer in which the two protomers are bridged by a bipartite nuclear localization signal. Data in Brief, 47: 108988 (2023).
    3. *Matsuura, Y. High-resolution structural analysis shows how different crystallographic environments can induce alternative modes of binding of a phosphotyrosine peptide to the SH2 domain of Fer tyrosine kinase. Protein Science, 28: 2011-2019 (2019).
    4. *Matsuura, Y. Structural and biochemical characterization of the recognition of the 53BP1 nuclear localization signal by importin-α. Biochem Biophys Res Commun, 510: 236-241 (2019).
    5. Kobayashi, J., *Matsuura, Y. Structure and dimerization of the catalytic domain of the protein phosphatase Cdc14p, a key regulator of mitotic exit in Saccharomyces cerevisiae. Protein Science, 26: 2105-2112 (2017).
    6. Koyama, M., Hirano, H., Shirai, N., *Matsuura, Y. Crystal structure of the Xpo1p nuclear export complex bound to the SxFG/PxFG repeats of the nucleoporin Nup42p. Genes Cells, 22: 861-875 (2017).
    7. Koyama, M., *Matsuura, Y. Crystal structure of importin-α3 bound to the nuclear localization signal of Ran-binding protein 3. Biochem Biophys Res Commun, 491: 609-613 (2017).
    8. Koyama, M., Sasaki, T., Sasaki, N., *Matsuura, Y. Crystal structure of human WBSCR16, an RCC1-like protein in mitochondria. Protein Science, 26: 1870-1877 (2017).
    9. Nakada, R., *Matsuura, Y. Crystal structure of importin-α bound to the nuclear localization signal of Epstein-Barr virus EBNA-LP protein. Protein Science, 26: 1231-1235 (2017).
    10. Nakada, R., Hirano, H., *Matsuura, Y. Structural basis for the regulation of nuclear import of Epstein-Barr virus nuclear antigen 1 (EBNA1) by phosphorylation of the nuclear localization signal. Biochem Biophys Res Commun, 484: 113-117 (2017).
    11. Hirano, H., Kobayashi, J., *Matsuura, Y. Structures of the karyopherins Kap121p and Kap60p bound to the nuclear pore targeting domain of the SUMO protease Ulp1p. J Mol Biol, 429: 249-260 (2017).
    12. Nakada, R., Hirano, H., *Matsuura, Y. Structure of importin-α bound to a non-classical nuclear localization signal of the influenza A virus nucleoprotein. Scientific Reports, 5: 15055 (2015).
    13. Kobayashi, J., Hirano, H., *Matsuura, Y. Crystal structure of the karyopherin Kap121p bound to the extreme C-terminus of the protein phosphatase Cdc14p. Biochem Biophys Res Commun, 463: 309-314 (2015).
    14. Koyama, M., Shirai, N., *Matsuura, Y. Structural insights into how Yrb2p accelerates the assembly of the Xpo1p nuclear export complex. Cell Reports, 9: 983-995 (2014).
    15. Kobayashi, J., *Matsuura, Y. Structural basis for cell-cycle-dependent nuclear import mediated by the karyopherin Kap121p. J Mol Biol, 425: 1852-1868 (2013).
    16. Saito, N., *Matsuura, Y. A 2.1-Å-resolution crystal structure of unliganded CRM1 reveals the mechanism of autoinhibition. J Mol Biol, 425: 350-364 (2013).
    17. Pan, D., *Matsuura, Y. Structures of the pleckstrin homology domain of Saccharomyces cerevisiae Avo1 and its human orthologue Sin1, an essential subunit of TOR complex 2. Acta Crystallogr Sect F Struct Biol Cryst Commun, 68: 386-392 (2012).
    18. Hirano, H., *Matsuura, Y. Sensing actin dynamics: structural basis for G-actin-sensitive nuclear import of MAL. Biochem Biophys Res Commun, 414: 373-378 (2011).
    19. Koyama, M., *Matsuura, Y. An allosteric mechanism to displace nuclear export cargo from CRM1 and RanGTP by RanBP1. EMBO J, 29: 2002-2013 (2010).
    20. Matsuura, Y., *Stewart, M. Nup50/Npap60 function in nuclear protein import complex disassembly and importin recycling. EMBO J, 24: 3681-3689 (2005).
    21. Lee, S.J., Matsuura, Y., Liu, S.M., *Stewart, M. Structural basis for nuclear import complex dissociation by RanGTP. Nature, 435: 693-696 (2005).
    22. Matsuura, Y., *Stewart, M. Structural basis for the assembly of a nuclear export complex. Nature, 432: 872-877 (2004).
    23. Matsuura, Y., Lange, A., Harreman, M.T., Corbett, A.H., *Stewart, M. Structural basis for Nup2p function in cargo release and karyopherin recycling in nuclear import. EMBO J, 22: 5358-5369 (2003).
    24. Matsuura, Y., Stewart, M., Kawamoto, M., Kamiya, N., Saeki, K., Yasunaga, T., *Wakabayashi, T. Structural basis for the higher Ca2+-activation of the regulated actin-activated myosin ATPase observed with Dictyostelium/Tetrahymena actin chimeras. J Mol Biol, 296: 579-595 (2000).

    【主な総説】

    1. *Matsuura, Y. Defective recognition of a nonclassical nuclear localization signal in neurodevelopmental disorders. Structure, 31: 891-892 (2023).
    2. *Matsuura, Y. Mechanistic insights from structural analyses of Ran GTPase-driven nuclear export of proteins and RNAs. J Mol Biol, 428: 2025-2039 (2016).
    3. 小山昌子、松浦能行「CRM1核外輸送複合体の形成と解体の構造基盤の解明と創薬への応用」生化学 87: 41-48 (2015).
    4. Koyama, M., *Matsuura, Y. Mechanistic insights from recent structures of the CRM1 nuclear export complex and its disassembly intermediate. Biophysics, 8: 145-150 (2012).
    5. 松浦能行「核-細胞質間高分子輸送の構造生物学」生物物理 51: 208-213 (2011).
    6. 小山昌子、松浦能行「CRM1による核外輸送機構の構造基盤」生化学 83: 834-838 (2011).
    7. 松浦能行「蛋白質核外輸送複合体のX線結晶構造解析」蛋白質 核酸 酵素 50: 420-426 (2005).
    8. 松浦能行「蛋白質複合体結晶構造が明らかにした蛋白質相互作用の多様性、巧妙性:核外輸送複合体の場合」生体の科学 56: 564-570 (2005).
    9. *Stewart, M., Baker, R.P., Bayliss, R., Clayton, L., Grant, R.P., Littlewood, T., Matsuura, Y. Molecular mechanism of translocation through nuclear pore complexes during nuclear protein import. FEBS Lett, 498: 145-149 (2001).

    【科研費】

    1. 基盤研究C 「がんシグナル分子PKM2の核移行制御機構の構造基盤」(2022~2024年度)
    2. 基盤研究C 「がんの発症と進展に寄与するシグナル分子の核移行メカニズムの構造基盤」(2019~2021年度)
  • 更新月

    2023.09