横川 真梨子 (ヨコガワ マリコ)

Yokogawa, Mariko

写真a

所属(所属キャンパス)

薬学部 薬科学科 生命機能物理学講座 (芝共立)

職名

専任講師

外部リンク

学位 【 表示 / 非表示

  • 博士(薬学), 東京大学, 課程

免許・資格 【 表示 / 非表示

  • 薬剤師免許

 

研究分野 【 表示 / 非表示

  • 物理系薬学

  • 構造生物化学

研究キーワード 【 表示 / 非表示

  • NMR

  • イオンチャネル

  • 構造生物学

  • 膜タンパク質

 

論文 【 表示 / 非表示

  • Structural mechanism underlying G protein family-specific regulation of G protein-gated inwardly rectifying potassium channel

    Kano H., Toyama Y., Imai S., Iwahashi Y., Mase Y., Yokogawa M., Osawa M., Shimada I.

    Nature Communications (Nature Communications)  10 ( 1 )  2019年12月

     概要を見る

    © 2019, The Author(s). G protein-gated inwardly rectifying potassium channel (GIRK) plays a key role in regulating neurotransmission. GIRK is opened by the direct binding of the G protein βγ subunit (Gβγ), which is released from the heterotrimeric G protein (Gαβγ) upon the activation of G protein-coupled receptors (GPCRs). GIRK contributes to precise cellular responses by specifically and efficiently responding to the Gi/o-coupled GPCRs. However, the detailed mechanisms underlying this family-specific and efficient activation are largely unknown. Here, we investigate the structural mechanism underlying the Gi/o family-specific activation of GIRK, by combining cell-based BRET experiments and NMR analyses in a reconstituted membrane environment. We show that the interaction formed by the αA helix of Gαi/o mediates the formation of the Gαi/oβγ-GIRK complex, which is responsible for the family-specific activation of GIRK. We also present a model structure of the Gαi/oβγ-GIRK complex, which provides the molecular basis underlying the specific and efficient regulation of GIRK.

  • Nanodiscs for structural biology in a membranous environment

    Yokogawa M., Fukuda M., Osawa M.

    Chemical and Pharmaceutical Bulletin (Chemical and Pharmaceutical Bulletin)  67 ( 4 ) 321 - 326 2019年

    ISSN  00092363

     概要を見る

    © 2019 The Pharmaceutical Society of Japan The structures of many membrane proteins have been analyzed in detergent micelles. However, the environment of detergent micelles differs somewhat from that of the lipid bilayer, where membrane proteins exhibit physiological functions. Therefore, a more membrane-like environment has been awaited for structural analysis of membrane proteins. Nanodiscs are “hockey-puck”-shaped lipid bilayer particles that distribute in a monodispersed manner in aqueous solution. We review how nanodiscs or protein-reconstituted nanodiscs are prepared and how they are utilized to analyze protein structure, dynamics, and interactions with lipid molecules using solution NMR and cryo-electron microscopy.

  • Structural basis for the ethanol action on G-protein-activated inwardly rectifying potassium channel 1 revealed by NMR spectroscopy.

    Toyama Y, Kano H, Mase Y,Yokogawa M, Osawa M, Shimada I

    Proc Natl Acad Sci U S A. 115 ( 15 ) 3858 - 3863 2018年03月

    研究論文(学術雑誌), 共著, 査読有り

  • Characterization of the multimeric structure of poly(A)-binding protein on a poly(A) tail.

    Ryoichi Sawazaki, Shunsuke Imai, Mariko Yokogawa,Nao Hosoda, Shin-ichi Hoshino, Muneyo Mio, Kazuhiro Mio, Ichio Shimada, and Masanori Osawa

    Sci. Rep. 8   1455 2018年01月

    研究論文(学術雑誌), 査読有り

     概要を見る

    Eukaryotic mature mRNAs possess a poly adenylate tail (poly(A)), to which multiple molecules of poly(A)-binding protein C1 (PABPC1) bind. PABPC1 regulates translation and mRNA metabolism by binding to regulatory proteins. To understand functional mechanism of the regulatory proteins, it is necessary to reveal how multiple molecules of PABPC1 exist on poly(A). Here, we characterize the structure of the multiple molecules of PABPC1 on poly(A), by using transmission electron microscopy (TEM), chemical cross-linking, and NMR spectroscopy. The TEM images and chemical cross-linking results indicate that multiple PABPC1 molecules form a wormlike structure in the PABPC1-poly(A) complex, in which the PABPC1 molecules are linearly arrayed. NMR and cross-linking analyses indicate that PABPC1 forms a multimer by binding to the neighbouring PABPC1 molecules via interactions between the RNA recognition motif (RRM) 2 in one molecule and the middle portion of the linker region of another molecule. A PABPC1 mutant lacking the interaction site in the linker, which possesses an impaired ability to form the multimer, reduced the in vitro translation activity, suggesting the importance of PABPC1 multimer formation in the translation process. We therefore propose a model of the PABPC1 multimer that provides clues to comprehensively understand the regulation mechanism of mRNA translation.

  • Dynamic regulation of GDP binding to G proteins revealed by magnetic field-dependent NMR relaxation analyses

    Yuki Toyama, Hanaho Kano, Yoko Mase, Mariko Yokogawa, Masanori Osawa, and Ichio Shimada

    Nat. Commun. 8   14523 2017年01月

    研究論文(学術雑誌), 共著

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KOARA(リポジトリ)収録論文等 【 表示 / 非表示

総説・解説等 【 表示 / 非表示

  • Nuclear Magnetic Resonance Approaches for Characterizing Protein-Protein Interactions.

    Toyama Y, Mase Y, Kano H, Yokogawa Mariko, Osawa M, Shimada I

    Methods Mol Biol. 1684   115 - 128 2018年10月

    総説・解説(学術雑誌)

競争的資金等の研究課題 【 表示 / 非表示

  • B型肝炎ウイルスの肝細胞侵入および増殖機構の構造生物学的解析

    2018年04月
    -
    2021年03月

    文部科学省・日本学術振興会, 科学研究費助成事業, 横川 真梨子, 基盤研究(C), 補助金,  代表

  • B型肝炎ウイルスの感染機構の構造基盤

    2016年04月
    -
    2018年03月

    文部科学省・日本学術振興会, 科学研究費助成事業, 横川 真梨子, 若手研究(B), 補助金,  代表

 

担当授業科目 【 表示 / 非表示

  • 課題研究(生命機能物理学)

    2019年度

  • 演習(生命機能物理学)

    2019年度

  • 卒業研究A

    2019年度

  • 物理化学3

    2019年度

  • 物理分析学

    2019年度

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担当経験のある授業科目 【 表示 / 非表示

  • 薬学基礎実習

    慶應義塾, 2015年度, 秋学期, 専門科目, 実習・実験

  • C1(4)物質の変化

    慶應義塾, 2015年度, 秋学期, 講義

    反応速度

  • 薬学実習IIA(化学、物理)

    慶應義塾, 2015年度, 春学期, 専門科目, 実習・実験