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Structural analysis of novel RabGEF proteins

Research Project

Project/Area Number 17K15072
Research Category

Grant-in-Aid for Young Scientists (B)

Allocation TypeMulti-year Fund
Research Field Structural biochemistry
Research InstitutionThe University of Tokyo

Principal Investigator

ITO Sakurako  東京大学, 定量生命科学研究所, 助教 (60597152)

Research Collaborator SATO Ken  
Project Period (FY) 2017-04-01 – 2019-03-31
Project Status Completed (Fiscal Year 2018)
Budget Amount *help
¥4,550,000 (Direct Cost: ¥3,500,000、Indirect Cost: ¥1,050,000)
Fiscal Year 2018: ¥2,080,000 (Direct Cost: ¥1,600,000、Indirect Cost: ¥480,000)
Fiscal Year 2017: ¥2,470,000 (Direct Cost: ¥1,900,000、Indirect Cost: ¥570,000)
KeywordsRab / GEF / 低分子量GTPase / X線結晶構造解析 / 立体構造解析 / 細胞内輸送 / 生体膜
Outline of Final Research Achievements

We have determined the crystal structure of a complex of Rab11a and its novel GEF, SH3BP5. SH3BP5 harbors the V-shaped structure composed of two coiled coils. SH3BP5 pulls out the switch I region of Rab11a, and thereby promotes the nucleotide exchange. Mutational analysis based on the structure elucidated important interactions between SH3BP5 and Rab11a.

Academic Significance and Societal Importance of the Research Achievements

RabGEFのヌクレオチド交換触媒ドメインは多様であることが知られている。本研究では、SH3BP5-Rab11a複合体の立体構造解析により、新規のRabGEFであるSH3BP5の反応機構を解明した。また、連携研究者である群馬大学の佐藤健研究室との共同研究により、SH3BP5の細胞内挙動を解析した。論文執筆中に、カナダのグループからSH3BP5-Rab11a複合体構造についての論文がnature communicationsに発表されてしまった。その内容は我々の研究成果と一致するものであり、我々の結果を裏付けた。得られた研究成果をまとめてLife Science Allianceに発表した。

Report

(3 results)
  • 2018 Annual Research Report   Final Research Report ( PDF )
  • 2017 Research-status Report
  • Research Products

    (5 results)

All 2019 2018 2017

All Journal Article (4 results) (of which Int'l Joint Research: 1 results,  Peer Reviewed: 4 results,  Open Access: 3 results) Presentation (1 results)

  • [Journal Article] Structural basis of guanine nucleotide exchange for Rab11 by SH3BP52019

    • Author(s)
      Goto-Ito Sakurako、Morooka Nobukatsu、Yamagata Atsushi、Sato Yusuke、Sato Ken、Fukai Shuya
    • Journal Title

      Life Science Alliance

      Volume: 2 Issue: 2 Pages: e201900297-e201900297

    • DOI

      10.26508/lsa.201900297

    • Related Report
      2018 Annual Research Report
    • Peer Reviewed / Open Access
  • [Journal Article] Structural insights into two distinct binding modules for Lys63-linked polyubiquitin chains in RNF1682018

    • Author(s)
      Takahashi Tomio S.、Hirade Yoshihiro、Toma Aya、Sato Yusuke、Yamagata Atsushi、Goto-Ito Sakurako、Tomita Akiko、Nakada Shinichiro、Fukai Shuya
    • Journal Title

      Nature Communications

      Volume: 9 Issue: 1 Pages: 170-170

    • DOI

      10.1038/s41467-017-02345-y

    • Related Report
      2017 Research-status Report
    • Peer Reviewed / Open Access
  • [Journal Article] Structural basis of trans-synaptic interactions between PTPδ and SALMs for inducing synapse formation2018

    • Author(s)
      Goto-Ito Sakurako、Yamagata Atsushi、Sato Yusuke、Uemura Takeshi、Shiroshima Tomoko、Maeda Asami、Imai Ayako、Mori Hisashi、Yoshida Tomoyuki、Fukai Shuya
    • Journal Title

      Nature Communications

      Volume: 9 Issue: 1

    • DOI

      10.1038/s41467-017-02417-z

    • Related Report
      2017 Research-status Report
    • Peer Reviewed / Open Access
  • [Journal Article] Structural basis for specific cleavage of Lys6-linked polyubiquitin chains by USP302017

    • Author(s)
      Sato Yusuke、Okatsu Kei、Saeki Yasushi、Yamano Koji、Matsuda Noriyuki、Kaiho Ai、Yamagata Atsushi、Goto-Ito Sakurako、Ishikawa Minoru、Hashimoto Yuichi、Tanaka Keiji、Fukai Shuya
    • Journal Title

      Nature Structural & Molecular Biology

      Volume: 24 Issue: 11 Pages: 911-919

    • DOI

      10.1038/nsmb.3469

    • Related Report
      2017 Research-status Report
    • Peer Reviewed / Int'l Joint Research
  • [Presentation] PTPRDとSALMによるシナプス形成誘導機構の構造基盤2017

    • Author(s)
      伊藤桜子、山形敦史、佐藤裕介、植村健、城島知子、前田亜沙美、今井彩子、森寿、吉田知之、深井周也
    • Organizer
      ConBio2017
    • Related Report
      2017 Research-status Report

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Published: 2017-04-28   Modified: 2020-03-30  

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