• Search Research Projects
  • Search Researchers
  • How to Use
  1. Back to previous page

Structural analysis of the Rab and SNARE localization

Research Project

Project/Area Number 23770107
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, 放射光連携研究機構, 特任助教 (60597152)

Project Period (FY) 2011 – 2012
Project Status Completed (Fiscal Year 2012)
Budget Amount *help
¥4,550,000 (Direct Cost: ¥3,500,000、Indirect Cost: ¥1,050,000)
Fiscal Year 2012: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2011: ¥2,990,000 (Direct Cost: ¥2,300,000、Indirect Cost: ¥690,000)
KeywordsX線結晶構造解析 / タンパク質 / 生体膜 / 立体構造解析 / 膜融合 / X線結晶解析 / 小胞輸送
Research Abstract

In eukaryotic cells, Rab and SNARE regulate the fusion of membrane compartments. Rabs are inseted into membranes via the prenylated moieties which are post-translationally attached. A membrane protein called GDF is proposed to catalyze the membrane insertion of Rab. As GDF and VAMP2, one of the SNARE protein, is shown to interact with each other, we are trying to reveal the structural basis of GDF-SNARE cooperation. So far, we have succeeded in the crystallization of GDF, and now trying to improve thediffraction quality of crystals. Also, we are trying to prepare GDF-VAMP2 complex.

Report

(3 results)
  • 2012 Annual Research Report   Final Research Report ( PDF )
  • 2011 Research-status Report
  • Research Products

    (5 results)

All 2013 2012 2011

All Journal Article (4 results) (of which Peer Reviewed: 4 results) Presentation (1 results)

  • [Journal Article] Crystallographic and mutational studies on the tRNA thiouridine synthetase TtuA2013

    • Author(s)
      Hirofumi Nakagawa
    • Journal Title

      Proteins:Structure, function, and bioinformatics

      Volume: Epub ahead of print Issue: 7 Pages: 1232-1244

    • DOI

      10.1002/prot.24273

    • Related Report
      2012 Annual Research Report
    • Peer Reviewed
  • [Journal Article] Get1 stabilizes an open dimer conformation of get3 ATPase by binding two distinct interfaces.2012

    • Author(s)
      Kubota K, Yamagata A, Sato Y, Goto-Ito S, Fukai S.
    • Journal Title

      J Mol Biol.

      Volume: 422(3) Issue: 3 Pages: 366-75

    • DOI

      10.1016/j.jmb.2012.05.045

    • Related Report
      2012 Annual Research Report 2012 Final Research Report
    • Peer Reviewed
  • [Journal Article] Molecular basis of Lys-63-linked polyubiquitination inhibition by the interaction between human deubiquitinating enzyme OTUB1 and ubiquitin-conjugating enzyme UBC13.2012

    • Author(s)
      Sato Y, Yamagata A, Goto-Ito S, Kubota K, Miyamoto R, Nakada S, Fukai S.
    • Journal Title

      J Biol Chem.

      Volume: 287(31) Issue: 31 Pages: 25860-8

    • DOI

      10.1074/jbc.m112.364752

    • Related Report
      2012 Annual Research Report 2012 Final Research Report
    • Peer Reviewed
  • [Journal Article] Differentiating analogous tRNA methyltransferases by fragments of the methyl donor.2011

    • Author(s)
      Lahoud G, Goto-Ito S, Yoshida K, Ito T, Yokoyama S
    • Journal Title

      Hou YM.RNA.

      Volume: 17(7) Issue: 7 Pages: 1236-46

    • DOI

      10.1261/rna.2706011

    • Related Report
      2012 Final Research Report
    • Peer Reviewed
  • [Presentation] Get3 による翻訳後膜埋込み機構の構造学的基盤2012

    • Author(s)
      山形敦史
    • Organizer
      第35回日本分子生物学会年会
    • Place of Presentation
      福岡国際会議場・マリンメッセ福岡
    • Related Report
      2012 Annual Research Report

URL: 

Published: 2011-08-05   Modified: 2019-07-29  

Information User Guide FAQ News Terms of Use Attribution of KAKENHI

Powered by NII kakenhi