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Structural study of FIP200, a scaffold protein of mammalian autophagy initiation complex

Research Project

Project/Area Number 16K21593
Research Category

Grant-in-Aid for Young Scientists (B)

Allocation TypeMulti-year Fund
Research Field Structural biochemistry
Physical pharmacy
Research InstitutionMicrobial Chemistry Research Foundation

Principal Investigator

SUZUKI Hironori  公益財団法人微生物化学研究会, 微生物化学研究所, 博士研究員 (20625694)

Project Period (FY) 2016-04-01 – 2018-03-31
Project Status Completed (Fiscal Year 2017)
Budget Amount *help
¥4,160,000 (Direct Cost: ¥3,200,000、Indirect Cost: ¥960,000)
Fiscal Year 2017: ¥1,820,000 (Direct Cost: ¥1,400,000、Indirect Cost: ¥420,000)
Fiscal Year 2016: ¥2,340,000 (Direct Cost: ¥1,800,000、Indirect Cost: ¥540,000)
KeywordsX線結晶構造解析 / オートファジー / X線結晶構造解析
Outline of Final Research Achievements

A lot of proteins involved in autophagy are widely conserved in eukaryotes from budding yeast to humans. However, some proteins are unique factors to higher eukaryotes such as human. One of which is FIP200, a scaffold protein of mammalian autophagy initiation complex.
In this study, we first prepared to stable region to use biochemical analysis and crystallographic studies. Moreover, we crystallized and determined the structure of a part of FIP200. The C-terminal region of FIP200 formed a parallel coiled-coil dimer. This result indicates that the large protein FIP200 functioning as a scaffold protein assumes a parallel dimeric structure.

Report

(3 results)
  • 2017 Annual Research Report   Final Research Report ( PDF )
  • 2016 Research-status Report
  • Research Products

    (5 results)

All 2018 2017 2016

All Journal Article (4 results) (of which Peer Reviewed: 4 results,  Open Access: 3 results,  Acknowledgement Compliant: 2 results) Presentation (1 results) (of which Int'l Joint Research: 1 results)

  • [Journal Article] Atg7 Activates an Autophagy-Essential Ubiquitin-like Protein Atg8 through Multi-Step Recognition2018

    • Author(s)
      Yamaguchi Masaya、Satoo Kenji、Suzuki Hironori、Fujioka Yuko、Ohsumi Yoshinori、Inagaki Fuyuhiko、Noda Nobuo N.
    • Journal Title

      Journal of Molecular Biology

      Volume: 430 Issue: 3 Pages: 249-257

    • DOI

      10.1016/j.jmb.2017.12.002

    • Related Report
      2017 Annual Research Report
    • Peer Reviewed
  • [Journal Article] Biophysical characterization of Atg11, a scaffold protein essential for selective autophagy in yeast2017

    • Author(s)
      Suzuki, H. and *Noda, N. N.
    • Journal Title

      FEBS Open Bio

      Volume: 8 Issue: 1 Pages: 110-116

    • DOI

      10.1002/2211-5463.12355

    • Related Report
      2017 Annual Research Report
    • Peer Reviewed / Open Access
  • [Journal Article] Structural biology of the core autophagy machinery.2017

    • Author(s)
      Suzuki H, Osawa T, Fujioka Y, Noda NN
    • Journal Title

      Current Opinion in Structural Biology

      Volume: 43 Pages: 10-17

    • DOI

      10.1016/j.sbi.2016.09.010

    • Related Report
      2016 Research-status Report
    • Peer Reviewed / Open Access / Acknowledgement Compliant
  • [Journal Article] The Intrinsically Disordered Protein Atg13 Mediates Supramolecular Assembly of Autophagy Initiation Complexes.2016

    • Author(s)
      Yamamoto H, Fujioka Y, Suzuki SW, Noshiro D, Suzuki H, Kondo-Kakuta C, Kimura Y, Hirano H, Ando T, Noda NN, Ohsumi Y
    • Journal Title

      Developmental Cell

      Volume: 38 Issue: 1 Pages: 86-99

    • DOI

      10.1016/j.devcel.2016.06.015

    • Related Report
      2016 Research-status Report
    • Peer Reviewed / Open Access / Acknowledgement Compliant
  • [Presentation] Structure of Atg101 in complex with Atg13: Functional insights into mammalian autophagy initiation2016

    • Author(s)
      Suzuki H, Kaizuka T, Mizushima N, Noda NN
    • Organizer
      第42回内藤コンファレンス 生命科学に革命をもたらす最先端構造生物学
    • Place of Presentation
      シャトレーゼガトーキングダムサッポロ(北海道札幌市)
    • Year and Date
      2016-10-04
    • Related Report
      2016 Research-status Report
    • Int'l Joint Research

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Published: 2016-04-21   Modified: 2019-03-29  

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