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Analysis of a dynamic behavior of the E3 ubiquitin ligase in the endoplasmic reticulum

Research Project

Project/Area Number 25870312
Research Category

Grant-in-Aid for Young Scientists (B)

Allocation TypeMulti-year Fund
Research Field Functional biochemistry
Cell biology
Research InstitutionNagoya University

Principal Investigator

NAKATSUKASA Kunio  名古屋大学, 理学(系)研究科(研究院), 助教 (90547522)

Project Period (FY) 2013-04-01 – 2015-03-31
Project Status Completed (Fiscal Year 2014)
Budget Amount *help
¥4,290,000 (Direct Cost: ¥3,300,000、Indirect Cost: ¥990,000)
Fiscal Year 2014: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
Fiscal Year 2013: ¥2,600,000 (Direct Cost: ¥2,000,000、Indirect Cost: ¥600,000)
Keywords小胞体 / タンパク質 / 品質管理機構 / ユビキチン / 分解 / 品質管理 / ユビキチンリガーゼ / タンパク質複合体 / 生体膜
Outline of Final Research Achievements

Inactivation of Cdc48p/p97 stalled retrotranslocation and triggered formation of a complex that contains the 26S proteasome, Cdc48p/p97, ubiquitinated substrates, select components of the Hrd1 complex, and the lumenal recognition factor, Yos9p. We proposed that the actions of Cdc48p/p97 and the proteasome are tightly coupled during ERAD. Our data also support a model in which the Hrd1 complex links substrate recognition and degradation on opposite sides of the ER membrane. Based on these results, we performed in vivo site-specific crosslinking experiments. Non-natural photo-reactive amino acids were incorporated into Hrd3 in yeast to detect cross-linked Hrd1. Although we could detect some cross-linked products with Hrd3, it is currently unclear if these are Hrd1-Hrd3 crosslinked products. We are now trying to scale up the system to better detect Hrd1. In addition, we are analyzing a role of the transmembrane domain of Hrd3 especially under the stress conditions.

Report

(3 results)
  • 2014 Annual Research Report   Final Research Report ( PDF )
  • 2013 Research-status Report
  • Research Products

    (4 results)

All 2014 2013

All Journal Article (3 results) (of which Peer Reviewed: 3 results) Presentation (1 results)

  • [Journal Article] Recent technical developments in the study of ER-associated degradation.2014

    • Author(s)
      Nakatsukasa, K., Kamura T., Brodsky, JL.
    • Journal Title

      Current Opinion in Cell Biology

      Volume: 29 Pages: 82-91

    • DOI

      10.1016/j.ceb.2014.04.008

    • Related Report
      2014 Annual Research Report
    • Peer Reviewed
  • [Journal Article] The nutrient stress-induced small GTPase Rab5 contributes to the activation of vesicle trafficking and vacuolar activity.2014

    • Author(s)
      Nakatsukasa, K., Kanada, A., Matsuzaki, M., Byrne, SD., Okumura, F., Kamura, T.
    • Journal Title

      J Biol Chem

      Volume: 289 Issue: 30 Pages: 20970-20978

    • DOI

      10.1074/jbc.m114.548297

    • Related Report
      2014 Annual Research Report
    • Peer Reviewed
  • [Journal Article] A stalled retrotranslocation complex reveals physical linkage between substrate recognition and proteasomal degradation during ER associated degradation2013

    • Author(s)
      Kunio Nakatsukasa. Jeffrey L. Brodsky, Takumi Kamura
    • Journal Title

      Molecular Biology of the Cell

      Volume: (印刷中) Issue: 11 Pages: 1765-1775

    • DOI

      10.1091/mbc.e12-12-0907

    • Related Report
      2013 Research-status Report
    • Peer Reviewed
  • [Presentation] Subcellular fractionation analysis of the extraction of ubiquitinated polytopic substrates during ER-associated degradation2014

    • Author(s)
      Nakatsukasa K., Kamura T.
    • Organizer
      American Society for Cell Biology
    • Place of Presentation
      フィラデルフィア
    • Year and Date
      2014-12-06 – 2014-12-10
    • Related Report
      2014 Annual Research Report

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Published: 2014-07-25   Modified: 2019-07-29  

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