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Membrane localization of LRRK2, a causative gene for familial Parkinson's

Research Project

Project/Area Number 24790068
Research Category

Grant-in-Aid for Young Scientists (B)

Allocation TypeMulti-year Fund
Research Field Biological pharmacy
Research InstitutionThe University of Tokyo

Principal Investigator

ITO Genta  東京大学, 医学(系)研究科(研究員), 助教 (10431892)

Project Period (FY) 2012 – 2013
Project Status Completed (Fiscal Year 2013)
Budget Amount *help
¥4,550,000 (Direct Cost: ¥3,500,000、Indirect Cost: ¥1,050,000)
Fiscal Year 2013: ¥2,210,000 (Direct Cost: ¥1,700,000、Indirect Cost: ¥510,000)
Fiscal Year 2012: ¥2,340,000 (Direct Cost: ¥1,800,000、Indirect Cost: ¥540,000)
Keywordsパーキンソン病 / LRRK2 / キナーゼ / LRRK2 / 細胞内局在
Research Abstract

It has been reported that LRRK2 exists on membrane of organelles or vesicles in cytoplasm by electron microscopic analysis. However, the membrane localization of LRRK2 has not been precisely characterized. In this study, we found that asmall fraction of LRRK2 was eluted in the detergent-soluble membrane fraction. We also found that LRRK2 translocates to the LAMP1-positive structure upon treatment of cells with a LRRK2 inhibitor. In addition, we succeeded in forcing LRRK2 to translocate to organelles by using a chemical-induced localization system.

Report

(3 results)
  • 2013 Annual Research Report   Final Research Report ( PDF )
  • 2012 Research-status Report
  • Research Products

    (7 results)

All 2012 Other

All Journal Article (2 results) (of which Peer Reviewed: 2 results) Presentation (2 results) Remarks (3 results)

  • [Journal Article] Re-examination of the dimerization state of leucine-rich repeat kinase 2: class FormattedString { value: Predominance of the monomeric form }2012

    • Author(s)
      Ito G, Iwatsubo T.
    • Journal Title

      Biochemical Journal

      Volume: 441 Issue: 3 Pages: 987

    • DOI

      10.1042/bj20111215

    • URL

      https://localhost/en/publications/48147140-5aed-494d-829b-b94de9730eaa

    • Related Report
      2013 Final Research Report
    • Peer Reviewed
  • [Journal Article] Phosphorylation of α-synuclein protein at Ser-129 reduces neuronal dysfunction by lowering its membrane binding property in Caenorhabditis elegans2012

    • Author(s)
      Kuwahara T, Tonegawa R, Ito G, Mitani S, Iwatsubo T
    • Journal Title

      J. Biol. Chem.

      Volume: 287 Issue: 10 Pages: 7098-7109

    • DOI

      10.1074/jbc.m111.237131

    • Related Report
      2013 Final Research Report
    • Peer Reviewed
  • [Presentation] Molecular mechanisnl of hypophosphorylation of LRRK2 caused by familial mutations2012

    • Author(s)
      Genta Ito, Shogo Kamikawaji, Takeshi Iwatsubo
    • Organizer
      米国神経科学会
    • Place of Presentation
      ニューオーリンズ、アメリカ合衆国
    • Year and Date
      2012-10-15
    • Related Report
      2013 Final Research Report
  • [Presentation] Molecular mechanism of hypophosphorylation of LRRK2 caused by familial mutations2012

    • Author(s)
      伊藤弦太、上川路翔悟、岩坪威
    • Organizer
      Neuroscience 2012
    • Place of Presentation
      New Orleans, USA
    • Related Report
      2012 Research-status Report
  • [Remarks]

    • URL

      http://www.neuropathology.m.u-tokyo.ac.jp/

    • Related Report
      2013 Final Research Report
  • [Remarks] 東京大学大学院 医学系研究科 神経病理学分野

    • URL

      http://www.neuropathology.m.u-tokyo.ac.jp/

    • Related Report
      2013 Annual Research Report
  • [Remarks] 東京大学大学院医学系研究科神経病理学分野

    • URL

      http://www.neuropathology.m.u-tokyo.ac.jp/

    • Related Report
      2012 Research-status Report

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Published: 2013-05-31   Modified: 2019-07-29  

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