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Role for OMP25 and the associated proteins in regulation of morphology and mtracellular distribution of mitochondria

Research Project

Project/Area Number 13680797
Research Category

Grant-in-Aid for Scientific Research (C)

Allocation TypeSingle-year Grants
Section一般
Research Field Cell biology
Research InstitutionTohoku University (2002)
The Institute of Physical and Chemical Research (2001)

Principal Investigator

NEMOTO Yasuo  Tohoku University, Graduate School of Medicine, Lecturer, 大学院・医学系研究科, 講師 (30250088)

Project Period (FY) 2001 – 2002
Project Status Completed (Fiscal Year 2002)
Budget Amount *help
¥3,600,000 (Direct Cost: ¥3,600,000)
Fiscal Year 2002: ¥1,700,000 (Direct Cost: ¥1,700,000)
Fiscal Year 2001: ¥1,900,000 (Direct Cost: ¥1,900,000)
KeywordsMitochondria / Protein / Lipid / Enzyme / Cell / Metabolism
Research Abstract

A novel protein, p200, was identified as a binding protein for OMP25. The specific antibodies against p200 were raised and immunocytochemistry with them showed that p200 is widely distributed among rat ant mUrine tissues and it is localized on the endoplasmic reticulum membrane within cells. Biochemical experiments indicated that the carboxy terminal portion of p200 is oriented toward cytoplasm and specifically binds to the PDZ domain of OMP25. Overexpression of OMP25 in mammalian cultured cells caused the morphological changes of the endoplasmic reticulum and the mitochondria with apparently no effects on other organ el les. The results of the present studies have indicated that the binding of p200 and OMP25 may mediate the association of the endoplasmic reticulum and mitochondria in mammalian cells.

Report

(3 results)
  • 2002 Annual Research Report   Final Research Report Summary
  • 2001 Annual Research Report
  • Research Products

    (6 results)

All Other

All Publications (6 results)

  • [Publications] Ringstad, N., et al.: "Differential expression of endophilin 1 and 2 dimers at central nervous system synapses"The Journal of Biological Chemistry. 276・44. 40424-40430 (2001)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      2002 Final Research Report Summary
  • [Publications] Nemoto, Y., et al.: "Identification and characterization of aynaptojanin 2 isoform predominantly expressed in nerve terminals"The Journal of Biological Chemistry. 276・44. 41133-41142 (2001)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      2002 Final Research Report Summary
  • [Publications] Ringstad,N., Nemoto,Y., De Camilli: "P.Differential expression of endophiiin 1 and 2 dimers at central nervpus synapses"Journal of Biological Chemistry. 276. 40424-40430 (2001)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      2002 Final Research Report Summary
  • [Publications] Nemoto,Y., Wentc,M.R., Watanabe,M., Daniell,L., Murakami,T., Ringstad,N., Yamada,H., Takei,K., De Camilli, P.: "Identification and characterization of synaptojanin 2 isoform predominantly expressed in nerve terminals"Journal of Biological Chemistry. 276. 41133-41142 (2001)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      2002 Final Research Report Summary
  • [Publications] Ringstad, N., Nemoto, Y., De Camilli, P: "Differential expression of endophilin 1 and 2 dimers at central nervous system synapses."The Journal of Biological Chemistry. 276・44. 40424-40430 (2001)

    • Related Report
      2001 Annual Research Report
  • [Publications] Nemoto, Y., et al.: "Identification and characterization of a synaptojanin 2 splice isoform predominantly expressed in nerve terminals."The Journal of Biological Chemistry. 276・44. 41133-41142 (2001)

    • Related Report
      2001 Annual Research Report

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Published: 2001-04-01   Modified: 2016-04-21  

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