Role for OMP25 and the associated proteins in regulation of morphology and mtracellular distribution of mitochondria
Project/Area Number |
13680797
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Research Category |
Grant-in-Aid for Scientific Research (C)
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Allocation Type | Single-year Grants |
Section | 一般 |
Research Field |
Cell biology
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Research Institution | Tohoku 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)
|
Keywords | Mitochondria / 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.
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Report
(3 results)
Research Products
(6 results)
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[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)
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