| Co-Investigator(Kenkyū-buntansha) |
SASAKI Takuya Kobe University. Faculty of Medicine, Research Associate, 医学部, 助手 (40241278)
KIKUCHI Akira Kobe University. Faculty of Medicine, Associate Professor, 医学部, 講師 (10204827)
KAIBUCHI Kozo Kobe University. Faculty of Medicine, Associate Professor, 医学部, 助教授 (00169377)
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| Research Abstract |
There is the small GTP- binding protein (G protein) superfamily which consists of over fiftu members. All members have monomeric proteins with Mrs between 20,000 and 30,000 which exhibit both GDP/GTO-binding and GTP ase activities. In the present research project, we studied the functions and modes of activation of small G proteins. Ras is the representative of this su perfamily and is well known to regulate cell proliferation, differentiation, and transformation, but its modes of activation and action remain to be clarified. We characterized three GDP/GTP exchange proteins for Ras including Smq GDS, CDC25Mm, and msos. We identified a target protein for Ras and named it REKS, which phosphorylated MAP kinase and thereby activated it in a Ras-dependent manner. Accumulating evidence suggests that Rho regulates certain functions through an actomyosin system. By use of C3 exoenzyme and Rho GDI, we showed that Rho regulated cell morphogy, cell motility, membrane ruffling, cy-tokinesis, and smooth muscle contraction through an actomyosin system. Red family is known to regulate intracellular vesicle transport, such as exocytosis, endocytosis, and transcytosis. Rab3A is a member of Rab family which is particularly implicated in neurotransmitter release from the synapse. We isolated the cDNA encoding a target protein for Rab3A, which selectively in-teracted with the GTP-bound form of Rab3A, and named it rabphilin-3A.
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