期刊
EMBO JOURNAL
卷 21, 期 22, 页码 6125-6135出版社
OXFORD UNIV PRESS
DOI: 10.1093/emboj/cdf603
关键词
CSP; GDI; Hsp90; Rab3A; synaptic vesicle
资金
- NCI NIH HHS [CA 58689] Funding Source: Medline
- PHS HHS [GN 33301] Funding Source: Medline
The Rab-specific alphaGDP-dissociation inhibitor (alphaGDI) regulates the recycling of Rab GTPases. We have now identified a novel alphaGDI complex from synaptic membranes that contains three chaperone components: Hsp90, Hsc70 and cysteine string protein (CSP). We find that the alphaGDI-chaperone complex is dissociated in response to Ca2+-induced neurotransmitter release, that chaperone complex dissociation is sensitive to the Hsp90 inhibitor geldanamycin (GA) and that GA inhibits the ability of alphaGDI to recycle Rab3A during neurotransmitter release. We propose that alphaGDI interacts with a specialized membrane-associated Rab recycling Hsp90 chaperone system on the vesicle membrane to coordinate the Ca2+-dependent events triggering Rab-GTP hydrolysis with retrieval of Rab-GDP to the cytosol.
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