RGD Reference Report - Rab-alphaGDI activity is regulated by a Hsp90 chaperone complex. - Rat Genome Database

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Rab-alphaGDI activity is regulated by a Hsp90 chaperone complex.

Authors: Sakisaka, T  Meerlo, T  Matteson, J  Plutner, H  Balch, WE 
Citation: Sakisaka T, etal., EMBO J 2002 Nov 15;21(22):6125-35.
RGD ID: 632546
Pubmed: PMID:12426384   (View Abstract at PubMed)
PMCID: PMC137195   (View Article at PubMed Central)

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 Ca(2+)-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 Ca(2+)-dependent events triggering Rab-GTP hydrolysis with retrieval of Rab-GDP to the cytosol.

Gene Ontology Annotations    Click to see Annotation Detail View

Biological Process
TermQualifierEvidenceWithReferenceNotesSourceOriginal Reference(s)
response to calcium ion  IDA 632546 RGD 

Cellular Component
TermQualifierEvidenceWithReferenceNotesSourceOriginal Reference(s)
protein-containing complex  IDA 632546; 632546 RGD 

Molecular Function

Objects Annotated

Genes (Rattus norvegicus)
Gdi1  (GDP dissociation inhibitor 1)
Rab3a  (RAB3A, member RAS oncogene family)

Objects referenced in this article
Gene Dnajc5 DnaJ heat shock protein family (Hsp40) member C5 Rattus norvegicus
Gene Hsp90aa1 heat shock protein 90 alpha family class A member 1 Rattus norvegicus

Additional Information