RGD Reference Report - Modulation of GDP-dissociation inhibitor protein membrane retention by the cellular redox state in adipocytes. - Rat Genome Database
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Modulation of GDP-dissociation inhibitor protein membrane retention by the cellular redox state in adipocytes.

Authors: Chinni, SR  Brenz, M  Shisheva, A 
Citation: Chinni SR, etal., Exp Cell Res. 1998 Jul 10;242(1):373-80.
RGD ID: 9684967
Pubmed: (View Article at PubMed) PMID:9665834
DOI: Full-text: DOI:10.1006/excr.1998.4105

Small GTPases of the Rab family play a key role in the regulation of vesicular transport in eukaryotic cells. As they cycle on and off membranes, Rab proteins rely on the escort services of the GDP-dissociation inhibitor (GDI) proteins. While specific recognition of Rab-GDI complexes by membrane targets is suggested, the mechanisms underlying the subsequent GDI release into the cytosol remain unknown. In this study, we demonstrate that modulations of the cellular redox status in intact rat fat cells, 3T3-L1 adipocytes in culture, and other cultured cell types result in rapid, effective, dose-dependent, and selective membrane dynamics of GDI-1 and -2, membrane retention under reduced redox state, or dissociation under oxidized conditions. GDI retention on adipocyte membranes is associated with a complete arrest of insulin-induced translocation of GLUT4 glucose transporters onto plasma membrane. Together, these data suggest, first, that following Rab delivery to membranes, GDI release is promoted by a shift in the redox state and, second, that arrest of GDIs on membranes inhibits intracellular membrane trafficking events.

Annotation

Gene Ontology Annotations    

Biological Process

Cellular Component
cytosol  (IDA)
membrane  (IDA)

Objects Annotated

Genes (Rattus norvegicus)
Arhgdia  (Rho GDP dissociation inhibitor alpha)
Arhgdib  (Rho GDP dissociation inhibitor beta)


Additional Information