Linked Life Data

11278572

Source:http://linkedlifedata.com/resource/pubmed/id/11278572

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pubmed-article:11278572pubmed:abstractTextFas-mediated apoptosis results in the activation of caspases, which subsequently cleave cellular substrates that are essential for normal cell viability. In the present study, we show that the Ras-related GTP-binding protein Cdc42 is susceptible to caspase-catalyzed proteolysis in a number of cell lines, including NIH3T3 fibroblasts, human breast cancer cells (e.g. T47D), and COS-7 cells. Both caspase-3 and caspase-7 were able to catalyze the cleavage of Cdc42, whereas caspase-6 and caspase-8 were without effect. The susceptibility to the caspase-stimulated degradation is specific; although Rac can also serve as a caspase substrate, neither Rho nor Ras is degraded. Caspase sensitivity is conferred by a consensus sequence (DXXD) that lies immediately upstream of the Rho insert regions (residues 122-134) of Cdc42 and Rac. The removal of a stretch of residues (120) that includes the insert region or site-directed mutagenesis of either aspartic acid 118 or 121 within a constitutively active background (i.e. Cdc42(F28L)) as well as a wild-type Cdc42 background yields Cdc42 molecules that provide a marked protection against Fas ligand-induced apoptosis. Overall, these results are consistent with a model in which Cdc42 acts downstream of Fas, perhaps to influence the rate of apoptosis, with the ultimate caspase-mediated degradation of Cdc42 then allowing for a maximal apoptotic response.lld:pubmed
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pubmed-article:11278572pubmed:articleTitleCdc42 is a substrate for caspases and influences Fas-induced apoptosis.lld:pubmed
pubmed-article:11278572pubmed:affiliationDepartment of Molecular Medicine, Veterinary Medical Center, Baker Laboratory, Cornell University, Ithaca, New York, 14853, USA.lld:pubmed
pubmed-article:11278572pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:11278572pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
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