Title : Guanine nucleotides protect Rho proteins from endogenous proteolytic degradation in renal membranes.

Pub. Date : 1998

PMID : 9666307






4 Functional Relationships(s)
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1 In addition, Cdc42 and RhoA associated with brush border membranes were largely resistant to increased proteolytic degradation induced by membrane treatment with the denaturing reagent urea as well as to added trypsin when incubated in the presence of GTP gamma S. In brush border membranes, the resistance to endo- and exo-genous proteolytic activity conferred by GTP gamma S was usually lower for RhoA than for Cdc42. Guanosine Triphosphate ras homolog family member A Rattus norvegicus
2 In addition, Cdc42 and RhoA associated with brush border membranes were largely resistant to increased proteolytic degradation induced by membrane treatment with the denaturing reagent urea as well as to added trypsin when incubated in the presence of GTP gamma S. In brush border membranes, the resistance to endo- and exo-genous proteolytic activity conferred by GTP gamma S was usually lower for RhoA than for Cdc42. Guanosine Triphosphate ras homolog family member A Rattus norvegicus
3 In addition, Cdc42 and RhoA associated with brush border membranes were largely resistant to increased proteolytic degradation induced by membrane treatment with the denaturing reagent urea as well as to added trypsin when incubated in the presence of GTP gamma S. In brush border membranes, the resistance to endo- and exo-genous proteolytic activity conferred by GTP gamma S was usually lower for RhoA than for Cdc42. Guanosine Triphosphate ras homolog family member A Rattus norvegicus
4 Taken together, these results suggest that the GTP gamma S-bound forms of Cdc42 and RhoA are maintained in a conformation that protects them from proteases found in many cell membranes. Guanosine Triphosphate ras homolog family member A Rattus norvegicus