Title : GTP hydrolysis is not important for Ypt1 GTPase function in vesicular transport.

Pub. Date : 1998 Feb

PMID : 9447979






4 Functional Relationships(s)
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1 To test this idea, we inactivated the GTPase activity of Ypt1p by using the Q67L mutation, which targets a conserved residue that helps catalyze GTP hydrolysis in Ras. Guanosine Triphosphate RAB1A, member RAS oncogene family Homo sapiens
2 We demonstrate that the mutant Ypt1-Q67L protein is severely impaired in its ability to hydrolyze GTP both in the absence and in the presence of GAP and consequently is restricted mostly to the GTP-bound form. Guanosine Triphosphate RAB1A, member RAS oncogene family Homo sapiens
3 We demonstrate that the mutant Ypt1-Q67L protein is severely impaired in its ability to hydrolyze GTP both in the absence and in the presence of GAP and consequently is restricted mostly to the GTP-bound form. Guanosine Triphosphate RAB1A, member RAS oncogene family Homo sapiens
4 These results suggest that the function of Ypt1p in vesicular transport requires not only the GTP-bound form of the protein but also the interaction of Ypt1p with its GNEF. Guanosine Triphosphate RAB1A, member RAS oncogene family Homo sapiens