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Vol. 11, Issue 1, 339-354, January 2000
Department of Molecular and Cell Biology, University of California,
Berkeley, California 94720-3202
Cdc42p, a Rho family GTPase of the Ras superfamily, is a key
regulator of cell polarity and morphogenesis in eukaryotes. Using 37 site-directed cdc42 mutants, we explored the functions
and interactions of Cdc42p in the budding yeast Saccharomyces
cerevisiae. Cytological and genetic analyses of these
cdc42 mutants revealed novel and diverse phenotypes,
showing that Cdc42p possesses at least two distinct essential functions
and acts as a nodal point of cell polarity regulation in vivo. In
addition, mapping the functional data for each cdc42
mutation onto a structural model of the protein revealed as
functionally important a surface of Cdc42p that is distinct from the
canonical protein-interacting domains (switch I, switch II, and the C
terminus) identified previously in members of the Ras superfamily. This
region overlaps with a region (
5-helix) recently predicted by
structural models to be a specificity determinant for Cdc42p-protein interactions.
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