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J Biol Chem, Vol. 274, Issue 24, 16861-16870, June 11, 1999
From the Department of Microbiology and Molecular Genetics and the
Markey Center for Molecular Genetics, University of Vermont,
Burlington, Vermont 05405
The Cdc42p GTPase is involved in the signal
transduction cascades controlling bud emergence and polarized cell
growth in S. cerevisiae. Cells expressing the
cdc42V44A effector domain mutant allele
displayed morphological defects of highly elongated and multielongated
budded cells indicative of a defect in the apical-isotropic switch in
bud growth. In addition, these cells contained one, two, or multiple
nuclei indicative of a G2/M delay in nuclear division and
also a defect in cytokinesis and/or cell separation. Actin and chitin
were delocalized, and septin ring structure was aberrant and partially
delocalized to the tips of elongated cdc42V44A
cells; however, Cdc42V44Ap localization was normal.
Two-hybrid protein analyses showed that the V44A mutation interfered
with Cdc42p's interactions with Cla4p, a
p21(Cdc42/Rac)-activated kinase (PAK)-like kinase, and the
novel effectors Gic1p and Gic2p, but not with the Ste20p or Skm1p
PAK-like kinases, the Bni1p formin, or the Iqg1p IQGAP homolog. Furthermore, the cdc42V44A morphological
defects were suppressed by deletion of the Swe1p cyclin-dependent
kinase inhibitory kinase and by overexpression of Cla4p, Ste20p, the
Cdc12 septin protein, or the guanine nucleotide exchange factor Cdc24p.
In sum, these results suggest that proper Cdc42p function is essential
for timely progression through the apical-isotropic switch and
G2/M transition and that Cdc42V44Ap
differentially interacts with a number of effectors and regulators.
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