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Vol. 11, Issue 2, 773-793, February 2000
*Department of Biology and Program in Molecular Biology and
Biotechnology, University of North Carolina, Chapel Hill, North
Carolina 27599; and §Section of Molecular Genetics and
Microbiology and Institute for Cellular and Molecular Biology,
University of Texas, Austin, Texas 78712
In the yeast Saccharomyces cerevisiae, Cdc24p
functions at least in part as a guanine-nucleotide-exchange factor for
the Rho-family GTPase Cdc42p. A genetic screen designed to identify
possible additional targets of Cdc24p instead identified two previously known genes, MSB1 and CLA4, and one novel
gene, designated MSB3, all of which appear to function
in the Cdc24p-Cdc42p pathway. Nonetheless, genetic evidence suggests
that Cdc24p may have a function that is distinct from its Cdc42p
guanine-nucleotide-exchange factor activity; in particular,
overexpression of CDC42 in combination with
MSB1 or a truncated CLA4 in cells
depleted for Cdc24p allowed polarization of the actin cytoskeleton and
polarized cell growth, but not successful cell proliferation.
MSB3 has a close homologue (designated
MSB4) and two more distant homologues
(MDR1 and YPL249C) in S.
cerevisiae and also has homologues in
Schizosaccharomyces pombe, Drosophila
(pollux), and humans (the oncogene
tre17). Deletion of either MSB3 or
MSB4 alone did not produce any obvious phenotype, and
the msb3 msb4 double mutant was viable. However, the
double mutant grew slowly and had a partial disorganization of the
actin cytoskeleton, but not of the septins, in a fraction of cells that were larger and rounder than normal. Like Cdc42p, both Msb3p and Msb4p
localized to the presumptive bud site, the bud tip, and the mother-bud
neck, and this localization was Cdc42p dependent. Taken together, the
data suggest that Msb3p and Msb4p may function redundantly downstream
of Cdc42p, specifically in a pathway leading to actin organization.
From previous work, the BNI1, GIC1, and GIC2 gene products also appear to be involved in linking
Cdc42p to the actin cytoskeleton. Synthetic lethality and multicopy
suppression analyses among these genes, MSB, and
MSB4, suggest that the linkage is accomplished by two
parallel pathways, one involving Msb3p, Msb4p, and Bni1p, and the other
involving Gic1p and Gic2p. The former pathway appears to be more
important in diploids and at low temperatures, whereas the latter
pathway appears to be more important in haploids and at high temperatures.
Present addresses:
Department of Cell and Developmental Biology, University of
Pennsylvania, Philadelphia, PA 19104-6058;
School of
Medicine, University of North Carolina, Chapel Hill, NC 27599.
Corresponding author. E-mail address:
jpringle{at}emailunc.edu.
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