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Vol. 12, Issue 6, 1541-1555, June 2001
Department of Molecular Biology and Genetics, Cornell University,
Ithaca, New York 14853
Polarized growth in yeast requires cooperation between the
polarized actin cytoskeleton and delivery of post-Golgi secretory vesicles. We have previously reported that loss of the major
tropomyosin isoform, Tpm1p, results in cells sensitive to perturbations
in cell polarity. To identify components that bridge these processes, we sought mutations with both a conditional defect in secretion and a
partial defect in polarity. Thus, we set up a genetic screen for
mutations that conferred a conditional growth defect, showed synthetic
lethality with tpm1
, and simultaneously became denser at the restrictive temperature, a hallmark of secretion-defective cells. Of the 10 complementation groups recovered, the group with the
largest number of independent isolates was functionally null alleles of
RAS2. Consistent with this, ras2 and
tpm1 are synthetically lethal at 35°C. We show that
ras2 confers temperature-sensitive growth and
temperature-dependent depolarization of the actin cytoskeleton. Furthermore, we show that at elevated temperatures
ras2 cells are partially defective in endocytosis and
show a delocalization of two key polarity markers, Myo2p and Cdc42p.
However, the conditional enhanced density phenotype of
ras2 cells is not a defect in secretion. All the
phenotypes of ras2 cells can be fully suppressed by
expression of yeast RAS1 or RAS2 genes,
human Ha-ras, or the double disruption of the stress response genes
msn2msn4. Although the best
characterized pathway of Ras function in yeast involves activation of
the cAMP-dependent protein kinase A pathway, activation of the protein
kinase A pathway does not fully suppress the actin polarity defects,
suggesting that there is an additional pathway from Ras2p to Msn2/4p.
Thus, Ras2p regulates cytoskeletal polarity in yeast under conditions of mild temperature stress through the stress response pathway.
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