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Vol. 13, Issue 8, 2869-2880, August 2002
Department of Biochemistry and Molecular Biology, State University
of New York (SUNY) Upstate Medical University, Syracuse, NY, 13210, and
*Wadsworth Center, New York State Department and Department of
Biological Sciences, School of Public Health, SUNY, Albany, NY, 12208
Saccharomyces cerevisiae adapts to osmotic stress
through the activation of a conserved high-osmolarity growth (HOG)
mitogen-activated protein (MAP) kinase pathway. Transmission through
the HOG pathway is very well understood, yet other aspects of the
cellular response to osmotic stress remain poorly understood, most
notably regulation of actin organization. The actin cytoskeleton
rapidly disassembles in response to osmotic insult and is induced to
reassemble only after osmotic balance with the environment is
reestablished. Here, we show that one of three MEK kinases of the HOG
pathway, Ssk2p, is specialized to facilitate actin cytoskeleton
reassembly after osmotic stress. Within minutes of cells' experiencing
osmotic stress or catastrophic disassembly of the actin cytoskeleton
through latrunculin A treatment, Ssk2p concentrates in the neck of
budding yeast cells and concurrently forms a 1:1 complex with actin.
These observations suggest that Ssk2p has a novel, previously
undescribed function in sensing damage to the actin cytoskeleton. We
also describe a second function for Ssk2p in facilitating reassembly of
a polarized actin cytoskeleton at the end of the cell cycle, a
prerequisite for efficient cell cycle completion. Loss of Ssk2p, its
kinase activity, or its ability to localize and interact with actin led
to delays in actin recovery and a resulting delay in cell cycle
completion. These unique capabilities of Ssk2p are activated by a novel
mechanism that does not involve known components of the HOG pathway.
Corresponding author. E-mail address:
ambergd{at}mail.upstate.edu.
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