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doi:10.1534/genetics.106.063370
A more recent version of this article appeared on April 1, 2007.
Originally published as Genetics Published Articles Ahead of Print on January 21, 2007.
REGULAR RESEARCH PAPERS |
Requirement for the Polarisome and Formin Function in Ssk2p-mediated Actin Recovery From Osmotic Stress in Saccharomyces cerevisiae
Blaine T Bettinger 1, Michael G. Clark 1 and David C Amberg 1*
1 SUNY Upstate Medical University
* To whom correspondence should be addressed. E-mail: ambergd{at}upstate.edu.
Submitted on July 14, 2006
Revised on August 15, 2006
Accepted on 8 January 2007
Osmotic stress induces activation of an adaptive mitogen-activated protein kinase pathway in concert with disassembly of the actin cytoskeleton by a mechanism that is not understood. We have previously shown that the conserved actin-interacting MAP kinase kinase kinase Ssk2p/MEKK4, a member of the high osmolarity glycerol (HOG) MAPK pathway of Saccharomyces cerevisiae, mediates recovery of the actin cytoskeleton following osmotic stress. In this study, we have employed in vitro kinase assays to show that Ssk2p kinase activity is activated for the actin recovery pathway via a non-canonical, Ssk1p-independent mechanism. Our work also shows that Ssk2p requires the polarisome proteins Bud6p and Pea2p to promote efficient, polarized actin re-assembly but that this requirement can be bypassed by overexpression of Ssk2p. Formin (BNI1 or BNR1) and tropomyosin functions are also required for actin recovery but unlike for Bud6p and Pea2p, these requirements cannot be bypassed by overexpression of Ssk2p. These results suggest that Ssk2p acts downstream of Bud6p and Pea2p and upstream of tropomyosin to drive actin recovery, possibly by up-regulating the actin nucleation activity of the formins.
Key Words: MEKK4, Ssk2, actin, formins, osmotic stress
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