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Journal of Biochemistry Advance Access originally published online on July 24, 2009
Journal of Biochemistry 2009 146(5):705-712; doi:10.1093/jb/mvp116
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© The Authors 2009. Published by Oxford University Press on behalf of the Japanese Biochemical Society. All rights reserved

Importance of Polarisome Proteins in Reorganization of Actin Cytoskeleton at Low pH in Saccharomyces cerevisiae

Mitsuyoshi Motizuki* and Zhaojun Xu

Department of Biochemistry 2, Faculty of Medicine, University of Yamanashi, Chuo, Yamanashi 409-3898, Japan

*To whom correspondence should be addressed. Tel/Fax: +81-(55)-273-6784, E-mail: mitsum{at}yamanashi.ac.jp

Received March 10, 2009; Accepted July 10, 2009


  Abstract

The actin cytoskeleton of the yeast Saccharomyces cerevisiae can be altered rapidly in response to external cues. We reported previously that S. cerevisiae responds to low-pH stress by transiently depolarizing its actin cytoskeleton, and that this step requires a mitogen-activated protein kinase, high osmolarity glycerol 1 (Hog1p). This study further investigated the components involved in this actin reorganization at pH 3.0. Gene deletions on the Sln1p branch of the HOG pathway completely blocked actin depolarization, suggesting that Hog1p activation depends mainly on the osmosensor Sln1p. The protein-synthesis inhibitor cycloheximide did not influence the time course of actin depolarization, suggesting that the depolarization is a direct effect of the HOG pathway. Deletion of the scaffolding protein, Spa2p, or the Spa2p-interacting protein Pea2p, markedly inhibited the depolarization, and further deletion of the formin protein, Bni1p, notably delayed actin repolarization. Our results suggest the involvement of polarisome proteins, such as Spa2p, Pea2p and Bni1p, but not Bud6p, in Hog1p-dependent reorganization of the yeast actin cytoskeleton at low pH.

Key Words: actin cytoskeleton, Hog1, low pH, polarisome, Saccharomyces cerevisiae


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