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A more recent version of this article appeared on February 1, 2004
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Submitted on July 23, 2003
Revised on September 30, 2003
Accepted on October 1, 2003
1 Department of Biochemistry and Biophysics, University of California, San Francisco, San Francisco, California 94143-0448, Institute of Molecular Biology, 1229 University of Oregon, Eugene, OR 97403-1229
2 Department of Biochemistry and Biophysics, University of California, San Francisco, San Francisco, California 94143-0448
* Corresponding author. E-mail address: seanor{at}molbio.uoregon.edu.
The S. cerevisiae high osmolarity glycerol (HOG) MAPK pathway is required for osmoadaptation and contains two branches that activate a MAPK (Hog1) via a MAPKK (Pbs2). We have characterized the roles of common pathway components (Hog1 and Pbs2) and components in the two upstream branches (Ste11, Sho1, and Ssk1) in response to elevated osmolarity using whole-genome expression profiling. Several new features of the HOG pathway were revealed. First, Hog1 functions during gene induction and repression, cross talk inhibition, and in governing the regulatory period. Second, the phenotypes of pbs2 and hog1 mutants are identical, indicating that the sole role of Pbs2 is to activate Hog1. Third, the existence of genes whose induction is dependent on Hog1 and Pbs2 but not on Ste11 and Ssk1 suggests that there are additional inputs into Pbs2 under our inducing conditions. Fourth, the two upstream pathway branches are not redundant: the Sln1-Ssk1 branch has a much more prominent role than the Sho1-Ste11 branch for activation of Pbs2 by modest osmolarity. Finally, the general stress response pathway and both branches of the HOG pathway all function at high osmolarity. These studies demonstrate that cells respond to increased osmolarity using different signal transduction machinery under different conditions.
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