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J. Biol. Chem., Vol. 277, Issue 25, 22156-22167, June 21, 2002
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From the All members of the regulator
of G protein signaling (RGS) family contain a conserved core domain
that can accelerate G protein GTPase activity. The RGS in yeast, Sst2,
can inhibit a G protein signal leading to mating. In addition, some RGS
proteins contain an N-terminal domain of unknown function. Here we use
complementary whole genome analysis methods to investigate the function
of the N-terminal Sst2 domain. To identify a signaling pathway
regulated by N-Sst2, we performed genome-wide transcription profiling
of cells expressing this fragment alone and found differences in 53 transcripts. Of these, 40 are induced by N-Sst2, and nearly all contain
a stress response element (STRE) in the promoter region. To identify
components of a signaling pathway leading from N-Sst2 to STREs, we
performed a genome-wide two-hybrid analysis using N-Sst2 as bait and
found 17 interacting proteins. To identify the functionally relevant
interacting proteins, we analyzed all of the available gene deletion
mutants and found three (vps36
Regulation of Stress Response Signaling by the N-terminal
Dishevelled/EGL-10/Pleckstrin Domain of Sst2, a Regulator of G
Protein Signaling in Saccharomyces cerevisiae*
§,¶,
,,,,¶
Department of Pharmacology, Yale University
School of Medicine, New Haven, Connecticut 06536, Neuroscience
Research, Wyeth Ayerst-Research, CN 8000, Princeton, New Jersey
08543-8000, and the ** Departments of Genetics and Medicine
and §§ Howard Hughes Medical Institute,
University of Washington, Seattle, Washington 98195
, pep12,
and tlg2) that induce STRE and also repress
pheromone-dependent transcription. We selected
VPS36 for further characterization. A vps36
mutation diminishes signaling by pheromone as well as by downstream
components including the G protein, effector kinase (Ste11), and
transcription factor (Ste12). Conversely, overexpression of Vps36
enhances the pheromone response in sst2 cells but not in
wild type. These findings indicate that Vps36 and Sst2 have opposite
and opposing effects on the pheromone and stress response pathways,
with Vps36 acting downstream of the G protein and independently of Sst2
RGS activity.
*
This work was supported by a pilot grant from the Claude D. Pepper Center of Yale University (to S. A. B.) and National
Institutes of Health Grants P41 RR11823 (to S. F.) and GM55316 and
GM59167 (to H. G. D.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Present address: Institut für Genetik, Forschungszentrum
Karlsruhe, PO Box 3640, D-76021 Karlsruhe, Germany.
¶¶
An Investigator of the Howard Hughes Medical Institute.
An Established Investigator of the American Heart
Association. To whom correspondence should be addressed: Dept. of
Biochemistry and Biophysics, University of North Carolina at Chapel
Hill, 405 Mary Ellen Jones Bldg., Campus Box 7260, Chapel Hill, NC
27599-2852. Tel.: 919-843-6894; Fax: 919-966-2852; E-mail:
henrik_dohlman@med.unc.edu.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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