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Science 24 May 2002:
Vol. 296. no. 5572, pp. 1483 - 1486
DOI: 10.1126/science.1070540
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Reports

Regulation of MAPK Function by Direct Interaction with the Mating-Specific Galpha in Yeast

Metodi V. Metodiev,1 Dina Matheos,2 Mark D. Rose,2 David E. Stone1*

The mating response of the budding yeast Saccharomyces cerevisiae is mediated by a prototypical heterotrimeric GTP-binding protein (G protein) and mitogen-activated protein kinase (MAPK) cascade. Although signal transmission by such pathways has been modeled in detail, postreceptor down-regulation is less well understood. The pheromone-responsive G protein alpha  subunit (Galpha ) of yeast down-regulates the mating signal, but its targets are unknown. We have found that Galpha binds directly to the mating-specific MAPK in yeast cells responding to pheromone. This interaction contributes both to modulation of the mating signal and to the chemotropic response, and it demonstrates direct communication between the top and bottom of a Galpha -MAPK pathway.

1 Department of Biological Sciences, Laboratory for Molecular Biology, University of Illinois at Chicago, 900 South Ashland Avenue (M/C 567), Chicago, IL 60607, USA.
2 Princeton University, Department of Molecular Biology, Princeton, NJ 08544, USA.
*   To whom correspondence should be addressed. E-mail: dstone{at}uic.edu

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THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
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Eukaryot. Cell 4, 495-503
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Dominant-negative Inhibition of Pheromone Receptor Signaling by a Single Point Mutation in the G Protein {alpha} Subunit.
Y.-L. Wu, S. B. Hooks, T. K. Harden, and H. G. Dohlman (2004)
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Pheromone-induced polarization is dependent on the Fus3p MAPK acting through the formin Bni1p.
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G{beta}{gamma} Recruits Rho1 to the Site of Polarized Growth during Mating in Budding Yeast.
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