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Originally published as MBoC in Press, 10.1091/mbc.E09-01-0069 on April 22, 2009

Vol. 20, Issue 12, 2820-2830, June 15, 2009

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The Mating-specific G{alpha} Interacts with a Kinesin-14 and Regulates Pheromone-induced Nuclear Migration in Budding Yeast

Sofia V. Zaichick*,{dagger},{ddagger}, Metodi V. Metodiev*,{dagger},§, Scott A. Nelson{dagger},||, Oleksii Durbrovskyi*, Edward Draper*, John A. Cooper||, and David E. Stone*

*Laboratory for Molecular Biology, Department of Biological Sciences, University of Illinois at Chicago, Chicago, IL 60607; and ||Department of Cell Biology and Physiology, Washington University in St. Louis, St. Louis, MO 63110

Submitted January 23, 2009; Revised April 8, 2009; Accepted April 14, 2009
Monitoring Editor: Daniel J. Lew

InCytes from MBC

As a budding yeast cell elongates toward its mating partner, cytoplasmic microtubules connect the nucleus to the cell cortex at the growth tip. The Kar3 kinesin-like motor protein is then thought to stimulate plus-end depolymerization of these microtubules, thus drawing the nucleus closer to the site where cell fusion and karyogamy will occur. Here, we show that pheromone stimulates a microtubule-independent interaction between Kar3 and the mating-specific G{alpha} protein Gpa1 and that Gpa1 affects both microtubule orientation and cortical contact. The membrane localization of Gpa1 was found to polarize early in the mating response, at about the same time that the microtubules begin to attach to the incipient growth site. In the absence of Gpa1, microtubules lose contact with the cortex upon shrinking and Kar3 is improperly localized, suggesting that Gpa1 is a cortical anchor for Kar3. We infer that Gpa1 serves as a positional determinant for Kar3-bound microtubule plus ends during mating.


This article was published online ahead of print in MBC in Press (http://www.molbiolcell.org/cgi/doi/10.1091/mbc.E09-01-0069) on April 22, 2009.

{dagger} These authors contributed equally to this work.

Present addresses: {ddagger} Department of Microbiology and Immunology, Northwestern University, 303 East Chicago Ave., Chicago, IL 60611;

§ Department of Biological Sciences, University of Essex, Wivenhoe Park, Colchester, Essex CO4 3SQ, United Kingdom;

Department of Pharmacology, Loyola University Medical School, Maywood, IL 60153.

Address correspondence to: David E. Stone (dstone{at}uic.edu)


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