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MBC in Press, published online ahead of print December 6, 2006
Mol. Biol. Cell 10.1091/mbc.E06-09-0776

A more recent version of this article appeared on February 1, 2007
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Submitted on September 1, 2006
Revised on November 20, 2006
Accepted on November 22, 2006

The Plasma Membrane Proteins Prm1 and Fig1 Ascertain Fidelity of Membrane Fusion during Yeast Mating

Pablo S. Aguilar,* Alex Engel,* and Peter Walter

Howard Hughes Medical Institute, and Department of Biochemistry and Biophysics, University of California at San Francisco, San Francisco, CA 94158

Monitoring Editor: Charles Boone

As for most cell-cell fusion events, the molecular details of membrane fusion during yeast mating are poorly understood. The multipass membrane protein Prm1 is the only known component that acts at the step of bilayer fusion. In its absence, mutant mating pairs lyse or arrest in the mating reaction with tightly apposed plasma membranes. We show that deletion of FIG 1, which controls pheromone-induced Ca2+ influx, yields similar cell fusion defects. While extracellular Ca2+ is not required for efficient cell fusion of wild type cells, cell fusion in prm1 mutant mating pairs is dramatically reduced when Ca2+ is removed. This enhanced fusion defect is due to lysis. Time-lapse microscopy reveals that fusion and lysis events initiate with identical kinetics, suggesting that both outcomes result from engagement of the fusion machinery. The yeast synaptotagmin ortholog and Ca2+ binding protein Tcb3 has a role in reducing lysis of prm1 mutants, which opens the possibility that the observed role of Ca2+ is to engage a wound-repair mechanism. Thus, our results suggest that Prm1 and Fig1 have a role in enhancing membrane fusion and maintaining its fidelity. Their absence results in frequent mating pair lysis, which is counteracted by Ca2+-dependent membrane repair.

*These authors contributed equally to this work.

Address correspondence to: Pablo S. Aguilar (pablo.aguilar{at}ucsf.edu)




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