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© The Rockefeller University Press, 0021-9525/1998//567 $5.00
The Journal of Cell Biology, Volume 141, Number 3, , 1998 567-584

Articles

Rvs161p Interacts with Fus2p to Promote Cell Fusion in Saccharomyces cerevisiae



Valeria Brizzio, Alison E. Gammie, and Mark D. Rose

Department of Molecular Biology, Princeton University, Princeton, New Jersey 08544-1014

FUS7 was previously identified by a mutation that causes a defect in cell fusion in a screen for bilateral mating defects. Here we show that FUS7 is allelic to RVS161/END6, a gene implicated in a variety of processes including viability after starvation, endocytosis, and actin cytoskeletal organization. Two lines of evidence indicate that RVS161/END6's endocytic function is not required for cell fusion. First, several other endocytic mutants showed no cell fusion defects. Second, we isolated five function-specific alleles of RVS161/FUS7 that were defective for endocytosis, but not mating, and three alleles that were defective for cell fusion but not endocytosis. The organization of the actin cytoskeleton was normal in the cell fusion mutants, indicating that Rvs161p's function in cell fusion is independent of actin organization. The three to fourfold induction of RVS161 by mating pheromone and the localization of Rvs161p-GFP to the cell fusion zone suggested that Rvs161p plays a direct role in cell fusion. The phenotypes of double mutants, the coprecipitation of Rvs161p and Fus2p, and the fact that the stability of Fus2p was strongly dependent on Rvs161p's mating function lead to the conclusion that Rvs161p is required to interact with Fus2p for efficient cell fusion.

Abbreviations used in this paper: 5-FOA, 5-fluoro-orotic acid medium; DIC, differential interference contrast; cM, centiMorgans; GST, glutathione-S-transferase; LY, Lucifer yellow; MAP, mitogen-activated protein; YEPD, yeast extract/peptone/dextrose; YPG, yeast extract/peptone/ glycerol.

This research was supported by the National Institutes of Health grant to M.D. Rose (GM37739). V. Brizzio was supported by an institutional National Institutes of Health training Grant on genetics, Cell, and Molecular Biology. A.E. Gammie was partially supported by a Fellowship from the Jane Coffin Child Memorial Fund for Cancer Research.

Address all correspondence to Mark D. Rose, Department of Molecular Biology, Princeton University, Princeton, New Jersey 08544-1014. Tel.: 609-258-2804; Fax: 609-258-6175; E-mail: mrose{at}molbio.princeton.edu


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