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Vol. 17, Issue 3, 1306-1321, March 2006
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Department of Medical Genetics and Microbiology, Banting and Best Department of Medical Research, University of Toronto, Toronto, Ontario, Canada M5S 1A8
Submitted June 1, 2005;
Revised December 13, 2005;
Accepted December 27, 2005
Monitoring Editor: David Drubin
We have used comprehensive synthetic lethal screens and biochemical assays to examine the biological role of the yeast amphiphysin homologues Rvs161p and Rvs167p, two proteins that play a role in regulation of the actin cytoskeleton, endocytosis, and sporulation. We found that unlike some forms of amphiphysin, Rvs161p-Rvs167p acts as an obligate heterodimer during vegetative growth and neither Rvs161p nor Rvs167p forms a homodimer in vivo. RVS161 and RVS167 have an identical set of 49 synthetic lethal interactions, revealing functions for the Rvs proteins in cell polarity, cell wall synthesis, and vesicle trafficking as well as a shared role in mating. Consistent with these roles, we show that the Rvs167p-Rvs161p heterodimer, like its amphiphysin homologues, can bind to phospholipid membranes in vitro, suggesting a role in vesicle formation and/or fusion. Our genetic screens also reveal that the interaction between Abp1p and the Rvs167p Src homology 3 (SH3) domain may be important under certain conditions, providing the first genetic evidence for a role for the SH3 domain of Rvs167p. Our studies implicate heterodimerization of amphiphysin family proteins in various functions related to cell polarity, cell integrity, and vesicle trafficking during vegetative growth and the mating response.
* These authors contributed equally to this work.
Present address: PSF Biotech AG, Heubnerweg 6, Gebäude D, D-14059 Berlin, Germany
Present address: Samuel Lunenfeld Research Institute, Mount Sinai Hospital, Toronto, Ontario, Canada M5G 1X5.
Address correspondence to: Brenda Andrews (brenda.andrews{at}utoronto.ca).
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