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Vol. 17, Issue 3, 1110-1125, March 2006
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* Department of Cell and Developmental Biology, University of Pennsylvania School of Medicine, Philadelphia, PA 19104-6058;
Department of Biochemistry and Molecular Biology, Oklahoma State University, Stillwater, OK 74078-3035;
Department of Biotechnology, Korea University, Yeongi-gun, Chungcheongnam-do 339-700, Korea;
Department of Biochemistry and Molecular Biology, SUNY Upstate Medical University, Syracuse, NY 13210; and
|| Department of Biology and Program in Molecular Biology and Biotechnology, University of North Carolina, Chapel Hill, NC 27599-3280
Submitted August 24, 2005;
Revised December 1, 2005;
Accepted December 2, 2005
Monitoring Editor: Anthony Bretscher
The septins are GTP-binding, filament-forming proteins that are involved in cytokinesis and other processes. In the yeast Saccharomyces cerevisiae, the septins are recruited to the presumptive bud site at the cell cortex, where they form a ring through which the bud emerges. We report here that in wild-type cells, the septins typically become detectable in the vicinity of the bud site several minutes before ring formation, but the ring itself is the first distinct structure that forms. Septin recruitment depends on activated Cdc42p but not on the normal pathway for bud-site selection. Recruitment occurs in the absence of F-actin, but ring formation is delayed. Mutant phenotypes and suppression data suggest that the Cdc42p effectors Gic1p and Gic2p, previously implicated in polarization of the actin cytoskeleton, also function in septin recruitment. Two-hybrid, in vitro protein binding, and coimmunoprecipitation data indicate that this role involves a direct interaction of the Gic proteins with the septin Cdc12p.
The online version of this article contains supplemental material at MBC Online (http://www.molbiolcell.org).
Address correspondence to: Erfei Bi (ebi{at}mail.med.upenn.edu).
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