Journal
MOLECULAR BIOLOGY OF THE CELL
Volume 17, Issue 3, Pages 1110-1125Publisher
AMER SOC CELL BIOLOGY
DOI: 10.1091/mbc.E05-08-0793
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Funding
- NIGMS NIH HHS [GM31006, R01 GM062392, GM62392, R01 GM031006, GM59216, R37 GM031006, R01 GM059216] Funding Source: Medline
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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.
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