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Adjacent positioning of cellular structures enabled by a Cdc42 GTPase-activating protein–mediated zone of inhibition
Zongtian Tong1, Xiang-Dong Gao1,2, Audrey S. Howell3, Indrani Bose3, Daniel J. Lew3, and Erfei Bi1
1 Department of Cell and Developmental Biology, University of Pennsylvania School of Medicine, Philadelphia, PA 19104
2 State Key Laboratory of Virology, College of Life Sciences, Wuhan University, Wuhan 430072, China
3 Department of Pharmacology and Cancer Biology, Duke University Medical Center, Durham, NC 27710
Correspondence to E. Bi: Cells of the budding yeast Saccharomyces cerevisiae are born carrying localized transmembrane landmark proteins that guide the subsequent establishment of a polarity axis and hence polarized growth to form a bud in the next cell cycle. In haploid cells, the relevant landmark proteins are concentrated at the site of the preceding cell division, to which they recruit Cdc24, the guanine nucleotide exchange factor for the conserved polarity regulator Cdc42. However, instead of polarizing at the division site, the new polarity axis is directed next to but not overlapping that site. Here, we show that the Cdc42 guanosine triphosphatase–activating protein (GAP) Rga1 establishes an exclusion zone at the division site that blocks subsequent polarization within that site. In the absence of localized Rga1 GAP activity, new buds do in fact form within the old division site. Thus, Cdc42 activators and GAPs establish concentric zones of action such that polarization is directed to occur adjacent to but not within the previous cell division site.
Abbreviations used in this paper: GAP, GTPase-activating protein; GEF, guanine nucleotide exchange factor; PBD, p21 binding domain; SEM, scanning EM.
