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Comment
. 2003 Dec;5(12):1048-9.
doi: 10.1038/ncb1203-1048.

Go ahead, break my symmetry!

Kendall J Blumer, John A Cooper
Comment

Go ahead, break my symmetry!

Kendall J Blumer et al. Nat Cell Biol. 2003 Dec.

Abstract

Work in this issue advances our understanding of how the small G protein Cdc42 functions to polarize budding yeast. Remarkably, Cdc42 can polarize in the absence of upstream cues or positive feedback from the cytoskeleton. Polarization requires the scaffold protein Bem1 and cycling of Cdc42 between its GTP- and GDP-bound states.

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Figures

Figure 1
Figure 1
Symmetry breaking by Cdc42. In the absence of upstream polarity cues, Cdc42 associates with assorted proteins, including a scaffold, a GEF, a GTPase-activating protein (GAP) and an effector, to form a multisubunit complex. Next, the complex assembles into a polymer, a process driven by GTP/GDP cycling of Cdc42. One polymer forms, and its location establishes the new bud site.
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