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A more recent version of this article appeared on March 1, 2005
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Submitted on May 24, 2004
Accepted on December 15, 2004
Department of Pharmacology and Cancer Biology, Duke University Medical Center, Durham, NC 27710
Monitoring Editor: Anthony Bretscher
In animal and fungal cells, the monomeric GTPase Cdc42p is a key regulator of cell polarity that itself exhibits a polarized distribution in asymmetric cells. Previous work showed that in budding yeast, Cdc42p polarization is unaffected by depolymerization of the actin cytoskeleton. Surprisingly, we now report that unlike complete actin depolymerization, partial actin depolymerization leads to the dispersal of Cdc42p from the polarization site in unbudded cells. We provide evidence that dispersal is due to endocytosis associated with cortical actin patches, and that actin cables are required to counteract the dispersal and maintain Cdc42p polarity. Thus, although Cdc42p is initially polarized in an actin-independent manner, maintaining that polarity may involve a reinforcing feedback between Cdc42p and polarized actin cables to counteract the dispersing effects of actin-dependent endocytosis. In addition, we report that once a bud has formed, polarized Cdc42p becomes more resistant to dispersal, revealing an unexpected difference between unbudded and budded cells in the organization of the polarization site.
Present address: Dept. of Molecular Biology, Massachusetts General Hospital, Harvard Medical Center, 50 Blossom St, 10 Wellman, Boston, MA 02114.
Corresponding author.
E-mail: daniel.lew{at}duke.edu