Opposing roles for actin in Cdc42p polarization.
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 (Ayscough et al., J. Cell Biol. 137, 399-416, 1997). 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.
Irazoqui
Javier E
JE
Department of Pharmacology and Cancer Biology, Duke University Medical Center, Durham, NC 27710, USA.
Howell
Audrey S
AS
Theesfeld
Chandra L
CL
Lew
Daniel J
DJ
D000199:Actins / Q000737:chemistry* / Q000502:physiology*; D001665:Binding Sites; D003599:Cytoskeleton / Q000378:metabolism; D004705:Endocytosis; D005838:Genotype; D008856:Microscopy, Fluorescence; D008954:Models, Biological; D009154:Mutation; D011485:Protein Binding; D012441:Saccharomyces cerevisiae / Q000378:metabolism / Q000502:physiology*; D013696:Temperature; D013997:Time Factors; D020764:cdc42 GTP-Binding Protein / Q000737:chemistry*
D000199:Actins; D020764:cdc42 GTP-Binding Protein