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Published online 16 June 2003. doi:10.1083/jcb.200212040
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© The Rockefeller University Press, 0021-9525/2003/6/1081 $5.00
The Journal of Cell Biology, Volume 161, Number 6, 1081-1092

Article

 Formin-dependent actin assembly is regulated by distinct modes of Rho signaling in yeast

Yuqing Dong, David Pruyne and Anthony Bretscher

Department of Molecular Biology and Genetics, Cornell University, Ithaca, NY 14853

Address correspondence to Anthony Bretscher, Department of Molecular Biology and Genetics, Cornell University, 353 Biotechnology Building, Ithaca, NY. Tel.: (607) 255-5713. Fax: (607) 255-6249. E-mail: apb5{at}cornell.edu

Formins are actin filament nucleators regulated by Rho-GTPases. In budding yeast, the formins Bni1p and Bnr1p direct the assembly of actin cables, which guide polarized secretion and growth. From the six yeast Rho proteins (Cdc42p and Rho1–5p), we have determined that four participate in the regulation of formin activity. We show that the essential function of Rho3p and Rho4p is to activate the formins Bni1p and Bnr1p, and that activated alleles of either formin are able to bypass the requirement for these Rho proteins. Through a separate signaling pathway, Rho1p is necessary for formin activation at elevated temperatures, acting through protein kinase C (Pkc1p), the major effector for Rho1p signaling to the actin cytoskeleton. Although Pkc1p also activates a MAPK pathway, this pathway does not function in formin activation. Formin-dependent cable assembly does not require Cdc42p, but in the absence of Cdc42p function, cable assembly is not properly organized during initiation of bud growth. These results show that formin function is under the control of three distinct, essential Rho signaling pathways.

Key Words: actin; polarity; Cdc42; PKC; MAPK

* Abbreviations used in this paper: DAD, Dia autoregulatory domain; FH, formin homology; RBD, Rho-binding domain.


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