This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Tcheperegine, S. E.
Right arrow Articles by Bi, E.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Tcheperegine, S. E.
Right arrow Articles by Bi, E.

 Previous Article  |  Next Article 

Molecular and Cellular Biology, October 2005, p. 8567-8580, Vol. 25, No. 19
0270-7306/05/$08.00+0     doi:10.1128/MCB.25.19.8567-8580.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Regulation of Cell Polarity by Interactions of Msb3 and Msb4 with Cdc42 and Polarisome Components

Serguei E. Tcheperegine, Xiang-Dong Gao, and Erfei Bi*

Department of Cell and Developmental Biology, University of Pennsylvania School of Medicine, Philadelphia, Pennsylvania 19104

Received 7 January 2005/ Returned for modification 4 March 2005/ Accepted 14 July 2005

In Saccharomyces cerevisiae, polarized growth depends on interactions between the actin cytoskeleton and the secretory machinery. Here we show that the Rab GTPase-activating proteins (GAPs) Msb3 and Msb4 interact directly with Spa2, a scaffold protein of the "polarisome" that also interacts with the formin Bni1. Spa2 is required for the polarized localization of Msb3 and Msb4 at the bud tip. We also show that Msb3 and Msb4 bind specifically to Cdc42-GDP and Rho1-GDP in vitro and that Msb3 and Rho GDP dissociation inhibitor act independently but oppositely on Cdc42. Finally, we show that Msb3 and Msb4 are involved in Bni1-nucleated actin assembly in vivo. These results suggest that Msb3 and Msb4 regulate polarized growth by multiple mechanisms, directly regulating exocytosis through their GAP activity toward Sec4 and potentially coordinating the functions of Cdc42, Rho1, and Bni1 in the polarisome through their binding to these GTPases. A functional equivalent of the polarisome probably exists in other fungi and mammals.


* Corresponding author. Mailing address: Department of Cell and Developmental Biology, University of Pennsylvania School of Medicine, 421 Curie Blvd., Room 1012, BRB II/III, Philadelphia, PA 19104-6058. Phone: (215) 573-6676. Fax: (215) 898-9871. E-mail: ebi{at}mail.med.upenn.edu.


Molecular and Cellular Biology, October 2005, p. 8567-8580, Vol. 25, No. 19
0022-538X/05/$08.00+0     doi:10.1128/MCB.25.19.8567-8580.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.




This article has been cited by other articles:

  • Tiedje, C., Sakwa, I., Just, U., Hofken, T. (2008). The Rho GDI Rdi1 Regulates Rho GTPases by Distinct Mechanisms. Mol. Biol. Cell 19: 2885-2896 [Abstract] [Full Text]  
  • Juanes, M. A., Queralt, E., Bano, M. C., Igual, J. C. (2007). Rot1 plays an antagonistic role to Clb2 in actin cytoskeleton dynamics throughout the cell cycle. J. Cell Sci. 120: 2390-2401 [Abstract] [Full Text]  
  • Buttery, S. M., Yoshida, S., Pellman, D. (2007). Yeast Formins Bni1 and Bnr1 Utilize Different Modes of Cortical Interaction during the Assembly of Actin Cables. Mol. Biol. Cell 18: 1826-1838 [Abstract] [Full Text]  
  • Park, H.-O., Bi, E. (2007). Central Roles of Small GTPases in the Development of Cell Polarity in Yeast and Beyond. Microbiol. Mol. Biol. Rev. 71: 48-96 [Abstract] [Full Text]