QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

Vol. 18, Issue 6, 2090-2101, June 2007

This Article Full Text Full Text (PDF) Supplemental Material All Versions of this Article: E06-09-0883v1 18/6/2090    most recent Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Das, M. Articles by Verde, F. Search for Related Content PubMed PubMed Citation Articles by Das, M. Articles by Verde, F.

Regulation of Cell Diameter, For3p Localization, and Cell Symmetry by Fission Yeast Rho-GAP Rga4p

Maitreyi Das^*, David J. Wiley^*,, Saskia Medina, Helen A. Vincent, Michelle Larrea, Andrea Oriolo, and Fulvia Verde

Department of Molecular and Cellular Pharmacology, University of Miami Miller School of Medicine, Miami, FL 33101-1015

Submitted October 2, 2006; Revised February 21, 2007; Accepted March 13, 2007
Monitoring Editor: Fred Chang

Control of cellular dimensions and cell symmetry are critical for development and differentiation. Here we provide evidence that the putative Rho-GAP Rga4p of Schizosaccharomyces pombe controls cellular dimensions. rga4 cells are wider in diameter and shorter in length, whereas Rga4p overexpression leads to reduced diameter of the growing cell tip. Consistent with a negative role in cell growth control, Rga4p protein localizes to the cell sides in a "corset" pattern, and to the nongrowing cell tips. Additionally, rga4 cells show an altered growth pattern similar to that observed in mutants of the formin homology protein For3p. Consistent with these observations, Rga4p is required for normal localization of For3p and for normal distribution of the actin cytoskeleton. We show that different domains of the Rga4p protein mediate diverse morphological functions. The C-terminal GAP domain mediates For3p localization to the cell tips and maintains cell diameter. Conversely, overexpression of the N-terminal LIM homology domain of Rga4p promotes actin cable formation in a For3p-dependent manner. Our studies indicate that Rga4p functionally interacts with For3p and has a novel function in the control of cell diameter and cell growth.

The online version of this article contains supplemental material at MBC Online (http://www.molbiolcell.org).

* These authors contributed equally to this work.

Present address: Department of Microbiology and Immunology, University of Miami Miller School of Medicine, Miami, FL 33136.

Address correspondence to: Fulvia Verde (fverde{at}miami.edu)

Abbreviations used: GAP, GTPase-activating protein.

This article has been cited by other articles:

				S. Maerz, C. Ziv, N. Vogt, K. Helmstaedt, N. Cohen, R. Gorovits, O. Yarden, and S. Seiler The Nuclear Dbf2-Related Kinase COT1 and the Mitogen-Activated Protein Kinases MAK1 and MAK2 Genetically Interact to Regulate Filamentous Growth, Hyphal Fusion and Sexual Development in Neurospora crassa Genetics, July 1, 2008; 179(3): 1313 - 1325. [Abstract] [Full Text] [PDF]

				D. J. Wiley, P. Catanuto, F. Fontanesi, C. Rios, N. Sanchez, A. Barrientos, and F. Verde Bot1p Is Required for Mitochondrial Translation, Respiratory Function, and Normal Cell Morphology in the Fission Yeast Schizosaccharomyces pombe Eukaryot. Cell, April 1, 2008; 7(4): 619 - 629. [Abstract] [Full Text] [PDF]