Molecular Biology of the Cell track citations

Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
QUICK SEARCH:   [advanced]


     

Originally published as MBC in Press, 10.1091/mbc.E07-07-0718 on February 6, 2008

Vol. 19, Issue 4, 1727-1738, April 2008

This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Supplemental Materials
Right arrow All Versions of this Article:
E07-07-0718v1
19/4/1727    most recent
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Related articles in Mol. Biol. Cell
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 arrow reprints & permissions
Google Scholar
Right arrow Articles by Pinar, M.
Right arrow Articles by Pérez, P.
PubMed
Right arrow PubMed Citation
Right arrow Articles by Pinar, M.
Right arrow Articles by Pérez, P.

Schizosaccharomyces pombe Pxl1 Is a Paxillin Homologue That Modulates Rho1 Activity and Participates in Cytokinesis

Mario Pinar, Pedro M. Coll, Sergio A. Rincón, and Pilar Pérez

Instituto de Microbiología Bioquímica, Consejo Superior de Investigaciones Científicas/Departamento de Microbiología y Genética, Universidad de Salamanca, Edificio Departamental, 37007 Salamanca, Spain

Submitted July 28, 2007; Revised January 17, 2008; Accepted January 29, 2008
Monitoring Editor: Daniel Lew

InCytes from MBC

Schizosaccharomyces pombe Rho GTPases regulate actin cytoskeleton organization and cell integrity. We studied the fission yeast gene SPBC4F6.12 based on its ability to suppress the thermosensitivity of cdc42-1625 mutant strain. This gene, named pxl1+, encodes a protein with three LIM domains that is similar to paxillin. Pxl1 does not interact with Cdc42 but it interacts with Rho1, and it negatively regulates this GTPase. Fission yeast Pxl1 forms a contractile ring in the cell division region and deletion of pxl1+ causes a delay in cell–cell separation, suggesting that it has a function in cytokinesis. Pxl1 N-terminal region is required and sufficient for its localization to the medial ring, whereas the LIM domains are necessary for its function. Pxl1 localization requires actin polymerization and the actomyosin ring, but it is independent of the septation initiation network (SIN) function. Moreover, Pxl1 colocalizes and interacts with Myo2, and Cdc15, suggesting that it is part of the actomyosin ring. Here, we show that in cells lacking Pxl1, the myosin ring is not correctly assembled and that actomyosin ring contraction is delayed. Together, these data suggest that Pxl1 modulates Rho1 GTPase signaling and plays a role in the formation and contraction of the actomyosin ring during cytokinesis.

This was published online ahead of print in MBC in Press (http://www.molbiolcell.org/cgi/doi/10.1091/mbc.E07-07-0718) on February 6, 2008.

Address correspondence to: Pilar Pérez (piper{at}gugu.usal.es)


Related articles in Mol. Biol. Cell:

InCytes from MBC, April 2008

Mol. Biol. Cell 2008 19: 1281. [PDF]  





Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
Copyright © 2008 by The American Society for Cell Biology. Terms of copyright protection, warranties, and disclaimers.