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

Vol. 19, Issue 5, 2208-2219, May 2008

This Article Full Text Full Text (PDF) Supplemental Materials All Versions of this Article: E07-07-0731v1 19/5/2208    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 Yonetani, A. Articles by Chang, F. Search for Related Content PubMed PubMed Citation Articles by Yonetani, A. Articles by Chang, F.

Regulation and Targeting of the Fission Yeast Formin cdc12p in Cytokinesis

Ann Yonetani^*, Raymond J. Lustig^*,, James B. Moseley^,, Tetsuya Takeda^*,||, Bruce L. Goode, and Fred Chang^*

*Department of Microbiology, Columbia University College of Physicians and Surgeons, New York, NY 10032; and Department of Biology and Rosenstiel Basic Medical Sciences Research Center, Brandeis University, Waltham, MA 02454

Submitted July 31, 2007; Revised February 13, 2008; Accepted February 19, 2008
Monitoring Editor: David Drubin

Formins are conserved actin nucleators which promote the assembly of actin filaments for the formation of diverse actin structures. In fission yeast Schizosaccharomyces pombe, the formin cdc12p is required specifically in assembly of the actin-based contractile ring during cytokinesis. Here, using a mutational analysis of cdc12p, we identify regions of cdc12p responsible for ring assembly and localization. Profilin-binding residues of the FH1 domain regulate actin assembly and processive barbed-end capping by the FH2 domain. Studies using photobleaching (FRAP) and sensitivity to latrunculin A treatment show that profilin binding modulates the rapid dynamics of actin and cdc12p within the ring in vivo. Visualized by functional GFP-fusion constructs expressed from the endogenous promoter, cdc12p appears in a small number of cytoplasmic motile spot structures that deliver the formin to the ring assembly site, without detectable formation of an intermediate band of "nodes." The FH3/DID region directs interphase spot localization, while an N-terminal region and the FH1-FH2 domains of cdc12p can target its localization to the ring. Mutations in putative DID and DAD regions do not alter regulation, suggesting that cdc12p is not regulated by a canonical autoinhibition mechanism. Our findings provide insights into the regulation of formin activity and the mechanisms of contractile ring dynamics and assembly.

Present addresses: Rockefeller University, 1230 York Avenue, New York, NY 10065;

^|| Department of Genetics, University of Cambridge, Downing Street, Cambridge, CB2 3EH, United Kingdom;

Julliard School, Lincoln Center, New York, NY 10023.

Address correspondence to: Fred Chang (fc99{at}columbia.edu)

This article has been cited by other articles:

				C. T. Skau, E. M. Neidt, and D. R. Kovar Role of Tropomyosin in Formin-mediated Contractile Ring Assembly in Fission Yeast Mol. Biol. Cell, April 15, 2009; 20(8): 2160 - 2173. [Abstract] [Full Text] [PDF]

				Y. Huang, H. Yan, and M. K. Balasubramanian Assembly of normal actomyosin rings in the absence of Mid1p and cortical nodes in fission yeast J. Cell Biol., December 15, 2008; 183(6): 979 - 988. [Abstract] [Full Text] [PDF]

				R. H. Roberts-Galbraith and K. L. Gould Stepping into the ring: the SIN takes on contractile ring assembly Genes & Dev., November 15, 2008; 22(22): 3082 - 3088. [Abstract] [Full Text] [PDF]

				E. M. Neidt, C. T. Skau, and D. R. Kovar The Cytokinesis Formins from the Nematode Worm and Fission Yeast Differentially Mediate Actin Filament Assembly J. Biol. Chem., August 29, 2008; 283(35): 23872 - 23883. [Abstract] [Full Text] [PDF]