JCB logo
CrossRef
  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents
Published online 24 March 2003. doi:10.1083/jcb.200212016
This Article
Right arrow Full Text
Right arrow Full Text (PDF, 667K)
Right arrow PPT slides of all figures
Right arrow Alert me when this article is cited
Right arrow Citation Map
Services
Right arrow Email this article
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new content in the JCB
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Berlin, A.
Right arrow Articles by Chang, F.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Berlin, A.
Right arrow Articles by Chang, F.
Right arrowPubmed/NCBI databases
*Domain*Gene
*GEO Profiles*Protein
*Substance via MeSH
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Facebook   Add to Reddit   Add to Technorati   Add to Twitter  
What's this?

© The Rockefeller University Press, 0021-9525/2003/3/1083 $5.00
The Journal of Cell Biology, Volume 160, Number 7, 1083-1092

Article

Mid2p stabilizes septin rings during cytokinesis in fission yeast



Ana Berlin1, Anne Paoletti2 and Fred Chang1

1 Department of Microbiology, Columbia University College of Physicians and Surgeons, New York, NY 10032
2 Institut Curie, UMR144 du Centre National de la Rescherche Scientifique, 75248 Paris, France Cedex 05

Address correspondence to Fred Chang, Dept. of Microbiology, Columbia University College of Physicians and Surgeons, 701 W. 168th St., New York, NY 10032. Tel.: (212) 305-0252. Fax: (212) 305-1468. E-mail: fc99{at}columbia.edu

Septins are filament-forming proteins with a conserved role in cytokinesis. In the fission yeast Schizosaccharomyces pombe, septin rings appear to be involved primarily in cell–cell separation, a late stage in cytokinesis. Here, we identified a protein Mid2p on the basis of its sequence similarity to S. pombe Mid1p, Saccharomyces cerevisiae Bud4p, and Candida albicans Int1p. Like septin mutants, mid2{Delta} mutants had delays in cell–cell separation. mid2{Delta} mutants were defective in septin organization but not contractile ring closure or septum formation. In wild-type cells, septins assembled first during mitosis in a single ring and during septation developed into double rings that did not contract. In mid2{Delta} cells, septins initially assembled in a single ring but during septation appeared in the cleavage furrow, forming a washer or disc structure. FRAP studies showed that septins are stable in wild-type cells but exchange 30-fold more rapidly in mid2{Delta} cells. Mid2p colocalized with septins and required septins for its localization. A COOH-terminal pleckstrin homology domain of Mid2p was required for its localization and function. No genetic interactions were found between mid2 and the related gene mid1. Thus, these studies identify a new factor responsible for the proper stability and function of septins during cytokinesis.

Key Words: cytokinesis; septin; fission yeast Schizosaccharomyces pombe; contractile ring; FRAP

* Abbreviations used in this paper: DIC, differential interference contrast; PH, pleckstrin homology.


Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Facebook Facebook   Add to Reddit Reddit   Add to Technorati Technorati   Add to Twitter Twitter    What's this?


This article has been cited by other articles:



  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents