Molecular Biology of the Cell Call for Nominations: MBC Editor-in-Chief

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


     


MBC in Press, published online ahead of print September 22, 2004
Mol. Biol. Cell 10.1091/mbc.E04-07-0640

A more recent version of this article appeared on December 1, 2004
This Article
Right arrow Full Text (PDF)
Right arrow Supplemental Material
Right arrow All Versions of this Article:
E04-07-0640v1
15/12/5551    most recent
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 arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by An, H.
Right arrow Articles by Gould, K. L.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by An, H.
Right arrow Articles by Gould, K. L.

Submitted on July 28, 2004
Accepted on September 9, 2004

Requirements of Fission Yeast Septins for Complex Formation, Localization and Function

Hanbing An,* Jennifer L. Morrell,{dagger} Jennifer L. Jennings,{ddagger} Andrew J. Link,{ddagger} and Kathleen L. Gould*{dagger}{sect}

*Howard Hughes Medical Institute, {dagger}Department of Cell and Developmental Biology, and {ddagger}Department of Microbiology and Immunology, Vanderbilt University School of Medicine, Nashville, TN 37232

Monitoring Editor: Trisha Davis

Septins are GTP binding proteins important for cytokinesis in many eukaryotes. The Schizosaccaromyces pombe genome sequence predicts orthologues of four of five S. cerevisiae septins involved in cytokinesis and these are named Spns1-4p. That spns1-4 are not essential genes permitted the application of a combined genetic and proteomics approach to determine their functional relationships. Our findings indicate that Spns1-4p are present throughout interphase as a diffusely localized ~8.5S complex containing two copies of each septin linked together as a chain in the order Spn3p-Spn4p-Spn1p-Spn2p. Septin recruitment to the medial region of the cell is genetically separable from ring formation and while it is normally restricted to mitosis, it can be promoted without activation of the mitotic cell cycle machinery. Coalescence into ring structures requires Spn1p and Spn4p associate with at least one other septin subunit and the expression of Mid2p that is normally restricted to mitosis. This study establishes the functional requirements for septin complex organization in vivo.


{sect}Corresponding author. E-mail: kathy.gould{at}vanderbilt.edu







Home Help [Feedback] [For Subscribers] [Archive] [Search] --
Copyright © 2004 by The American Society for Cell Biology. Terms of copyright protection, warranties, and disclaimers.