spacer gif spacer gif spacer gif spacer gif spacer gif
QUICK SEARCH:   [advanced]


spacer gif
     Home     Help     Feedback     Subscriptions     Archive     Search     Table of Contents    

First published online 13 June 2006
doi: 10.1242/jcs.02998

Journal of Cell Science 119, 2768-2779 (2006)
Published by The Company of Biologists 2006
This Article
Right arrow Figures Only
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Supplementary Material
Right arrow All Versions of this Article:
jcs.02998v1
119/13/2768    most recent
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
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 Martín-García, R.
Right arrow Articles by Valdivieso, M.-H.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Martín-García, R.
Right arrow Articles by Valdivieso, M.-H.

Research Article

The fission yeast Chs2 protein interacts with the type-II myosin Myo3p and is required for the integrity of the actomyosin ring

Rebeca Martín-García and M.-Henar Valdivieso*

Departamento de Microbiología y Genética/Instituto de Microbiología Bioquímica, Universidad de Salamanca/CSIC, Edificio Departamental, Laboratorio 231, Campus Miguel de Unamuno, 37007 Salamanca, Spain

* Author for correspondence (e-mail: henar{at}usal.es)

Accepted 28 March 2006

In Schizosaccharomyces pombe cytokinesis requires the function of a contractile actomyosin ring. Fission yeast Chs2p is a transmembrane protein structurally similar to chitin synthases that lacks such enzymatic activity. Chs2p localisation and assembly into a ring that contracts during division requires the general system for polarised secretion, some components of the actomyosin ring, and an active septation initiation network. Chs2p interacts physically with the type-II myosin Myo3p revealing a physical link between the plasma membrane and the ring. In chs2{Delta} mutants, actomyosin ring integrity is compromised during the last stages of contraction and it remains longer in the midzone. In synchronous cultures, chs2{Delta} cells exhibit a delay in septation with respect to the control strain. All these results show that Chs2p participates in the correct functioning of the medial ring.

Key words: Schizosaccharomyces pombe, Saccharomyces cerevisiae, Cytokinesis, Actomyosin ring, Type-II Myosin






© The Company of Biologists Ltd 2006