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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
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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


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This article has been cited by other articles:


Home page
 J. Biol. Chem.Home page
M. R. Sharifmoghadam and M.-H. Valdivieso
The Fission Yeast SEL1 Domain Protein Cfh3p: A NOVEL REGULATOR OF THE GLUCAN SYNTHASE Bgs1p WHOSE FUNCTION IS MORE RELEVANT UNDER STRESS CONDITIONS
J. Biol. Chem., April 24, 2009; 284(17): 11070 - 11079.
[Abstract] [Full Text] [PDF]


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