The fission yeast Chs2 protein interacts with the type-II myosin Myo3p and is required for the integrity of the actomyosin ring.
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 chs2Delta mutants, actomyosin ring integrity is compromised during the last stages of contraction and it remains longer in the midzone. In synchronous cultures, chs2Delta 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.
Mesh Terms:
Actomyosin, Bodily Secretions, Cell Cycle Proteins, Cell Polarity, Chitin Synthase, Cytokinesis, Linkage (Genetics), Myosin Heavy Chains, Protein Binding, Schizosaccharomyces, Schizosaccharomyces pombe Proteins, Sequence Deletion, Signal Transduction, Tissue Distribution, Transfection
Actomyosin, Bodily Secretions, Cell Cycle Proteins, Cell Polarity, Chitin Synthase, Cytokinesis, Linkage (Genetics), Myosin Heavy Chains, Protein Binding, Schizosaccharomyces, Schizosaccharomyces pombe Proteins, Sequence Deletion, Signal Transduction, Tissue Distribution, Transfection
J. Cell. Sci.
Date: Jul. 01, 2006
PubMed ID: 16772338
View in: Pubmed Google Scholar
Download Curated Data For This Publication
69849
Switch View:
- Interactions 17