Document Detail

The Kin1 kinase and the calcineurin phosphatase cooperate to link actin ring assembly and septum synthesis in fission yeast.
MedLine Citation:
PMID:  23294323     Owner:  NLM     Status:  Publisher    
BACKGROUND INFORMATION: The Kin1 protein kinase of fission yeast, which regulates cell surface cohesiveness during interphase cell growth, is also present at the cell division site during mitosis; however, its function in cell division has remained elusive. RESULTS: In FK506-mediated calcineurin deficient cells, mitosis is extended and ring formation is transiently compromised but septation remains normal. Here we show that Kin1 inhibition in these cells leads to polyseptation and defects in membrane closure. Actomyosin ring disassembly is prevented and ultimately the daughter cells fail to separate. We show that the Pmk1 MAP kinase pathway and the type V myosin MyoΔ act downstream of the cytokinetic function of Kin1. Kin1 inhibition also promotes polyseptation in myo3 , a type II myosin heavy chain mutant defective in ring assembly. In contrast Kin1 inactivation rescues septation in a myosin light chain cdc4-8 thermosensitive mutant. A structure/function analysis of the Kin1 protein sequence identified a novel motif outside the kinase domain that is important for its polarized localization and its catalytic activity. This motif is remarkably conserved in all fungal Kin1 homologues but is absent in related kinases of metazoans. CONCLUSIONS: We conclude that calcineurin and Kin1 activities must be tightly coordinated to link actomyosin ring assembly with septum synthesis and membrane closure and to ensure separation of the daughter cells.
Angela Cadou; Anne Couturier; Cathy Le Goff; Linfeng Xie; James R Paulson; Xavier Le Goff
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2013-1-8
Journal Detail:
Title:  Biology of the cell / under the auspices of the European Cell Biology Organization     Volume:  -     ISSN:  1768-322X     ISO Abbreviation:  Biol. Cell     Publication Date:  2013 Jan 
Date Detail:
Created Date:  2013-1-8     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  8108529     Medline TA:  Biol Cell     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Copyright Information:
Copyright © 2013 Soçiété Francaise des Microscopies and Société de Biologie Cellulaire de France.
CNRS UMR6290 Institut de Génétique et Développement de Rennes, France; Université de Rennes 1, UEB, SFR Biosit CNRS UMS3480, Rennes, France.
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