Document Detail


Mitotic exit kinase Dbf2 directly phosphorylates chitin synthase Chs2 to regulate cytokinesis in budding yeast.
MedLine Citation:
PMID:  22573892     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
How cell cycle machinery regulates extracellular matrix (ECM) remodeling during cytokinesis remains poorly understood. In the budding yeast Saccharomyces cerevisiae, the primary septum (PS), a functional equivalent of animal ECM, is synthesized during cytokinesis by the chitin synthase Chs2. Here, we report that Dbf2, a conserved mitotic exit kinase, localizes to the division site after Chs2 and directly phosphorylates Chs2 on several residues, including Ser-217. Both phosphodeficient (chs2-S217A) and phosphomimic (chs2-S217D) mutations cause defects in cytokinesis, suggesting that dynamic phosphorylation-dephosphorylation of Ser-217 is critical for Chs2 function. It is striking that Chs2-S217A constricts asymmetrically with the actomyosin ring (AMR), whereas Chs2-S217D displays little or no constriction and remains highly mobile at the division site. These data suggest that Chs2 phosphorylation by Dbf2 triggers its dissociation from the AMR during the late stage of cytokinesis. Of interest, both chs2-S217A and chs2-S217D mutants are robustly suppressed by increased dosage of Cyk3, a cytokinesis protein that displays Dbf2-dependent localization and also stimulates Chs2-mediated chitin synthesis. Thus Dbf2 regulates PS formation through at least two independent pathways: direct phosphorylation and Cyk3-mediated activation of Chs2. Our study establishes a mechanism for direct cell cycle control of ECM remodeling during cytokinesis.
Authors:
Younghoon Oh; Kuang-Jung Chang; Peter Orlean; Carsten Wloka; Raymond Deshaies; Erfei Bi
Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't     Date:  2012-05-09
Journal Detail:
Title:  Molecular biology of the cell     Volume:  23     ISSN:  1939-4586     ISO Abbreviation:  Mol. Biol. Cell     Publication Date:  2012 Jul 
Date Detail:
Created Date:  2012-06-29     Completed Date:  2012-11-05     Revised Date:  2013-06-25    
Medline Journal Info:
Nlm Unique ID:  9201390     Medline TA:  Mol Biol Cell     Country:  United States    
Other Details:
Languages:  eng     Pagination:  2445-56     Citation Subset:  IM    
Affiliation:
Department of Cell and Developmental Biology, University of Pennsylvania School of Medicine, Philadelphia, PA 19104, USA.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Amino Acid Substitution
Cell Cycle Proteins / chemistry,  metabolism*
Chitin / metabolism
Chitin Synthase / chemistry,  genetics,  metabolism*
Cytokinesis*
Fluorescence Recovery After Photobleaching
Microtubule-Associated Proteins / metabolism
Mutagenesis, Site-Directed
Phosphorylation
Protein Processing, Post-Translational
Protein Transport
Protein-Serine-Threonine Kinases / chemistry,  metabolism*
Saccharomyces cerevisiae / enzymology*,  growth & development,  physiology
Saccharomyces cerevisiae Proteins / chemistry,  metabolism*
Time-Lapse Imaging
Grant Support
ID/Acronym/Agency:
GM59216/GM/NIGMS NIH HHS; GM87365/GM/NIGMS NIH HHS; //Howard Hughes Medical Institute
Chemical
Reg. No./Substance:
0/Cell Cycle Proteins; 0/Cyk3 protein, S cerevisiae; 0/Microtubule-Associated Proteins; 0/Saccharomyces cerevisiae Proteins; 1398-61-4/Chitin; EC 2.4.1.16/Chitin Synthase; EC 2.4.1.16/chitin synthase 2; EC 2.7.11.1/DBF2 protein, S cerevisiae; EC 2.7.11.1/Protein-Serine-Threonine Kinases
Comments/Corrections

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


Previous Document:  GBF1 bears a novel phosphatidylinositol-phosphate binding module, BP3K, to link PI3K? activity with ...
Next Document:  Circulating malondialdehyde-modified low-density lipoprotein levels are associated with the presence...