Mitotic exit kinase Dbf2 directly phosphorylates chitin synthase Chs2 to regulate cytokinesis in budding yeast.

Molecular Biology of the Cell
Younghoon OhE Bi

Abstract

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...Continue Reading

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Citations

Jul 24, 2013·The Journal of Cell Biology·Masayuki OnishiJohn R Pringle
Mar 1, 2013·Molecular Biology of the Cell·Franz MeitingerGislene Pereira
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Methods Mentioned

BETA
GTPase
fluorescence microscopy
fluorescence recovery after photobleaching
synthase assay
PCR
protein assay

Software Mentioned

ImageJ
MetaMorph
Pro Plus
Image

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