Localization of the ubiquitin ligase Dma1 to the fission yeast contractile ring is modulated by phosphorylation

FEBS Letters

article

Jun-Song Chen¹  Christine M. Jones¹  Maya G. Igarashi¹  Liping Ren¹  Alyssa E. Johnson¹  Kathleen L. Gould¹ 

[1] Department of Cell and Developmental Biology, Vanderbilt University School of Medicine

关键词: cytokinesis;    fission yeast;    protein kinase;    septation initiation network;    signaling;    spindle pole body;    ubiquitin ligase;   

DOI  :  10.1002/1873-3468.14211

来源: John Wiley & Sons Ltd.

【 摘 要 】

The timing of cytokinesis relative to other mitotic events in the fission yeast Schizosaccharomyces pombe is controlled by the septation initiation network (SIN). During a mitotic checkpoint, the SIN is inhibited by the E3 ubiquitin ligase Dma1 to prevent chromosome mis-segregation. Dma1 dynamically localizes to spindle pole bodies (SPBs) and the contractile ring (CR) during mitosis, though its role at the CR is unknown. Here, we examined whether Dma1 phosphorylation affects its localization or function. We found that preventing Dma1 phosphorylation by substituting the six phosphosites with alanines diminished its CR localization but did not affect its mitotic checkpoint function. These studies reinforce the conclusion that Dma1 localization to the SPB is key to its role in the mitotic checkpoint.

【 授权许可】

Unknown