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Localization of the ubiquitin ligase Dma1 to the fission yeast contractile ring is modulated by phosphorylation
Author(s) -
Chen JunSong,
Jones Christine M.,
Igarashi Maya G.,
Ren Liping,
Johnson Alyssa E.,
Gould Kathleen L.
Publication year - 2021
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.14211
Subject(s) - microbiology and biotechnology , cytokinesis , mitosis , schizosaccharomyces pombe , schizosaccharomyces , ubiquitin ligase , mitotic exit , biology , chromosome segregation , spindle pole body , g2 m dna damage checkpoint , phosphorylation , ubiquitin , spindle apparatus , chemistry , cell cycle checkpoint , yeast , biochemistry , cell cycle , chromosome , cell division , saccharomyces cerevisiae , cell , gene
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.