Phospho-regulation of the Shugoshin - Condensin interaction at the centromere in budding yeast.

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Version: Final published version
License: CC BY 4.0
Serval ID
serval:BIB_D23C2314CE14
Type
Article: article from journal or magazin.
Collection
Publications
Institution
Title
Phospho-regulation of the Shugoshin - Condensin interaction at the centromere in budding yeast.
Journal
PLoS genetics
Author(s)
Metwaly G.Y., Wu Y., Peplowska K., Röhrl J., Soh Y.M., Bürmann F., Gruber S., Storchova Z.
ISSN
1553-7404 (Electronic)
ISSN-L
1553-7390
Publication state
Published
Issued date
18/08/2020
Peer-reviewed
Oui
Volume
16
Number
8
Pages
e1008569
Language
english
Notes
Publication types: Journal Article
Publication Status: aheadofprint
Abstract
Correct bioriented attachment of sister chromatids to the mitotic spindle is essential for chromosome segregation. In budding yeast, the conserved protein shugoshin (Sgo1) contributes to biorientation by recruiting the protein phosphatase PP2A-Rts1 and the condensin complex to centromeres. Using peptide prints, we identified a Serine-Rich Motif (SRM) of Sgo1 that mediates the interaction with condensin and is essential for centromeric condensin recruitment and the establishment of biorientation. We show that the interaction is regulated via phosphorylation within the SRM and we determined the phospho-sites using mass spectrometry. Analysis of the phosphomimic and phosphoresistant mutants revealed that SRM phosphorylation disrupts the shugoshin-condensin interaction. We present evidence that Mps1, a central kinase in the spindle assembly checkpoint, directly phosphorylates Sgo1 within the SRM to regulate the interaction with condensin and thereby condensin localization to centromeres. Our findings identify novel mechanisms that control shugoshin activity at the centromere in budding yeast.
Pubmed
Open Access
Yes
Create date
28/08/2020 8:13
Last modification date
15/01/2021 8:12
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