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

  • 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.

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Author:Galal YahyaORCiD, Yehui WuORCiD, Karolina Peplowska, Jennifer RöhrlORCiD, Young-Min SohORCiD, Frank BürmannORCiD, Stephan GruberORCiD, Zuzana StorchováORCiD
URN (permanent link):urn:nbn:de:hbz:386-kluedo-61637
Parent Title (English):PLoS Genetics
Document Type:Article
Language of publication:English
Publication Date:2020/08/18
Year of Publication:2020
Publishing Institute:Technische Universität Kaiserslautern
Date of the Publication (Server):2021/01/07
Issue:2020, 16(8)
Number of page:19
Faculties / Organisational entities:Fachbereich Biologie
DDC-Cassification:5 Naturwissenschaften und Mathematik / 570 Biowissenschaften, Biologie
Licence (German):Zweitveröffentlichung