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

Metwaly, G. Y., Wu, Y., Peplowska, K., Röhrl, J., Soh, Y.-M., Burmann, F., et al. (2020). Phospho-regulation of the Shugoshin-Condensin interaction at the centromere in budding yeast. PLoS Genetics, 16(8): e1008569. doi:10.1371/journal.pgen.1008569.

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Metwaly, Galal Yahya1, Author
Wu, Yehui2, Author           
Peplowska, Karolina2, Author           
Röhrl, Jennifer2, Author           
Soh, Young-Min1, Author
Burmann, Frank1, Author
Gruber, Stephan1, Author
Storchova, Zuzana1, Author
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1external, ou_persistent22              
2Storchova, Zuzana / Maintenance of Genome Stability, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565171              

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Free keywords: RECRUITS PP2A; PHOSPHORYLATION; COHESIN; KINASE; CHROMOSOMES; SGO1; BUB1Genetics & Heredity;
 Abstract: Author summary Proper chromosome segregation in eukaryotes is ensured through correct attachment of the spindle microtubules to the centromeric chromosomal regions. The attachment is mediated via the multimolecular proteinaceous complex called the kinetochore. This enables the establishment of bioirentation, when each sister chromatid is attached to microtubules emanating from opposite spindle poles. Shugoshin (Sgo1) is a conserved centromeric protein that facilitates biorientation through its interactions with the protein phosphatase PP2A/Rts1, chromosome passenger complex and centromeric condensin. Here, we identified a serine-rich motif that is required for the interaction of shugoshin with the condensin complex. We show that loss of this region impairs condensin enrichment at the centromere, chromosome biorientation, segregation as well as the function of the chromosome passenger complex in the error correction. Moreover, the interaction is phosphoregulated, as phosphorylation of the serine-rich motif on Sgo1 disrupts its interaction with condensin. Finally, we show that the conserved spindle assembly checkpoint kinase Mps1 is responsible for this phosphorylation. Our findings uncover novel regulatory mechanisms that facilitate proper chromosome segregation.
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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Language(s): eng - English
 Dates: 2020
 Publication Status: Published online
 Pages: 19
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 Table of Contents: We thank Nagarunja Nagaraj for his help with the identification of the phosphosites on Sgo1 that was performed by the Mass Spectrometry Core Facility at the MPI Biochemistry, Martinsried, Germany.
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Title: PLoS Genetics
  Other : PLoS Genet.
Source Genre: Journal
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Publ. Info: San Francisco, CA : Public Library of Science
Pages: - Volume / Issue: 16 (8) Sequence Number: e1008569 Start / End Page: - Identifier: ISSN: 1553-7390
CoNE: https://pure.mpg.de/cone/journals/resource/1000000000017180