Evidence map›Paper›PMID 32810145›Full record

ArticlePLoS genetics2020

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

Galal Yahya, Yehui Wu, Karolina Peplowska, Jennifer Röhrl, Young-Min Soh, Frank Bürmann, Stephan Gruber, Zuzana Storchova

Abstract read
In one paragraph

Article in PLoS genetics, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

8 citing papers in PubMed.

  1. Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors.

Galal YahyaDepartment of Microbiology and Immunology, School of Pharmacy, Zagazig University, Egypt.ORCID 0000-0002-9466-7863
Yehui WuMax Planck Institute of Biochemistry, Martinsried, Germany.ORCID 0000-0002-0871-1419
Karolina PeplowskaMax Planck Institute of Biochemistry, Martinsried, Germany.
Jennifer RöhrlMax Planck Institute of Biochemistry, Martinsried, Germany.ORCID 0000-0001-8715-3330
Young-Min SohDepartment of Fundamental Microbiology, UNIL-Sorge District, Lausanne, Switzerland.ORCID 0000-0002-3804-7168
Frank BürmannMRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge, United Kingdom.ORCID 0000-0002-9428-0933
Stephan GruberDepartment of Fundamental Microbiology, UNIL-Sorge District, Lausanne, Switzerland.ORCID 0000-0002-0150-0395
Zuzana StorchovaDepartment of Molecular Genetics, TU Kaiserlautern, Kaiserslautern, Germany.ORCID 0000-0003-2376-7047

Funding

Medical Research Council MC_U105184326
6 · The paper itself

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.

Indexed as

Adenosine TriphosphatasesAmino Acid MotifsCentromereDNA-Binding ProteinsMultiprotein ComplexesNuclear ProteinsPhosphorylationProtein BindingProtein Phosphatase 2Protein Serine-Threonine KinasesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAdenosine Triphosphatasescondensin complexesDNA-Binding ProteinsMPS1 protein, S cerevisiaeMultiprotein ComplexesNuclear ProteinsProtein Phosphatase 2Protein Serine-Threonine KinasesRts1 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSgo1 protein, S cerevisiae

Identifiers

PMID32810145
PMCPMC7454948

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.