Shugoshin collaborates with protein phosphatase 2A to protect cohesin

Tomoya S. Kitajima, Takeshi Sakuno, Kei-ichiro Ishiguro, Shun-ichiro Iemura, Tohru Natsume, Shigehiro A. Kawashima and Yoshinori Watanabe ()
Additional contact information
Tomoya S. Kitajima: Institute of Molecular and Cellular Biosciences
Takeshi Sakuno: Institute of Molecular and Cellular Biosciences
Kei-ichiro Ishiguro: Institute of Molecular and Cellular Biosciences
Shun-ichiro Iemura: Biological Information Research Center
Tohru Natsume: Biological Information Research Center
Shigehiro A. Kawashima: Institute of Molecular and Cellular Biosciences
Yoshinori Watanabe: Institute of Molecular and Cellular Biosciences

Nature, 2006, vol. 441, issue 7089, 46-52

Abstract: Abstract Sister chromatid cohesion, mediated by a complex called cohesin, is crucial—particularly at centromeres—for proper chromosome segregation in mitosis and meiosis. In animal mitotic cells, phosphorylation of cohesin promotes its dissociation from chromosomes, but centromeric cohesin is protected by shugoshin until kinetochores are properly captured by the spindle microtubules. However, the mechanism of shugoshin-dependent protection of cohesin is unknown. Here we find a specific subtype of serine/threonine protein phosphatase 2A (PP2A) associating with human shugoshin. PP2A colocalizes with shugoshin at centromeres and is required for centromeric protection. Purified shugoshin complex has an ability to reverse the phosphorylation of cohesin in vitro, suggesting that dephosphorylation of cohesin is the mechanism of protection at centromeres. Meiotic shugoshin of fission yeast also associates with PP2A, with both proteins collaboratively protecting Rec8-containing cohesin at centromeres. Thus, we have revealed a conserved mechanism of centromeric protection of eukaryotic chromosomes in mitosis and meiosis.

Date: 2006
References: Add references at CitEc
Citations: View citations in EconPapers (2)

Downloads: (external link)
https://www.nature.com/articles/nature04663 Abstract (text/html)
Access to the full text of the articles in this series is restricted.

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:nature:v:441:y:2006:i:7089:d:10.1038_nature04663

Ordering information: This journal article can be ordered from
https://www.nature.com/

DOI: 10.1038/nature04663

Access Statistics for this article

Nature is currently edited by Magdalena Skipper

More articles in Nature from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().