期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 110, 期 33, 页码 13404-13409出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1305020110
关键词
cell cycle; chromosome segregation; prophase pathway
资金
- Ministry of Education, Culture, Sports, Science, and Technology (MEXT)
- Precursory Research for Embryonic Science and Technology (PRESTO) from Japan Science and Technology Agency (JST)
- Boehringer Ingelheim
- Vienna Science and Technology Fund [WWTF LS09-13]
- Austrian Science Fund (FWF Special Research Program) [SFB F34, Z196-B20, SFB F3402, TRP 308-N15]
- European Commission Seventh Framework Programme [241548, 262067]
- Austrian GEN-AU initiative
- Bundesminsterium fur Bildung und Wissenschaft
- Grants-in-Aid for Scientific Research [25711002] Funding Source: KAKEN
- Austrian Science Fund (FWF) [TRP 308] Funding Source: researchfish
Sister chromatid cohesion depends on Sororin, a protein that stabilizes acetylated cohesin complexes on DNA by antagonizing the cohesin release factor Wings-apart like protein (Wapl). Cohesion is essential for chromosome biorientation but has to be dissolved to enable sister chromatid separation. To achieve this, the majority of cohesin is removed from chromosome arms in prophase and prometaphase in a manner that depends on Wapl and phosphorylation of cohesin's subunit stromal antigen 2 (SA2), whereas centromeric cohesin is cleaved in metaphase by the protease separase. Here we show that the mitotic kinases Aurora B and Cyclin-dependent kinase 1 (Cdk1) destabilize interactions between Sororin and the cohesin subunit precocious dissociation of sisters protein 5 (Pds5) by phosphorylating Sororin, leading to release of acetylated cohesin from chromosome arms and loss of cohesion. At centromeres, the cohesin protector shugoshin (Sgo1)-protein phosphatase 2A (PP2A) antagonizes Aurora B and Cdk1 partly by dephosphorylating Sororin and thus maintains cohesion until metaphase. We propose that the stepwise loss of cohesion between chromosome arms and centromeres is caused by local regulation of Wapl activity, which is controlled by the phosphorylation state of Sororin.
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