期刊
MOLECULAR CELL
卷 40, 期 3, 页码 455-464出版社
CELL PRESS
DOI: 10.1016/j.molcel.2010.09.025
关键词
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资金
- National Institutes of Health [R01 GM078069]
- NIH [NCI 5 T32 CA09657]
- NIH/National Center for Research Resources Funded Yeast Resource Center [RR011823]
Proper centromere function is critical to maintain genomic stability and to prevent aneuploidy, a hallmark of tumors and birth defects. A conserved feature of all eukaryotic centromeres is an essential histone H3 variant called CENP-A that requires a centromere targeting domain (CATD) for its localization. Although proteolysis prevents CENP-A from mislocalizing to euchromatin, regulatory factors have not been identified. Hero, we identify an E3 ubiquitin ligase called Psh1 that leads to the degradation of Cse4., the budding yeast CENP-A homolog. Cse4 overexpression is toxic to psh1 Delta cells and results in euchromatic localization. Strikingly, the Cse4 CATD is a key regulator of its stability and helps Psh1 discriminate Cse4 from histone H3. Taken together, we propose that the CATD has a previously unknown role in maintaining the exclusive localization of Cse4 by preventing its mislocalization to euchromatin via Psh1-mediated degradation.
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