期刊
JOURNAL OF CELL SCIENCE
卷 124, 期 4, 页码 622-634出版社
COMPANY OF BIOLOGISTS LTD
DOI: 10.1242/jcs.072629
关键词
Kinetochore; NDC80; Hec1; Microtubule; Aurora B
类别
资金
- National Institutes of Health [K01CA125051, R01534521]
- Basil O'Conner Starter Scholar Research Award
- Pew Scholars Program in the Biomedical Sciences
- Netherlands Organization for Scientific Research [Vidi 917.66.332]
- Dutch Cancer Society [KWF-UU 2009-4311]
Precise control of the attachment strength between kinetochores and spindle microtubules is essential to preserve genomic stability. Aurora B kinase has been implicated in regulating the stability of kinetochore-microtubule attachments but its relevant kinetochore targets in cells remain unclear. Here, we identify multiple serine residues within the N-terminus of the kinetochore protein Hec1 that are phosphorylated in an Aurora-B-kinase-dependent manner during mitosis. On all identified target sites, Hec1 phosphorylation at kinetochores is high in early mitosis and decreases significantly as chromosomes bi-orient. Furthermore, once dephosphorylated, Hec1 is not highly rephosphorylated in response to loss of kinetochore-microtubule attachment or tension. We find that a subpopulation of Aurora B kinase remains localized at the outer kinetochore even upon Hec1 dephosphorylation, suggesting that Hec1 phosphorylation by Aurora B might not be regulated wholly by spatial positioning of the kinase. Our results define a role for Hec1 phosphorylation in kinetochore-microtubule destabilization and error correction in early mitosis and for Hec1 dephosphorylation in maintaining stable attachments in late mitosis.
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