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J Biol Chem. 2011 Jan 14;286(2):1627-38. doi: 10.1074/jbc.M110.174946. Epub 2010 Nov 5.

CENP-U cooperates with Hec1 to orchestrate kinetochore-microtubule attachment.

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  • 1Anhui Laboratory of Cellular Dynamics and Chemical Biology, Hefei National Laboratory for Physical Sciences at Nanoscale, Hefei 230027, China.

Abstract

Mitosis is an orchestration of dynamic interaction between chromosomes and spindle microtubules by which genomic materials are equally distributed into two daughter cells. Previous studies showed that CENP-U is a constitutive centromere component essential for proper chromosome segregation. However, the precise molecular mechanism has remained elusive. Here, we identified CENP-U as a novel interacting partner of Hec1, an evolutionarily conserved kinetochore core component essential for chromosome plasticity. Suppression of CENP-U by shRNA resulted in mitotic defects with an impaired kinetochore-microtubule attachment. Interestingly, CENP-U not only binds microtubules directly but also displays a cooperative microtubule binding activity with Hec1 in vitro. Furthermore, we showed that CENP-U is a substrate of Aurora-B. Importantly, phosphorylation of CENP-U leads to reduced kinetochore-microtubule interaction, which contributes to the error-correcting function of Aurora-B. Taken together, our results indicate that CENP-U is a novel microtubule binding protein and plays an important role in kinetochore-microtubule attachment through its interaction with Hec1.

PMID:
21056971
PMCID:
PMC3020771
DOI:
10.1074/jbc.M110.174946
[PubMed - indexed for MEDLINE]
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