2011年1月14日，我室生物大分子结构与功能研究部姚雪彪教授和窦震副教授在JOURNAL OF BIOLOGICAL CHEMISTRY上发表题为CENP-U Cooperates with Hec1 to Orchestrate Kinetochore-Microtubule Attachment的论文。

Source: JOURNAL OF BIOLOGICAL CHEMISTRY Volume: 286 Issue: 2 Pages: 1627-1638 Published: JAN 14 2011

Hua SS (Hua, Shasha)1, Wang ZK (Wang, Zhikai)1,2, Jiang K (Jiang, Kai)1,2, Huang YJ (Huang, Yuejia)1,2, Ward T (Ward, Tarsha)2, Zhao LL (Zhao, Lingli)1, Dou Z (Dou, Zhen)1,2, Yao XBA (Yao, Xuebiao)1
Addresses:
1. Hefei Natl Lab Phys Sci Nanoscale, Anhui Lab Cellular Dynam & Chem Biol, Hefei 230027, Peoples R China
2. Morehouse Sch Med, Dept Physiol, Atlanta, GA 30310 USA
E-mail Addresses: douzhen@ustc.edu.cn, yaoxb@ustc.edu.cn

Reprint Address: Dou, Z (reprint author), Hefei Natl Lab Phys Sci Nanoscale, Anhui Lab Cellular Dynam & Chem Biol, Hefei 230027, Peoples R 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.