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MBC in Press, published online ahead of print May 9, 2007
Mol. Biol. Cell 10.1091/mbc.E06-04-0345

A more recent version of this article appeared on July 1, 2007
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Submitted on April 26, 2006
Revised on March 22, 2007
Accepted on April 26, 2007

Nudel Modulates Kinetochore Association and Function of Cytoplasmic Dynein in M Phase

Yun Liang,*{dagger} Wei Yu,*{dagger} Yan Li,*{dagger} Lihou Yu,* Qiangge Zhang,* Fubin Wang,* Zhenye Yang,* Juan Du,* Qiongping Huang,* Xuebiao Yao,{ddagger} and Xueliang Zhu*

*Laboratory of Molecular Cell Biology, Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai 200031, China; {ddagger}Hefei National Laboratory for Physical Sciences and the School of Life Sciences, University of Science and Technology of China, Anhui 230027, China

Monitoring Editor: Kerry Bloom

The microtubule-based motor cytoplasmic dynein/dynactin is a force generator at the kinetochore. It also transports proteins away from kinetochores to spindle poles. Regulation of such diverse functions, however, is poorly understood. We have previously shown that Nudel is critical for dynein-mediated protein transport, whereas mitosin, a kinetochore protein that binds Nudel, is involved in retention of kinetochore dynein/dynactin against microtubule-dependent stripping. Here we demonstrate that Nudel is required for robust localization of dynein/dynactin at the kinetochore. It localizes to kinetochores after nuclear envelope breakdown, depending mostly (~78%) on mitosin and slightly on dynein/dynactin. Depletion of Nudel by RNAi or overexpression of its mutant incapable of binding either Lis1 or dynein heavy chain abolishes the kinetochore protein transport and mitotic progression. Similar to mitosin RNAi, Nudel RNAi also leads to increased stripping of kinetochore dynein/dynactin in the presence of microtubules. Taking together, our results suggest a dual role of kinetochore Nudel: it activates dynein-mediated protein transport and, when interacting with both mitosin and dynein, stabilizes kinetochore dynein/dynactin against microtubule-dependent stripping to facilitate the force generation function of the motor.

{dagger}These authors contributed equally to this work.

Address correspondence to: Xueliang Zhu (xlzhu{at}sibs.ac.cn)




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