Journal
JOURNAL OF CELL BIOLOGY
Volume 210, Issue 5, Pages 727-735Publisher
ROCKEFELLER UNIV PRESS
DOI: 10.1083/jcb.201502044
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Funding
- National Natural Science Foundation of China [91313302, 31030044, 31371365]
- State Key Basic Research and Development Plan of the Ministry of Science and Technology of China [2010CB833705, 2014CB138402]
- National Institutes of Health [5SC2GM089622-03]
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During the G2 to M phase transition, a portion of mitotic regulator Plk1 localizes to the kinetochores and regulates the initiation of kinetochore-microtubule attachments for proper chromosome alignment. Once kinetochore-microtubule attachment is achieved, this portion of Plk1 is removed from the kinetochores as a result of ubiquitination. However, the crucial molecular mechanism that promotes the localization and the maintenance of Plk1 on the kinetochores until metaphase is still unclear. We report that ubiquitin-specific peptidase 16 (Usp16) plays a key role during this process. Usp16 deubiquitinates Plk1, resulting in an enhanced interaction with kinetochore-localized proteins such as BubR1, and thereby retains Plk1 on the kinetochores to promote proper chromosome alignment in early mitosis. Down-regulation of Usp16 causes increased ubiquitination and decreased kinetochore localization of Plk1. Thus, our data unveil a unique mechanism by which Usp16 promotes the localization and maintenance of Plk1 on the kinetochores for proper chromosome alignment.
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