期刊
JOURNAL OF ZHEJIANG UNIVERSITY-SCIENCE B
卷 15, 期 12, 页码 1032-1038出版社
ZHEJIANG UNIV
DOI: 10.1631/jzus.B1400180
关键词
p53; USP11; Deubiquitination; Stability
类别
资金
- Key Project of Colleges and Universities in Fujian Province Serving the Construction of the West-strait [A101]
- Foundation for the 2013 Research Plan of University Key Teacher Domestic Visitor of the Ministry of Education
- Foundation for the Second Batch of Key Teacher of Quanzhou Normal College (personnel department of QNC), China
The p53 tumor suppressor protein coordinates the cellular responses to a broad range of cellular stresses, leading to DNA repair, cell cycle arrest or apoptosis. The stability of p53 is essential for its tumor suppressor function, which is tightly controlled by ubiquitin-dependent degradation primarily through its negative regulator murine double minute 2 (Mdm2). To better understand the regulation of p53, we tested the interaction between p53 and USP11 using co-immunoprecipitation. The results show that USP11, an ubiquitin-specific protease, forms specific complexes with p53 and stabilizes p53 by deubiquitinating it. Moreover, down-regulation of USP11 dramatically attenuated p53 induction in response to DNA damage stress. These findings reveal that USP11 is a novel regulator of p53, which is required for p53 activation in response to DNA damage.
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