4.6 Article

OTUD5 Regulates p53 Stability by Deubiquitinating p53

Journal

PLOS ONE
Volume 8, Issue 10, Pages -

Publisher

PUBLIC LIBRARY SCIENCE
DOI: 10.1371/journal.pone.0077682

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Funding

  1. National Natural Science Foundation of China [81102078, 81172597]
  2. Natural Science Foundation of Jiangsu Province [BK2009102]
  3. Innovative Project of Jiangsu Province [BL2012046]
  4. Changzhou Social Development [CE20125026]
  5. Priority Academic Program Development of Jiangsu Higher Education Institutions (PAPD)

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Background: The p53 tumour suppressor protein is a transcription factor that prevents oncogenic progression by activating the expression of apoptosis and cell-cycle arrest genes in stressed cells. The stability of p53 is tightly regulated by ubiquitin-dependent degradation, driven mainly by its negative regulators ubiquitin ligase MDM2. Principal Findings: In this study, we have identified OTUD5 as a DUB that interacts with and deubiquitinates p53. OTUD5 forms a direct complex with p53 and controls level of ubiquitination. The function of OTUD5 is required to allow the rapid activation of p53-dependent transcription and a p53-dependent apoptosis in response to DNA damage stress. Conclusions: As a novel deubiquitinating enzyme for p53, OTUD5 is required for the stabilization and the activation of a p53 response.

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