Monoubiquitination is critical for ovarian tumor domain-containing ubiquitin aldehyde binding protein 1 (Otub1) to suppress UbcH5 enzyme and Stabilize p53 protein

Yuhuang Li, Xiao Xin Sun, Johannes Elferich, Ujwal Shinde, Larry L. David, Mu Shui Dai

Research output: Contribution to journalArticle

26 Scopus citations

Abstract

Background: Otub1 suppresses E2 UbcH5 to stabilize and activate p53. Results: UbcH5 monoubiquitinates Otub1, and monoubiquitination-defective Otub1 mutants fail to inhibit UbcH5 and induce p53. Conclusion: Monoubiquitination is critical for Otub1 to suppress UbcH5 and induce p53. Significance: We report the discovery of a novel molecular mechanism underlying Otub1 suppression of E2 and activation of p53.

Original languageEnglish (US)
Pages (from-to)5097-5108
Number of pages12
JournalJournal of Biological Chemistry
Volume289
Issue number8
DOIs
StatePublished - Feb 21 2014

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ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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