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 David, Mushui Dai

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26 Citations (Scopus)

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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Tumors
Carrier Proteins
Chemical activation
Enzymes
Neoplasms
Proteins
ubiquitin-aldehyde

ASJC Scopus subject areas

  • Biochemistry
  • Cell Biology
  • Molecular Biology

Cite this

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title = "Monoubiquitination is critical for ovarian tumor domain-containing ubiquitin aldehyde binding protein 1 (Otub1) to suppress UbcH5 enzyme and Stabilize p53 protein",
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.",
author = "Yuhuang Li and Xiao-Xin Sun and Johannes Elferich and Ujwal Shinde and Larry David and Mushui Dai",
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T1 - Monoubiquitination is critical for ovarian tumor domain-containing ubiquitin aldehyde binding protein 1 (Otub1) to suppress UbcH5 enzyme and Stabilize p53 protein

AU - Li, Yuhuang

AU - Sun, Xiao-Xin

AU - Elferich, Johannes

AU - Shinde, Ujwal

AU - David, Larry

AU - Dai, Mushui

PY - 2014/2/21

Y1 - 2014/2/21

N2 - 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.

AB - 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.

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