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

doi:10.1074/jbc.M113.533109

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 journal › Article › peer-review

41 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 language	English (US)
Pages (from-to)	5097-5108
Number of pages	12
Journal	Journal of Biological Chemistry
Volume	289
Issue number	8
DOIs	https://doi.org/10.1074/jbc.M113.533109
State	Published - Feb 21 2014

ASJC Scopus subject areas

Biochemistry
Molecular Biology
Cell Biology

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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 Sun, {Xiao Xin} and Johannes Elferich and Ujwal Shinde and David, {Larry L.} and Dai, {Mu Shui}",

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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 L.

AU - Dai, Mu Shui

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

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