Acetylation-regulated interaction between p53 and SET reveals a widespread regulatory mode

Donglai Wang, Ning Kon, Gorka Lasso, Le Jiang, Wenchuan Leng, Wei-Guo Zhu, Jun Qin, Barry Honig and Wei Gu ()
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Donglai Wang: Institute for Cancer Genetics, Herbert Irving Comprehensive Cancer Center, College of Physicians & Surgeons, Columbia University
Ning Kon: Institute for Cancer Genetics, Herbert Irving Comprehensive Cancer Center, College of Physicians & Surgeons, Columbia University
Gorka Lasso: Center for Computational Biology and Bioinformatics, Howard Hughes Medical Institute, Columbia University
Le Jiang: Institute for Cancer Genetics, Herbert Irving Comprehensive Cancer Center, College of Physicians & Surgeons, Columbia University
Wenchuan Leng: State Key Laboratory of Proteomics, National Center for Protein Sciences (The PHOENIX Center, Beijing)
Wei-Guo Zhu: Shenzhen University School of Medicine
Jun Qin: State Key Laboratory of Proteomics, National Center for Protein Sciences (The PHOENIX Center, Beijing)
Barry Honig: Center for Computational Biology and Bioinformatics, Howard Hughes Medical Institute, Columbia University
Wei Gu: Institute for Cancer Genetics, Herbert Irving Comprehensive Cancer Center, College of Physicians & Surgeons, Columbia University

Nature, 2016, vol. 538, issue 7623, 118-122

Abstract: The acidic domain of SET binds and represses unacetylated p53, but this interaction is prevented by cellular-stress-induced p53 CTD acetylation.

Date: 2016
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DOI: 10.1038/nature19759

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