期刊
ONCOGENE
卷 36, 期 3, 页码 362-372出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/onc.2016.204
关键词
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资金
- NSFC [91540205, 31571447, 31171347]
- MOST [2012CB966600, 2015CB553800, 2013CB945303]
- NIH [R01GM63773, R01AR053591, R01CA108454, R01DK073932]
- Project 111
- PhD Programs Foundation of Ministry of Education of China [20110101120152]
- Fundamental Research Funds for the Central Universities
Smad proteins are central mediators in the canonical transforming growth factor-beta (TGF-beta) signaling pathway in mammalian cells. We report here that bromodomain-ontaining protein 7 (BRD7) functions as a novel transcription coactivator for Smads in TGF-beta signaling. BRD7 forms a TGF-beta inducible complex with Smad3/ 4 through its N-terminal Smad-binding domain. BRD7 simultaneously binds to acetylated histones to promote Smad-chromatin association, and associates with histone acetyltransferase p300 to enhance Smad transcriptional activity. Ectopic expression of BRD7, but not its mutants defective in Smad binding, enhances TGF-beta transcriptional, tumor-suppressing and epithelial-mesenchymal transition responses. Conversely, depletion of BRD7 inhibits TGF-beta responses. Thus, our study provides compelling evidence for a new function of BRD7 in fine-tuning TGF-beta physiological responses.
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