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Stimulation of c-MYC transcriptional activity and acetylation by recruitment of the cofactor CBP 总被引:1,自引:0,他引:1
Vervoorts J Lüscher-Firzlaff JM Rottmann S Lilischkis R Walsemann G Dohmann K Austen M Lüscher B 《EMBO reports》2003,4(5):484-490
The c-MYC oncoprotein regulates various aspects of cell behaviour by modulating gene expression. Here, we report the identification of the cAMP-response-element-binding protein (CBP) as a novel c-MYC binding partner. The two proteins interact both in vitro and in cells, and CBP binds to the carboxy-terminal region of c-MYC. Importantly, CBP, as well as p300, is associated with E-box-containing promoter regions of genes that are regulated by c-MYC. Furthermore, c-MYC and CBP/p300 function synergistically in the activation of reporter-gene constructs. Thus, CBP and p300 function as positive cofactors for c-MYC. In addition, c-MYC is acetylated in cells. This modification does not require MYC box II, suggesting that it is independent of TRRAP complexes. Instead, CBP acetylates c-MYC in vitro, and co-expression of CBP with c-MYC stimulates in vivo acetylation. Functionally, this results in a decrease in ubiquitination and stabilization of c-MYC proteins. Thus, CBP and p300 are novel functional binding partners of c-MYC. 相似文献
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Sharada Ramasubramanyan Aditi Kanhere Kay Osborn Kirsty Flower Richard G. Jenner Alison J. Sinclair 《Journal of virology》2012,86(23):12494-12502
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