期刊
MOLECULAR AND CELLULAR BIOLOGY
卷 24, 期 24, 页码 10826-10834出版社
AMER SOC MICROBIOLOGY
DOI: 10.1128/MCB.24.24.10826-10834.2004
关键词
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资金
- NCI NIH HHS [CA 085678, CA 090465, R01 CA085678, R01 CA090465, R01 CA098172, CA 098172] Funding Source: Medline
- NIDDK NIH HHS [R37 DK058044, DK 58044, R01 DK058044] Funding Source: Medline
The c-MYC oncoprotein functions as a sequence-specific transcription factor. The ability of c-MYC to activate transcription relies in part on the recruitment of cofactor complexes containing the histone acetyltransferases mammalian GCN5 (mGCN5)/PCAF and TIP60. In addition to acetylating histones, these enzymes have been shown to acetylate other proteins involved in transcription, including sequence-specific transcription factors. This study was initiated in order to determine whether c-MYC is a direct substrate of mGCN5 and TIP60. We report here that mGCN5/PCAF and TIP60 acetylate c-MYC in vivo. By using nanoelectrospray tandem mass spectrometry to examine c-MYC purified from human cells, the major mGCN5-induced acetylation sites have been mapped. Acetylation of c-MYC by either mGCNS/PCAF or TIP60 results in a dramatic increase in protein stability. The data reported here suggest a conserved mechanism by which acetyltransferases regulate c-MYC function by altering its rate of degradation.
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