期刊
GENES & DEVELOPMENT
卷 23, 期 7, 页码 849-861出版社
COLD SPRING HARBOR LAB PRESS, PUBLICATIONS DEPT
DOI: 10.1101/gad.1748409
关键词
NF-kappa B; RelA; GCN5; COMMD1; ubiquitin; Cul2
资金
- VA Merit Review Entry Program Award
- CCFA Senior Research Award
- NIH [R01 DK073639]
- NCI [CA104397]
- DOD [W81XWH-06-10186]
- University of Michigan's Cancer Center Grant [NIH 5 P30 CA46592]
The transcription factor NF-kappa B is a critical regulator of inflammatory and cell survival signals. Proteasomal degradation of NF-kappa B subunits plays an important role in the termination of NF-kappa B activity, and at least one of the identified ubiquitin ligases is a multimeric complex containing Copper Metabolism Murr1 Domain 1 (COMMD1) and Cul2. We report here that GCN5, a histone acetyltransferase, associates with COMMD1 and other components of the ligase, promotes RelA ubiquitination, and represses kappa B-dependent transcription. In this role, the acetyltransferase activity of GCN5 is not required. Interestingly, GCN5 binds more avidly to RelA after phosphorylation on Ser 468, an event that is dependent on IKK activity. Consistent with this, we find that both GCN5 and the I kappa B Kinase ( IKK) complex promote RelA degradation. Collectively, the data indicate that GCN5 participates in the ubiquitination process as an accessory factor for a ubiquitin ligase, where it provides a novel link between phosphorylation and ubiquitination.
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