Journal
EMBO JOURNAL
Volume 25, Issue 14, Pages 3264-3274Publisher
WILEY
DOI: 10.1038/sj.emboj.7601228
Keywords
acetylation; haemopoiesis; phosphorylation; transcription; ubiquitination
Categories
Funding
- Telethon [D.001] Funding Source: Medline
- Wellcome Trust [059602] Funding Source: Medline
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Regulation of transcription requires mechanisms to both activate and terminate transcription factor activity. GATA-1 is a key haemopoietic transcription factor whose activity is increased by acetylation. We show here that acetylated GATA-1 is targeted for degradation via the ubiquitin/ proteasome pathway. Acetylation positively signals ubiquitination, suggesting that activation by acetylation simultaneously marks GATA-1 for degradation. Promoter-specific MAPK phosphorylation then cooperates with acetylation to execute protein loss. The requirement for both modifications is novel and suggests a way by which degradation of the active protein can be specifically regulated in response to external phosphorylation-mediated signalling. As many transcription factors are activated by acetylation, we suggest that this might be a general mechanism to control transcription factor activity.
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