Abstract
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.
Original language | English |
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Pages (from-to) | 3264-3274 |
Number of pages | 11 |
Journal | EMBO Journal |
Volume | 25 |
Issue number | 14 |
DOIs | |
Publication status | Published - Jul 26 2006 |
Keywords
- Acetylation
- Haemopoiesis
- Phosphorylation
- Transcription
- Ubiquitination
ASJC Scopus subject areas
- Genetics
- Cell Biology