Acetylation and MAPK phosphorylation cooperate to regulate the degradation of active GATA-1
Date
2006-07-26ICR Author
Author
Hernandez-Hernandez, A
Ray, P
Litos, G
Ciro, M
Ottolenghi, S
Beug, H
Boyes, J
Type
Journal Article
Metadata
Show full item recordAbstract
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.
Collections
Research team
Molecular Embryology
Language
eng
License start date
2006-07-26
Citation
EMBO JOURNAL, 2006, 25 pp. 3264 - 3274