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 |
|---|---|
| Pages (from-to) | 3264-3274 |
| Number of pages | 11 |
| Journal | EMBO Journal |
| Volume | 25 |
| Issue number | 14 |
| DOIs | |
| Publication status | Published - Jul 26 2006 |
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Keywords
- Acetylation
- Haemopoiesis
- Phosphorylation
- Transcription
- Ubiquitination
ASJC Scopus subject areas
- Genetics
- Cell Biology
Cite this
Acetylation and MAPK phosphorylation cooperate to regulate the degradation of active GATA-1. / Hernandez-Hernandez, Angel; Ray, Pampa; Litos, Gabi; Ciro, Marco; Ottolenghi, Sergio; Beug, Hartmut; Boyes, Joan.
In: EMBO Journal, Vol. 25, No. 14, 26.07.2006, p. 3264-3274.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Acetylation and MAPK phosphorylation cooperate to regulate the degradation of active GATA-1
AU - Hernandez-Hernandez, Angel
AU - Ray, Pampa
AU - Litos, Gabi
AU - Ciro, Marco
AU - Ottolenghi, Sergio
AU - Beug, Hartmut
AU - Boyes, Joan
PY - 2006/7/26
Y1 - 2006/7/26
N2 - 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.
AB - 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.
KW - Acetylation
KW - Haemopoiesis
KW - Phosphorylation
KW - Transcription
KW - Ubiquitination
UR - http://www.scopus.com/inward/record.url?scp=33746532476&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=33746532476&partnerID=8YFLogxK
U2 - 10.1038/sj.emboj.7601228
DO - 10.1038/sj.emboj.7601228
M3 - Article
VL - 25
SP - 3264
EP - 3274
JO - EMBO Journal
JF - EMBO Journal
SN - 0261-4189
IS - 14
ER -