Abstract
The nuclear retinoic acid receptor RARγ2 undergoes proteasome-dependent degradation upon ligand binding. Here we provide evidence that the domains that signal proteasome-mediated degradation overlap with those that activate transcription, i.e. the activation domains AF-1 and AF-2. The AF-1 domain signals RARγ2 degradation through its phosphorylation by p38MAPK in response to RA. The AF-2 domain acts via the recruitment of SUG-1, which belongs to the 19S regulatory subunit of the 26S proteasome. Blocking RARγ2 degradation through inhibition of either the p38MAPK pathway or the 26S proteasome function impairs its RA-induced transactivation activity. Thus, the turnover of RARγ2 is linked to transactivation.
| Original language | English |
|---|---|
| Pages (from-to) | 3760-3769 |
| Number of pages | 10 |
| Journal | EMBO Journal |
| Volume | 21 |
| Issue number | 14 |
| DOIs | |
| Publication status | Published - Jul 15 2002 |
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Keywords
- Degradation
- p38MAPK
- Phosphorylation
- Proteasome
- RARγ
- Transcription
ASJC Scopus subject areas
- Genetics
- Cell Biology
Cite this
Phosphorylation by p38MAPK and recruitment of SUG-1 are required for RA-induced RARγ degradation and transactivation. / Giannì, Maurizio; Bauer, Annie; Garattini, Enrico; Chambon, Pierre; Rochette-Egly, Cécile.
In: EMBO Journal, Vol. 21, No. 14, 15.07.2002, p. 3760-3769.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Phosphorylation by p38MAPK and recruitment of SUG-1 are required for RA-induced RARγ degradation and transactivation
AU - Giannì, Maurizio
AU - Bauer, Annie
AU - Garattini, Enrico
AU - Chambon, Pierre
AU - Rochette-Egly, Cécile
PY - 2002/7/15
Y1 - 2002/7/15
N2 - The nuclear retinoic acid receptor RARγ2 undergoes proteasome-dependent degradation upon ligand binding. Here we provide evidence that the domains that signal proteasome-mediated degradation overlap with those that activate transcription, i.e. the activation domains AF-1 and AF-2. The AF-1 domain signals RARγ2 degradation through its phosphorylation by p38MAPK in response to RA. The AF-2 domain acts via the recruitment of SUG-1, which belongs to the 19S regulatory subunit of the 26S proteasome. Blocking RARγ2 degradation through inhibition of either the p38MAPK pathway or the 26S proteasome function impairs its RA-induced transactivation activity. Thus, the turnover of RARγ2 is linked to transactivation.
AB - The nuclear retinoic acid receptor RARγ2 undergoes proteasome-dependent degradation upon ligand binding. Here we provide evidence that the domains that signal proteasome-mediated degradation overlap with those that activate transcription, i.e. the activation domains AF-1 and AF-2. The AF-1 domain signals RARγ2 degradation through its phosphorylation by p38MAPK in response to RA. The AF-2 domain acts via the recruitment of SUG-1, which belongs to the 19S regulatory subunit of the 26S proteasome. Blocking RARγ2 degradation through inhibition of either the p38MAPK pathway or the 26S proteasome function impairs its RA-induced transactivation activity. Thus, the turnover of RARγ2 is linked to transactivation.
KW - Degradation
KW - p38MAPK
KW - Phosphorylation
KW - Proteasome
KW - RARγ
KW - Transcription
UR - http://www.scopus.com/inward/record.url?scp=0037099584&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0037099584&partnerID=8YFLogxK
U2 - 10.1093/emboj/cdf374
DO - 10.1093/emboj/cdf374
M3 - Article
VL - 21
SP - 3760
EP - 3769
JO - EMBO Journal
JF - EMBO Journal
SN - 0261-4189
IS - 14
ER -