Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 108, Issue 51, Pages 20603-20608Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1102572108
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Funding
- Centre National de la Recherche Scientifique
- Institut National de la Sante et de la Recherche Medicale
- Agence Nationale pour la Recherche [ANR-05-BLAN-0390-02, ANR-09-BLAN-0297-01]
- Association pour la Recherche sur le Cancer [ARC-07-1-3169]
- Fondation pour la Recherche Medicale (FRM) [DEQ20090515423]
- Institut National du Cancer [INCa-PL09-194, PL07-96099]
- Ministere de l'Enseignement Superieur et de la Recherche
- FRM
- Lady TATA Memorial Trust
- Agence Nationale de la Recherche (ANR) [ANR-05-BLAN-0390, ANR-09-BLAN-0297] Funding Source: Agence Nationale de la Recherche (ANR)
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SRC-3 is an important coactivator of nuclear receptors including the retinoic acid (RA) receptor a. Most of SRC-3 functions are facilitated by changes in the posttranslational code of the protein that involves mainly phosphorylation and ubiquitination. We recently reported that SRC-3 is degraded by the proteasome in response to RA. Here, by using an RNAi E3-ubiquitin ligase entry screen, we identified CUL-3 and RBX1 as components of the E3 ubiquitin ligase involved in the RA-induced ubiquitination and subsequent degradation of SRC-3. We also show that the RA-induced ubiquitination of SRC-3 depends on its prior phosphorylation at serine 860 that promotes binding of the CUL-3-based E3 ligase in the nucleus. Finally, phosphorylation, ubiquitination, and degradation of SRC-3 cooperate to control the dynamics of transcription. In all, this process participates to the anti-proliferative effect of RA.
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