Cullin 3 mediates SRC-3 ubiquitination and degradation to control the retinoic acid response

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Abstract

SRC-3 is an important coactivator of nuclear receptors including the retinoic acid (RA) receptor α. 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 antiproliferative effect of RA.

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Ferry, C., Gaouar, S., Fischer, B., Boeglin, M., Paul, N., Samarut, E., … Rochette-Egly, C. (2011). Cullin 3 mediates SRC-3 ubiquitination and degradation to control the retinoic acid response. Proceedings of the National Academy of Sciences of the United States of America, 108(51), 20603–20608. https://doi.org/10.1073/pnas.1102572108

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