Phosphorylation of histone H3 is functionally linked to retinoic acid receptor β promoter activation - Inserm - Institut national de la santé et de la recherche médicale Accéder directement au contenu
Article Dans Une Revue EMBO Reports Année : 2002

Phosphorylation of histone H3 is functionally linked to retinoic acid receptor β promoter activation

Résumé

Ligand‐dependent transcriptional activation of retinoic acid receptors (RARs) is a multistep process culminating in the formation of a multimeric co‐activator complex on regulated promoters. Several co‐activator complexes harbor an acetyl transferase activity, which is required for retinoid‐induced transcription of reporter genes. Using murine P19 embryonal carcinoma cells, we examined the relationship between histone post‐translational modifications and activation of the endogenous RARβ2 promoter, which is under the control of a canonical retinoic acid response element and rapidly induced upon retinoid treatment. While histones H3 and H4 were constitutively acetylated at this promoter, retinoid agonists induced a rapid phosphorylation at Ser10 of histone H3. A retinoid antagonist, whose activity was independent of co‐repressor binding to RAR, could oppose this agonist‐induced H3 phosphorylation. Since such post‐translational modifications were not observed at several other promoters, we conclude that histone H3 phosphorylation may be a molecular signature of the activated, retinoid‐controlled mRARβ2 gene promoter.

Dates et versions

inserm-04532312 , version 1 (04-04-2024)

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Citer

Bruno Lefebvre, Keiko Ozato, Philippe Lefebvre. Phosphorylation of histone H3 is functionally linked to retinoic acid receptor β promoter activation. EMBO Reports, 2002, 3 (4), pp.335-340. ⟨10.1093/embo-reports/kvf066⟩. ⟨inserm-04532312⟩

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