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TRIM 24 mediates the interaction of the retinoic acid receptor alpha with the proteasome
Author(s) -
Carrier Marilyn,
Lutzing Regis,
Gaouar Samia,
RochetteEgly Cécile
Publication year - 2018
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.13033
Subject(s) - corepressor , proteasome , ubiquitin , retinoic acid , promoter , retinoic acid receptor , nuclear receptor , microbiology and biotechnology , transcription factor , ubiquitin conjugating enzyme , biology , chemistry , ubiquitin ligase , gene , biochemistry , gene expression
The nuclear retinoic acid ( RA ) receptors ( RAR α, β and γ) are ligand‐dependent regulators of transcription. Upon activation by RA , they are recruited at the promoters of target genes together with several coregulators. Then, they are degraded by the ubiquitin proteasome system. Here, we report that the degradation of the RAR α subtype involves ubiquitination and the tripartite motif protein TRIM 24, which was originally identified as a ligand‐dependent corepressor of RAR α. We show that in response to RA , TRIM 24 serves as an adapter linking RAR α to the proteasome for its degradation. In addition, TRIM 24 and the proteasome are recruited with RAR α to the promoters of target genes and thus are inherently linked to RAR α transcriptional activity.