Related Experiment Video
Updated: Jun 20, 2026

Monitoring Protein-RNA Interaction Dynamics In Vivo at High Temporal Resolution Using χCRAC
Published on: May 9, 2020
Liganded RARalpha and RARgamma interact with but are repressed by TNIP1
Igor Gurevich1, Brian J Aneskievich
1Department of Pharmaceutical Sciences, University of Connecticut, Storrs, CT 06269-3092, USA.
Abstract:
Nuclear receptor (NR) transcriptional activity is controlled by agonist binding and concomitant exchange of receptor-associating corepressor proteins for NR box-containing, receptor AF-2-targeting coactivator proteins. We report here that TNIP1 is an atypical NR coregulator. Requirements for TNIP1-RAR interaction-its NR boxes, ligand, and the receptor's AF-2 domain-are characteristic of coactivators. However, TNIP1 reduces RAR activity. Repression is partially relieved by SRC1, suggesting interference with coactivator recruitment as a mechanism of TNIP1 repression. TNIP1 does not bind RXRalpha and RARalpha AF-2 domain, necessary for that receptor's association with TNIP1, is insufficient to confer upon RXRalpha interaction with TNIP1. Preferential interaction of RARalpha over RARgamma with TNIP1 can be mapped to RARalpha ligand binding domain helices 5-9 and suggests regions outside the receptor helix 12 modulate interaction of NRs and NR box-containing corepressors. TNIP1 repression of RARs in the presence of RA places it in a small category of corepressors of agonist-bound NRs.
Related Concept Videos
Co-activators and Co-repressors
Co-activators and Co-repressors
Regulation of Nuclear Protein Sorting
Prokaryotic Transcriptional Activators and Repressors
Transcription of prokaryotic...
Prokaryotic Transcriptional Activators and Repressors
Transcription of prokaryotic...
Cooperative Binding of Transcription Regulators

