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Updated: Aug 29, 2026

Promoter Capture Hi-C: High-resolution, Genome-wide Profiling of Promoter Interactions
Published on: June 28, 2018
Characterization of four autonomous repression domains in the corepressor receptor interacting protein 140
Mark Christian1, Jennifer M A Tullet, Malcolm G Parker
1Institute of Reproductive and Developmental Biology, Faculty of Medicine, Imperial College London, London W12 ONN, United Kingdom. m.parker@imperial.ac.uk
Abstract:
Receptor interacting protein (RIP) 140 is a corepressor that can be recruited to nuclear receptors by means of LXXLL motifs. We have characterized four distinct autonomous repression domains in RIP140, termed RD1-4, that are highly conserved in mammals and birds. RD1 at the N terminus represses transcription in the presence of trichostatin A, suggesting that it functions by a histone deacetylase (HDAC)-independent mechanism. The repressive activity of RD2 is dependent upon carboxyl-terminal binding protein recruitment to two specific binding sites. Use of specific inhibitors indicates that RD2, RD3, and RD4 are capable of functioning by HDAC-dependent and HDAC-independent mechanisms, depending upon cell type.
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