Molecular interaction of retinoic acid receptors with coregulators PCAF and RIP140

Yixin Chen, Xinli Hu, Li Na Wei

Research output: Contribution to journalJournal Article peer-review

20 Scopus citations


p300/CBP-associating factor (PCAF) is a ligand-dependent coactivator, whereas receptor-interacting protein 140 (RIP140) is a ligand-dependent negative coregulator for retinoic acid (RA) receptor (RAR) and retinoid X receptor (RXR). To compare these molecular interactions and to determine the effect of RXR ligands, we focus on PCAF/RAR/RXR complex formation in this study for a comparison to RIP140/RAR/RXR complex formation. The LBD of RXR is identified as its primary PCAF-interacting motif. BIAcore studies determine the K d of RAR/RXR association with PCAF as 9.35 nM in the presence of RXR ligand AGN194204, and 47.2 nM in the absence of ligand. Cross-linking study demonstrates tri-molecular complex consisting of one RAR/RXR pair and one PCAF. In competition experiments, RIP140 strongly competes with PCAF for interaction with RAR/RXR both in vitro and in vivo. Chromatin immunoprecipitation demonstrates recruitment of RIP140 and PCAF to the endogenous RA-regulated gene, the RARβ2 promoter. This study presents kinetic evidence for competition of RIP140 with PCAF for ligand-dependent interactions with RAR/RXR, and provides kinetic explanation for the suppressive activity of RIP140 in RA-activated gene expression.

Original languageEnglish
Pages (from-to)43-50
Number of pages8
JournalMolecular and Cellular Endocrinology
Issue number1-2
StatePublished - 29 10 2004
Externally publishedYes


  • BIAcore
  • Kinetics
  • PCAF
  • RAR
  • RIP140
  • RXR


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