Effects of retinoid ligands on RIP140: Molecular interaction with retinoid receptors and biological activity

Mariya Farooqui, Peter J. Franco, Jim Thompson, Hiroyuki Kagechika, Roshantha A.S. Chandraratna, Len Banaszak, Li Na Wei*

*Corresponding author for this work

Research output: Contribution to journalJournal Article peer-review

22 Scopus citations

Abstract

Receptor interacting protein 140 (RIP140) interacts with retinoic acid receptor (RAR) and retinoid X receptor (RXR) constitutively, but hormone binding enhances this interaction. The ligand-independent interaction is mediated by the amino and central regions of RIP140 which contain a total of nine copies of the LXXLL motif, whereas the agonist-induced interaction is mediated by its carboxyl terminus which contains a novel motif (1063-1076, LTKTNPILYYMLQK). The ligand-independent interaction could be enhanced slightly by agonists, whereas the ligand-dependent interaction was strictly agonist dependent for both RAR and RXR. In the context of heterodimers, ligand occupancy of RXR played a more dominant role for both molecular interaction and biological activity of RIP140. Competition and mutation studies demonstrated an essential role for 1067Asn and 1073Met for a ligand-dependent interaction. A model was proposed to address the constitutive and agonist-dependent interaction of RIP140 with RAR/RXR.

Original languageEnglish
Pages (from-to)971-979
Number of pages9
JournalBiochemistry
Volume42
Issue number4
DOIs
StatePublished - 04 02 2003
Externally publishedYes

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