Effects of Retinoid Ligands on RIP140: Molecular Interaction with Retinoid Receptors and Biological Activity
Copyright policy )Effects of Retinoid Ligands on RIP140: Molecular Interaction with Retinoid Receptors and Biological Activity
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 (1067)Asn and (1073)Met for a ligand-dependent interaction. A model was proposed to address the constitutive and agonist-dependent interaction of RIP140 with RAR/RXR.
- University of Minnesota Morris United States
- University of Minnesota United States
- University of Minnesota System United States
- University of Tokyo Japan
- Allergan (Ireland) Ireland
Receptors, Retinoic Acid, Molecular Sequence Data, Nuclear Proteins, Ligands, Transfection, Binding, Competitive, Peptide Fragments, Nuclear Receptor Interacting Protein 1, Repressor Proteins, Retinoids, Retinoid X Receptors, Models, Chemical, COS Cells, Chlorocebus aethiops, Animals, Amino Acid Sequence, Dimerization, Adaptor Proteins, Signal Transducing, Protein Binding, Transcription Factors
Receptors, Retinoic Acid, Molecular Sequence Data, Nuclear Proteins, Ligands, Transfection, Binding, Competitive, Peptide Fragments, Nuclear Receptor Interacting Protein 1, Repressor Proteins, Retinoids, Retinoid X Receptors, Models, Chemical, COS Cells, Chlorocebus aethiops, Animals, Amino Acid Sequence, Dimerization, Adaptor Proteins, Signal Transducing, Protein Binding, Transcription Factors
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