The novel co-activator CRABPII binds to RARalpha and RXRalpha via two nuclear receptor interacting domains and does not require the AF-2 'core'.

Date publication

octobre 2001

Journal

FEBS letters

Auteurs

Membres identifiés du Cancéropôle Est :
Pr BASTIE Jean-Noël , Dr DELVA Laurent , Dr ROCHETTE-EGLY Cécile , Dr DESPOUY Gilles

Tous les auteurs :
Bastie JN, Despouy G, Balitrand N, Rochette-Egly C, Chomienne C, Delva L

Lien Pubmed

https://www.ncbi.nlm.nih.gov/pubmed/11682061

Résumé

We identify the RARalpha, RXRalpha and CRABPII domains required for the physical interaction of these proteins. On RARalpha and RXRalpha, the sequences correspond to the DEF and DE domains, respectively, but the interaction with CRABPII does not require the AF-2AD 'core'. On CRABPII, two interacting domains are identified (NRID1 and NRID2), one of which contains the only enhancement transactivation domain of CRABPII. The interaction is ligand-independent and does not require the ligand-binding domain of CRABPII. These results further stress that interaction of CRABPII with the nuclear receptors defines a novel level of transcriptional control.

Mots clés

Animals, Base Sequence, Binding Sites, COS Cells, DNA Primers, genetics, Humans, In Vitro Techniques, Ligands, Models, Molecular, Protein Structure, Tertiary, Receptors, Retinoic Acid, chemistry, Recombinant Fusion Proteins, chemistry, Retinoic Acid Receptor alpha, Retinoid X Receptors, Transcription Factors, chemistry

Référence

FEBS Lett.. 2001 Oct;507(1):67-73