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