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The novel co‐activator CRABPII binds to RARα and RXRα via two nuclear receptor interacting domains and does not require the AF‐2 ‘core’
Author(s) -
Bastie Jean-Noël,
Despouy Gilles,
Balitrand Nicole,
Rochette-Egly Cécile,
Chomienne Christine,
Delva Laurent
Publication year - 2001
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(01)02938-6
Subject(s) - transactivation , nuclear receptor , retinoid x receptor , activator (genetics) , chemistry , domain (mathematical analysis) , receptor , ligand (biochemistry) , transcription factor , biophysics , biology , biochemistry , mathematics , gene , mathematical analysis
We identify the RARα, RXRα and CRABPII domains required for the physical interaction of these proteins. On RARα and RXRα, 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.