Nucleic Acids Research, Vol 24, Issue 2 264-271, Copyright © 1996 by Oxford University Press
DH Dowhan and GE Muscat
The retinoid X receptors alpha, beta and gamma (RXRs) share a highly
conserved 'C' region or DNA binding domain (DBD). The conserved 'DE' region
or ligand binding domain (LBD) of the RXRs is functionally complex,
mediating dimerization and a ligand-dependent activation function (AF-2).
The AB or N-terminal region of the RXRs is poorly conserved and encodes a
ligand-independent activation function (AF-1). RXR gamma mRNA is
preferentially expressed in skeletal and cardiac muscle, however,
cell-specific steroid receptor-mediated trans- activation is a poorly
understood phenomenon. We utilized the GAL4 hybrid assay system and have
demonstrated that RXR gamma contains two functional domains in the AB and
DE regions that activate transcription in a ligand-independent and
-dependent manner respectively. The functions of the AB (AF-1) and DE
(AF-2) domains were regulated by cAMP- dependent protein kinases,
furthermore, the function of AF-2 in the LBD was activated by 8-Br-cAMP,
independent of 9-cis-retinoic acid treatment. Deletion analysis
demonstrated that the AF-1 of RXR gamma, is located between amino acids 1
and 103 and contained multiple motifs that were targets of cAMP-dependent
protein kinases. Transfection analyses in non-muscle and myogenic cells
clearly demonstrated that: (i) the AF-1 of RXR gamma functions in a
muscle-specific manner and is required for optimal ligand-dependent
trans-activation from an RXRE; (ii) RXR gamma trans-activates more
efficiently in a myogenic background.
ARTICLES
Characterization of the AB (AF-1) region in the muscle-specific retinoid X receptor-gamma: evidence that the AF-1 region functions in a cell-specific manner
University of Queensland, Centre for Molecular and Cellular Biology, St Lucia, Australia.
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