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J Biol Chem, Vol. 274, Issue 34, 23695-23698, August 20, 1999
From the Cornell University, Division of Nutritional Sciences,
Savage Hall, Ithaca, New York 14853
The pleiotropic effects of retinoic acid (RA) in
mammalian cells are mediated by two classes of proteins: the retinoic
acid receptors (RAR) and cellular retinoic acid-binding proteins
(CRABP-I and CRABP-II). Here we show that expression of CRABP-II, but
not CRABP-I, markedly enhanced RAR-mediated transcriptional activation of a reporter gene in COS-7 cells. The equilibrium dissociation constants of complexes of CRABP-I or CRABP-II with RA were found to
differ by 2-fold. It is thus unlikely that the distinct effects of the
two proteins on transactivation stem from differential ligand-binding
affinities. The mechanisms by which RA transfers from the CRABPs to RAR
were thus investigated directly. The rate constant for movement of RA
from CRABP-II, but not from CRABP-I, to RAR strongly depended on the
concentration of the acceptor. The data suggest that transfer of RA
from CRABP-I to RAR involves dissociation of the ligand from the
binding protein, followed by association with the receptor. In
contrast, movement of RA from CRABP-II to the receptor is facilitated
by a mechanism that involves direct interactions between CRABP-II and
RAR. These findings reveal a striking functional difference between
CRABP-I and CRABP-II, and point at a novel mechanism by which the
transcriptional activity of RA can be regulated by CRABP-II.
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