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J. Biol. Chem., Vol. 275, Issue 21, 16302-16308, May 26, 2000
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From the A transcriptional coactivator of the peroxisome
proliferator-activated receptor-
Modulation of Estrogen Receptor-
Transcriptional Activity
by the Coactivator PGC-1*
,,¶
Department of Pharmacology and Cancer
Biology, Duke University Medical Center, Durham, North Carolina
27710 and § Dana-Farber Cancer Institute, Harvard Medical
School, Boston, Massachusetts 02115
(PPAR),
PPAR-coactivator-1(PGC-1) interacts in a constitutive manner with
the hinge domain of PPAR and enhances its transcriptional activity.
In this study we demonstrate that PGC-1 is a coactivator of estrogen
receptor-
(ER)-dependent transcriptional activity.
However the mechanism by which PGC-1 interacts with ER is different
from that of PPAR. Specifically, it was determined that the carboxyl
terminus of PGC-1 interacts in a ligand-independent manner with the
ER hinge domain. In addition, an LXXLL motif within the
amino terminus of PGC-1 was shown to interact in an
agonist-dependent manner with the AF2 domain within the
carboxyl terminus of ER. The ability of PGC-1 to associate with and
potentiate the transcriptional activity of an ER-AF2 mutant that is
unable to interact with the p160 class of coactivators suggests that
this coactivator may have a unique role in estrogen signaling. It is
concluded from these studies that PGC-1 is a bona fide
ER coactivator, which may serve as a convergence point between
PPAR and ER signaling.
*
This work was supported by Grant DK48807 (to D. P. M.) from the National Institutes of Health.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
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