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/RXR Heterodimers
First Department of Internal Medicine (T.M., M.K., T.H., T.S.,
M.Y., M.M.) Gunma University School of Medicine Maebashi
371 Japan
Thyroid Unit (F.E.W., A.N.H.) Department of
Medicine Beth Israel Deaconess Medical Center and Harvard Medical
School Boston, Massachusetts 02215
p120 was originally isolated as a novel nuclear
coactivator for thyroid hormone receptor. In this study, we
characterized its interaction and transactivation of peroxisome
proliferator-activated receptor-
(PPAR) and
9-cis-retinoic acid receptor (RXR) heterodimers. Transient
transfection study revealed that p120 enhanced the transcriptional
activation of PPAR/RXR induced by PPAR- or RXR-specific ligands.
In the glutathione-S-transferase pull-down assay, while
steroid receptor coactivator-1 showed apparent interactions with both
RXR and PPAR, p120 bound only to RXR in a 9-cis-retinoic
acid (RA)-dependent manner and also did not bind to PPAR even
in the presence of thiazolidinediones. The yeast two-hybrid
analysis showed no interaction of p120 with PPAR under any
conditions, and electophoretic mobility shift assay showed apparent
DNA-PPAR/RXR/p120 complex formation only in the presence of
9-cis-RA. Furthermore, the yeast three-hybrid assay clearly
revealed a significant interaction between p120 and PPAR via RXR of
PPAR/RXR heterodimer only in the presence of 9-cis-RA.
These findings indicate that p120 acts as a specific coactivator for
the RXR of PPAR/RXR heterodimer in a 9-cis-RA-dependent
manner.
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