p120 Acts as a Specific Coactivator for 9-cis-Retinoic Acid Receptor (RXR) on Peroxisome Proliferator-Activated Receptor-γ/RXR Heterodimers | Zendy

Tsuyoshi Monden | Zendy; Mikiko Kishi | Zendy; Takeshi Hosoya | Zendy; Teturou Satoh | Zendy; Fredric E. Wondisford | Zendy; Anthony N. Hollenberg | Zendy; Masanobu Yamada | Zendy; Masatomo Mori | Zendy

Open Access

p120 Acts as a Specific Coactivator for 9-cis-Retinoic Acid Receptor (RXR) on Peroxisome Proliferator-Activated Receptor-γ/RXR Heterodimers

Author(s) -

Tsuyoshi Monden,

Mikiko Kishi,

Takeshi Hosoya,

Teturou Satoh,

Fredric E. Wondisford,

Anthony N. Hollenberg,

Masanobu Yamada,

Masatomo Mori

Publication year - 1999

Publication title -

molecular endocrinology

Language(s) - English

Resource type - Journals

eISSN - 1944-9917

pISSN - 0888-8809

DOI - 10.1210/mend.13.10.0353

Subject(s) - retinoid x receptor , coactivator , peroxisome proliferator activated receptor , biology , retinoic acid receptor , nuclear receptor , thyroid hormone receptor , ciglitazone , nuclear receptor coactivator 1 , retinoid x receptor gamma , receptor , transactivation , retinoic acid , transcription factor , biochemistry , microbiology and biotechnology , gene

p120 was originally isolated as a novel nuclear co-activator for thyroid hormone receptor. In this study, we characterized its interaction and transactivation of peroxisome proliferator-activated receptor-gamma (PPARgamma) and 9-cis-retinoic acid receptor (RXR) heterodimers. Transient transfection study revealed that p120 enhanced the transcriptional activation of PPARgamma/RXR induced by PPARgamma- or RXR-specific ligands. In the glutathione-S-transferase pull-down assay, while steroid receptor coactivator-1 showed apparent interactions with both RXR and PPARgamma, p120 bound only to RXR in a 9-cis-retinoic acid (RA)-dependent manner and also did not bind to PPARgamma even in the presence of thiazolidinediones. The yeast two-hybrid analysis showed no interaction of p120 with PPARgamma under any conditions, and electophoretic mobility shift assay showed apparent DNA-PPARgamma/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 PPARgamma via RXR of PPARgamma/RXR heterodimer only in the presence of 9-cis-RA. These findings indicate that p120 acts as a specific co-activator for the RXR of PPARgamma/RXR heterodimer in a 9-cis-RA-dependent manner.

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