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• W2023668418 abstract "Ligand-dependent gene transcription mediated by the nuclear receptors involves the recruitment of transcriptional coactivators to the ligand-binding domain (LBD), which leads to interaction with the basal transcription machinery, and ultimately with RNA polymerase II. Although most of these coactivators are ubiquitously expressed, a tissue-selective coactivator, PGC-1, has recently been characterized. Because PGC-1 and the retinoid X receptors (RXRs) possess an overlapping tissue distribution, we investigated whether PGC-1 is a coactivator for the retinoid X receptors. In a transient transfection assay, PGC-1 augments ligand-stimulated RXR transcription. Furthermore, PGC-1 efficiently enhances the RXR element-driven reporter gene transcription by all three RXR isoforms. An immunoprecipitation assay reveals that PGC-1 and RXRα interact in vivo. In addition, a glutathioneS-transferase pull-down assay showed that this interaction requires the presence of the LXXLL motif of PGC-1. We demonstrate further, in a mammalian two-hybrid assay, that this physical interaction also requires the presence of the AF-2 region of RXR to interact with the LXXLL motif of PGC-1, which is consistent with our protein·protein interaction results. A time-resolved fluorescence assay shows that a peptide within the NR box of PGC-1 is efficiently recruited by a ligand-bound RXRα in vitro. Finally, PGC-1 and TIF2 synergistically enhance ligand-activated RXRα transcriptional activity. Taken together, these results indicate that PGC-1 is a bona fide coactivator for RXRα." @default.
• W2023668418 created "2016-06-24" @default.
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• W2023668418 date "2002-02-01" @default.
• W2023668418 modified "2023-10-17" @default.
• W2023668418 title "PGC-1 Functions as a Transcriptional Coactivator for the Retinoid X Receptors" @default.
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• W2023668418 doi "https://doi.org/10.1074/jbc.m109409200" @default.
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