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• W1992206514 abstract "Using the DNA-binding domain (DBD) and hinge region of human peroxisome proliferator-activated receptor (PPAR)-γ as bait in yeast two-hybrid screen, we isolated partial cDNA identical with that of the C terminal of KIAA1769. KIAA1769 encodes a 2080-amino acid protein (molecular mass, 231 kDa) that was recently identified to interact with PPARα and termed PPARα-interacting cofactor 285 (here referred to as PPARγ-DBD-interacting protein 1 (PDIP1)-α). PDIP1 mRNA was expressed in 3T3-L1 adipocytes and THP-1 macrophages. We also identified the expression of the N terminal extended form of PDIP1α (referred to as PDIP1β) consisting of 2649 amino acids (295 kDa) in human cultured cell lines by RT-PCR, and 5′ rapid amplification of cDNA ends. Ribonuclease protection assay revealed that PDIP1β mRNA was expressed more abundantly than PDIP1α mRNA. The C-terminal region of PDIP1 directly binds DBD of PPARγ, and multiple LXXLL motifs in PDIP1 were not required for the interaction. PDIP1α and -β similarly enhanced PPARγ-mediated transactivation in transfection assays and short interfering RNA targeting PDIP1 mRNA significantly reduced transactivation by PPARγ. No potent intrinsic activation domain was identified in either PDIP1 isoforms in mammalian one-hybrid assays, and mutation of all LXXLL motifs did not affect enhancement of PPARγ-mediated transactivation. PDIP1α and -β similarly augmented transactivation by PPARα, PPARδ, thyroid hormone receptor (TR)-α1, TRβ1, and retinoid X receptor-α. PDIP1α also enhanced estrogen receptorα- and androgen receptor-mediated transactivation, whereas PDIP1β did not. PDIP1α showed receptor-specific synergism with activation function-2-interacting coactivators in PPARγ- and TRβ1-mediated transactivation. Together, PDIP1 might function as a transcriptional cofactor for a broad range of nuclear receptors, possibly in collaboration with specific activation function-2 interacting coactivators." @default.
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• W1992206514 date "2006-01-01" @default.
• W1992206514 modified "2023-09-23" @default.
• W1992206514 title "Isolation and Characterization of a Transcriptional Cofactor and Its Novel Isoform that Bind the Deoxyribonucleic Acid-Binding Domain of Peroxisome Proliferator-Activated Receptor-γ" @default.
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• W1992206514 doi "https://doi.org/10.1210/en.2005-0450" @default.
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