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- 주제어 : Nuclear receptor coactivator (검색결과 4 건)
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Kim, Mi Ae,Kim, Gil Jung,Maeng, Sejung,Jin, Deuk-Hee,Sohn, Young Chang Elsevier 2011 Molecular and cellular endocrinology Vol.331 No.1
<P><B>Abstract</B></P><P>Ligand-bound nuclear receptors (NRs) recruit coactivators such as members of the p160 steroid receptor coactivator (SRC) family and cyclic AMP responsive element binding protein (CREB)-binding protein (CBP) to specific enhancer elements and activate target gene transcription. In the present study, we isolated a novel SRC from the sea urchin <I>Strongylocentrotus nudus</I> (SnSRC) by using the ligand-binding domain of retinoid X receptor as a bait in a yeast two-hybrid screening. The SnSRC and vertebrate SRCs are different in size but share the overall characteristic domains, such as NR interacting domain (NID), CBP-binding and glutamine-rich regions. <I>SnSRC</I> mRNA showed highest expression levels at the 32-cell, 64-cell and pluteus larval stages. Full-length SnSRC (1992 amino acids) interacted with several NRs, including sea urchin estrogen receptor-related receptor (ERR), human and masu salmon estrogen receptors (ERα), mouse ERRγ, rat glucocorticoid receptor α, and rat thyroid receptor β. The SnSRC possesses two functional NIDs, both of which are dependent on their core LxxLL motifs. Furthermore, preferential interacting domains for ERα in the SnSRC are located in the central LxxLL motifs, revealed by the truncation and mutagenesis studies. Strikingly, the SnSRC has a single transcription activation domain, which interacts with CBP, a transcriptional integrator. In addition, transient knockdown of the <I>SnSRC</I> gene in the sea urchin embryo using morpholino antisense RNA induced abnormal phenotypes at gastrulation stage such as the lack of primary invagitation and exogastrulation. These results suggest that the SnSRC is a new member of the SRC family and plays an important role during early embryonic development.</P>
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Kim, Seung-Whan,Kim, Han-Jong,Jung, Dong-Ju,Lee, Soo-Kyung,Kim, Youn-Sung,Kim, Jae Hong,Kim, Tae Sung,Lee, Jae Woon 전남대학교 약품개발연구소 2001 약품개발연구지 Vol.10 No.-
Transcriptional coactivators SRC-1 and p300 specifically interact with liganded-nuclear receptors and also modulate other transcription factors, including serum response factor (SRF). Here, we report that retinoids repress transactivation by SRF and specific interactions exist between the DNA binding domains of SRF and retinoic acid and retinoid X receptors. We further demonstrate that the repression may involve retinoiddependent competition for a limiting amount of SRC-1 and p300 between SRF and retinoid receptors. We propose that the well-defined anti-proliferative action of retinoids could, at least in part, result from this novel transrepressive action on the mitogenic transcription factor SRF.
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Kyurae Kim,Myung-Ho Kim,Ji In Kang,Jong-In Baek,Byeong-Min Jeon,Ho Min Kim,Sun-Chang Kim,Won-Il Jeong 고려인삼학회 2024 Journal of Ginseng Research Vol.48 No.1
Background: Ginsenoside F2 (GF2), the protopanaxadiol-type constituent in Panax ginseng, has been reported toattenuate metabolic dysfunction-associated steatotic liver disease (MASLD). However, the mechanism of action isnot fully understood. Here, this study investigates the molecular mechanism by which GF2 regulates MASLDprogression through liver X receptor (LXR). Methods: To demonstrate the effect of GF2 on LXR activity, computational modeling of protein-ligand binding,Time-resolved fluorescence resonance energy transfer (TR-FRET) assay for LXR cofactor recruitment, andluciferase reporter assay were performed. LXR agonist T0901317 was used for LXR activation in hepatocytes andmacrophages. MASLD was induced by high-fat diet (HFD) feeding with or without GF2 administration in WT andLXRα / mice. Results: Computational modeling showed that GF2 had a high affinity with LXRα. LXRE-luciferase reporter assaywith amino acid substitution at the predicted ligand binding site revealed that the S264 residue of LXRα was thecrucial interaction site of GF2. TR-FRET assay demonstrated that GF2 suppressed LXRα activity by favoring thebinding of corepressors to LXRα while inhibiting the accessibility of coactivators. In vitro, GF2 treatments reducedT0901317-induced fat accumulation and pro-inflammatory cytokine expression in hepatocytes and macrophages,respectively. Consistently, GF2 administration ameliorated hepatic steatohepatitis and improved glucoseor insulin tolerance in WT but not in LXRα / mice. Conclusion: GF2 alters the binding affinities of LXRα coregulators, thereby interrupting hepatic steatosis andinflammation in macrophages. Therefore, we propose that GF2 might be a potential therapeutic agent for theintervention in patients with MASLD.
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Regulation of Hepatic Gluconeogenesis by Nuclear Receptor Coactivator 6
오경식,김시령,이은숙,윤진,류현경,김동섭,Seung-Whan Kim,Min-Kyung Shin 한국분자세포생물학회 2022 Molecules and cells Vol.45 No.4
Nuclear receptor coactivator 6 (NCOA6) is a transcriptional coactivator of nuclear receptors and other transcription factors. A general Ncoa6 knockout mouse was previously shown to be embryonic lethal, but we here generated liver-specific Ncoa6 knockout (Ncoa6 LKO) mice to investigate the metabolic function of NCOA6 in the liver. These Ncoa6 LKO mice exhibited similar blood glucose and insulin levels to wild type but showed improvements in glucose tolerance, insulin sensitivity, and pyruvate tolerance. The decrease in glucose production from pyruvate in these LKO mice was consistent with the abrogation of the fasting-stimulated induction of gluconeogenic genes, phosphoenolpyruvate carboxykinase 1 (Pck1) and glucose-6-phosphatase (G6pc). The forskolin-stimulated inductions of Pck1 and G6pc were also dramatically reduced in primary hepatocytes isolated from Ncoa6 LKO mice, whereas the expression levels of other gluconeogenic gene regulators, including cAMP response element binding protein (Creb), forkhead box protein O1 and peroxisome proliferator-activated receptor γ coactivator 1α, were unaltered in the LKO mouse livers. CREB phosphorylation via fasting or forskolin stimulation was normal in the livers and primary hepatocytes of the LKO mice. Notably, it was observed that CREB interacts with NCOA6. The transcriptional activity of CREB was found to be enhanced by NCOA6 in the context of Pck1 and G6pc promoters. NCOA6-dependent augmentation was abolished in cAMP response element (CRE) mutant promoters of the Pck1 and G6pc genes. Our present results suggest that NCOA6 regulates hepatic gluconeogenesis by modulating glucagon/cAMP-dependent gluconeogenic gene transcription through an interaction with CREB.
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