ArticleMolecular and cellular biology2001
Acetylation of nuclear hormone receptor-interacting protein RIP140 regulates binding of the transcriptional corepressor CtBP.
Article in Molecular and cellular biology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.
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Who cites it
55 citing papers in PubMed.
- Characterization of the Crustacean Methyl Farnesoate Transcriptional Signaling Genes.International journal of molecular sciences · 2026Article
- Reciprocal stabilization of CtBP and TRIM28 represses autophagy to promote metastasis.Nature structural & molecular biology · 2025Article
- Regulation of LCoR and RIP140 expression in cervical intraepithelial neoplasia and correlation with CIN progression and dedifferentiation.Journal of cancer research and clinical oncology · 2020Article
- Importance of RIP140 and LCoR Sub-Cellular Localization for Their Association With Breast Cancer Aggressiveness and Patient Survival.Translational oncology · 2018Article
- Discovery at the interface: Toward novel anti-proliferative agents targeting human estrogen receptor/S100 interactions.Cell cycle (Georgetown, Tex.) · 2016Article
- Retinoic Acid Induces Ubiquitination-Resistant RIP140/LSD1 Complex to Fine-Tune Pax6 Gene in Neuronal Differentiation.Stem cells (Dayton, Ohio) · 2016Article
- 20-Hydroxyecdysone (20E) Primary Response Gene E93 Modulates 20E Signaling to Promote Bombyx Larval-Pupal Metamorphosis.The Journal of biological chemistry · 2015Article
- Coordinated repressive chromatin-remodeling of Oct4 and Nanog genes in RA-induced differentiation of embryonic stem cells involves RIP140.Nucleic acids research · 2014Article
- Proteomic analysis of coregulators bound to ERα on DNA and nucleosomes reveals coregulator dynamics.Molecular cell · 2013Article
- C-Terminal Binding Protein: A Molecular Link between Metabolic Imbalance and Epigenetic Regulation in Breast Cancer.International journal of cell biology · 2013Article
- Biological activities of receptor-interacting protein 140 in adipocytes and metabolic diseases.Current diabetes reviews · 2012Review
- NF-κB-mediated degradation of the coactivator RIP140 regulates inflammatory responses and contributes to endotoxin tolerance.Nature immunology · 2012Article
- Control of target gene specificity during metamorphosis by the steroid response gene E93.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Aryl hydrocarbon receptor modulation of estrogen receptor α-mediated gene regulation by a multimeric chromatin complex involving the two receptors and the coregulator RIP140.Toxicological sciences : an official journal of the Society of Toxicology · 2012Article
- Nuclear hormone receptor co-repressors: structure and function.Molecular and cellular endocrinology · 2012Review
- Gene repressive activity of RIP140 through direct interaction with CDK8.Molecular endocrinology (Baltimore, Md.) · 2011Article
- Role of nuclear receptor corepressor RIP140 in metabolic syndrome.Biochimica et biophysica acta · 2011Review
- Regulation of the oncoprotein KLF8 by a switch between acetylation and sumoylation.American journal of translational research · 2011Article
- Manipulating protein acetylation in breast cancer: a promising approach in combination with hormonal therapies?Journal of biomedicine & biotechnology · 2011Review
- Bioinformatic analysis and post-translational modification crosstalk prediction of lysine acetylation.PloS one · 2011Article
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3 authors.
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Abstract
CtBP (carboxyl-terminal binding protein) participates in regulating cellular development and differentiation by associating with a diverse array of transcriptional repressors. Most of these interactions occur through a consensus CtBP-binding motif, PXDLS, in the repressor proteins. We previously showed that the CtBP-binding motif in E1A is flanked by a Lys residue and suggested that acetylation of this residue by the p300/CBP-associated factor P/CAF disrupts the CtBP interaction. In this study, we show that the interaction between CtBP and the nuclear hormone receptor corepressor RIP140 is regulated similarly, in this case by p300/CBP itself. CtBP was shown to interact with RIP140 in vitro and in vivo through a sequence, PIDLSCK, in the amino-terminal third of the RIP140 protein. Acetylation of the Lys residue in this motif, demonstrated in vivo by using an acetylated RIP140-specific antibody, dramatically reduced CtBP binding. Mutation of the Lys residue to Gln resulted in a decrease in CtBP binding in vivo and a loss of transcriptional repression. We suggest that p300/CBP-mediated acetylation disrupts the RIP140-CtBP complex and derepresses nuclear hormone receptor-regulated genes. Disruption of repressor-CtBP interactions by acetylation may be a general mode of gene activation.
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