ArticleJournal of proteome research2009
Lysine methylation of nuclear co-repressor receptor interacting protein 140.
Article in Journal of proteome research, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
14 citing papers in PubMed, 28 citations in OpenAlex.
- Gene-Specific Actions of Transcriptional Coregulators Facilitate Physiological Plasticity: Evidence for a Physiological Coregulator Code.Trends in biochemical sciences · 2020Review
- Retinoic Acid Induces Ubiquitination-Resistant RIP140/LSD1 Complex to Fine-Tune Pax6 Gene in Neuronal Differentiation.Stem cells (Dayton, Ohio) · 2016Article
- RIP140 contributes to foam cell formation and atherosclerosis by regulating cholesterol homeostasis in macrophages.Journal of molecular and cellular cardiology · 2015Article
- The functional diversity of protein lysine methylation.Molecular systems biology · 2014Review
- Cytoplasmic protein methylation is essential for neural crest migration.The Journal of cell biology · 2014Article
- Crystal structures of vertebrate dihydropyrimidinase and complexes from Tetraodon nigroviridis with lysine carbamylation: metal and structural requirements for post-translational modification and function.The Journal of biological chemistry · 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
- 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
- Cholesterol regulation of receptor-interacting protein 140 via microRNA-33 in inflammatory cytokine production.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2011Article
- A negative regulatory pathway of GLUT4 trafficking in adipocyte: new function of RIP140 in the cytoplasm via AS160.Cell metabolism · 2009Article
- RIP140 in thyroid hormone-repression and chromatin remodeling of Crabp1 gene during adipocyte differentiation.Nucleic acids research · 2009Article
- Minireview: role of protein methylation and demethylation in nuclear hormone signaling.Molecular endocrinology (Baltimore, Md.) · 2009Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Receptor interacting protein 140 (RIP140) undergoes extensive post-translational modifications (PTMs), including phosphorylation, acetylation, arginine methylation, and pyridoxylation. PTMs affect its subcellular distribution, protein-protein interaction, and biological activity in adipocyte differentiation. Arginine methylation on Arg(240), Arg(650), and Arg(948) suppresses the repressive activity of RIP140. Here, we find that endogenous RIP140 in differentiated 3T3-L1 cells is also modified by lysine methylation. Three lysine residues, Lys(591), Lys(653), and Lys(757), are mapped as potential methylation sites by mass spectrometry. Site-directed mutagenesis study shows that lysine methylation enhances its gene repressive activity. Mutation of lysine methylation sites enhances arginine methylation, while mutation on arginine methylation sites has little effect on its lysine methylation, suggesting a relationship between lysine methylation and arginine methylation. Kinetic analysis of PTMs of endogenous RIP140 in differentiated 3T3-L1 cells demonstrates sequential modifications on RIP140, initiated from constitutive lysine methylation, followed by increased arginine methylation later in differentiation. This study reveals a potential hierarchy of modifications, at least for lysine and arginine methylation, which bidirectionally regulate the functionality of a nonhistone protein.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.