ArticleCellular signalling2011
Cytoplasmic receptor-interacting protein 140 (RIP140) interacts with perilipin to regulate lipolysis.
Article in Cellular signalling, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 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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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
22 citing papers in PubMed, 29 citations in OpenAlex.
- Lipolysis in Health and Disease: Pathways, Regulation, and Metabolic Consequences.Current diabetes reports · 2026Review
- Human Adipose Tissue Metabolism in Obesity.Journal of obesity & metabolic syndrome · 2025Review
- Recent Insights on the Role of Nuclear Receptors in Alzheimer's Disease: Mechanisms and Therapeutic Application.International journal of molecular sciences · 2025Review
- Selection signature analysis reveals genes associated with tail phenotype in sheep.Frontiers in genetics · 2024Article
- HIF2α-induced upregulation of RNASET2 promotes triglyceride synthesis and enhances cell migration in clear cell renal cell carcinoma.FEBS open bio · 2023Article
- Genome-Wide Association Study Reveals Additive and Non-Additive Effects on Growth Traits in Duroc Pigs.Genes · 2022Article
- Identification of strong candidate genes for backfat and intramuscular fatty acid composition in three crosses based on the Iberian pig.Scientific reports · 2020Article
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- Behavioral stress reduces RIP140 expression in astrocyte and increases brain lipid accumulation.Brain, behavior, and immunity · 2015Article
- RIP140 contributes to foam cell formation and atherosclerosis by regulating cholesterol homeostasis in macrophages.Journal of molecular and cellular cardiology · 2015Article
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- RIP140, a Janus metabolic switch involved in defense functions.Cellular & molecular immunology · 2013Review
- Small GTPase Rab40c associates with lipid droplets and modulates the biogenesis of lipid droplets.PloS one · 2013Article
- Biological activities of receptor-interacting protein 140 in adipocytes and metabolic diseases.Current diabetes reviews · 2012Review
- Endothelin-1 promotes cytoplasmic accumulation of RIP140 through a ET(A)-PLCβ-PKCε pathway.Molecular and cellular endocrinology · 2012Article
- Protein arginine methyltransferase 5 (Prmt5) promotes gene expression of peroxisome proliferator-activated receptor γ2 (PPARγ2) and its target genes during adipogenesis.Molecular endocrinology (Baltimore, Md.) · 2012Article
- FAT SIGNALS--lipases and lipolysis in lipid metabolism and signaling.Cell metabolism · 2012Review
- NF-κB-mediated degradation of the coactivator RIP140 regulates inflammatory responses and contributes to endotoxin tolerance.Nature immunology · 2012Article
- Transcriptional Regulation by Nuclear Corepressors and PGC-1α: Implications for Mitochondrial Quality Control and Insulin Sensitivity.PPAR research · 2012Article
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) is abundantly expressed in mature adipocyte and modulates gene expression involved in lipid and glucose metabolism. Protein kinase C epsilon and protein arginine methyltransferase 1 can sequentially stimulate RIP140 phosphorylation and then methylation, thereby promoting its export to the cytoplasm. Here we report a lipid signal triggering cytoplasmic accumulation of RIP140, and a new functional role for cytoplasmic RIP140 in adipocyte to regulate lipolysis. Increased lipid content, particularly an elevation in diacylglycerol levels, promotes RIP140 cytoplasmic accumulation and increased association with lipid droplets (LDs) by its direct interaction with perilipin. By interacting with RIP140, perilipin more efficiently recruits hormone-sensitive lipase (HSL) to LDs and enhances adipose triglyceride lipase (ATGL) forming complex with CGI-58, an activator of ATGL. Consequentially, HSL can more readily access its substrates, and ATGL is activated, ultimately enhancing lipolysis. In adipocytes, blocking cytoplasmic RIP140 accumulation reduces basal and isoproterenol-stimulated lipolysis and the pro-inflammatory potential of their conditioned media (i.e. activating NF-κB and inflammatory genes in macrophages). These results show that in adipocytes with high lipid contents, RIP140 increasingly accumulates in the cytoplasm and enhances triglyceride catabolism by directly interacting with perilipin. The study suggests that reducing nuclear export of RIP140 might be a useful means of controlling adipocyte lipolysis.
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What OpenQuestion holds
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.