ArticleBiochimica et biophysica acta2014
Adipose triglyceride lipase activity is inhibited by long-chain acyl-coenzyme A.
Article in Biochimica et biophysica acta, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed, 64 citations in OpenAlex.
- Cloning, expression, tertiary structure, activity characteristics, design of inhibitor, hydrolysis and inhibition mechanisms analysis of carp adipose triglyceride lipase (ATGL).Food chemistry. Molecular sciences · 2026Article
- Adipose Tissue Remodeling Beyond Weight Loss: New Insights Into Incretin-Based Therapies and Bariatric Surgery.Current obesity reports · 2026Review
- TMEM120A maintains adipose tissue lipid homeostasis through ER CoA channeling.Nature communications · 2025Article
- Propelling sustainable energy: Multi-omics analysis of pennycress FATTY ACID ELONGATION1 knockout for biofuel production.Plant physiology · 2025Article
- S-acylation of ATGL is required for lipid droplet homoeostasis in hepatocytes.Nature metabolism · 2024Article
- Functional multi-organelle units control inflammatory lipid metabolism of macrophages.Nature cell biology · 2024Article
- A spatiotemporal proteomic map of human adipogenesis.Nature metabolism · 2024Article
- Direct effects of adipocyte lipolysis on AMPK through intracellular long-chain acyl-CoA signaling.Scientific reports · 2024Article
- Unmasking crucial residues in adipose triglyceride lipase for coactivation with comparative gene identification-58.Journal of lipid research · 2024Article
- The PNPLA family of enzymes: characterisation and biological role.Arhiv za higijenu rada i toksikologiju · 2023Article
- A FRET sensor for the real-time detection of long chain acyl-CoAs and synthetic ABHD5 ligands.Cell reports methods · 2023Article
- Approaches to Measuring the Activity of Major Lipolytic and Lipogenic Enzymes In Vitro and Ex Vivo.International journal of molecular sciences · 2022Review
- Expression and production of pigment epithelium-derived factor (PEDF) and PEDF receptor variants from mammalian and bacterial cells.Protein expression and purification · 2022Article
- Article
- Biogenic Phytochemicals Modulating Obesity: From Molecular Mechanism to Preventive and Therapeutic Approaches.Evidence-based complementary and alternative medicine : eCAM · 2022Review
- The Molecular Brakes of Adipose Tissue Lipolysis.Frontiers in physiology · 2022Review
- Adipose Triglyceride Lipase in Hepatic Physiology and Pathophysiology.Biomolecules · 2021Review
- Adipocyte lipolysis: from molecular mechanisms of regulation to disease and therapeutics.The Biochemical journal · 2020Review
- Aquaporin-7: A Dynamic Aquaglyceroporin With Greater Water and Glycerol Permeability Than Its Bacterial Homolog GlpF.Frontiers in physiology · 2020Article
- Of mice and men: The physiological role of adipose triglyceride lipase (ATGL).Biochimica et biophysica acta. Molecular and cell biology of lipids · 2019Review
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Authors and funding
10 authors at 1 institution in 1 country.
Funding
Abstract
Adipose triglyceride lipase (ATGL) is required for efficient mobilization of triglyceride (TG) stores in adipose tissue and non-adipose tissues. Therefore, ATGL strongly determines the availability of fatty acids for metabolic reactions. ATGL activity is regulated by a complex network of lipolytic and anti-lipolytic hormones. These signals control enzyme expression and the interaction of ATGL with the regulatory proteins CGI-58 and G0S2. Up to date, it was unknown whether ATGL activity is also controlled by lipid intermediates generated during lipolysis. Here we show that ATGL activity is inhibited by long-chain acyl-CoAs in a non-competitive manner, similar as previously shown for hormone-sensitive lipase (HSL), the rate-limiting enzyme for diglyceride breakdown in adipose tissue. ATGL activity is only marginally inhibited by medium-chain acyl-CoAs, diglycerides, monoglycerides, and free fatty acids. Immunoprecipitation assays revealed that acyl-CoAs do not disrupt the protein-protein interaction of ATGL and its co-activator CGI-58. Furthermore, inhibition of ATGL is independent of the presence of CGI-58 and occurs directly at the N-terminal patatin-like phospholipase domain of the enzyme. In conclusion, our results suggest that inhibition of the major lipolytic enzymes ATGL and HSL by long-chain acyl-CoAs could represent an effective feedback mechanism controlling lipolysis and protecting cells from lipotoxic concentrations of fatty acids and fatty acid-derived lipid metabolites.
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