ArticleThe Journal of biological chemistry2015
Structure of a CGI-58 motif provides the molecular basis of lipid droplet anchoring.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers, 1 of them a synthesis that pooled it.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
40 citing papers in PubMed, 1 synthesis or guideline pooled it.
- NDRG1 regulates neutral lipid metabolism in breast cancer cells.Breast cancer research : BCR · 2018Pooled it
- Lipolysis gone rogue: the HSL connection in feeding cancer.Cell biology and toxicology · 2025Review
- Crosstalk Between Skeletal Muscle and Proximal Connective Tissues in Lipid Dysregulation in Obesity and Type 2 Diabetes.Metabolites · 2025Review
- Essential Biology of Lipid Droplets.Annual review of biochemistry · 2025Review
- Hepatocyte-specific CLSTN3B ablation impairs lipid droplet maturation and alleviates diet-induced steatohepatitis in mice.bioRxiv : the preprint server for biology · 2025Article
- Unraveling the Molecular Mechanisms of ABHD5 Membrane Targeting.bioRxiv : the preprint server for biology · 2025Article
- Mutational scanning pinpoints distinct binding sites of key ATGL regulators in lipolysis.Nature communications · 2024Article
- Lipid droplets and cellular lipid flux.Nature cell biology · 2024Review
- Unmasking crucial residues in adipose triglyceride lipase for coactivation with comparative gene identification-58.Journal of lipid research · 2024Article
- Structural basis of lipid-droplet localization of 17-beta-hydroxysteroid dehydrogenase 13.Nature communications · 2023Article
- The lipase cofactor CGI58 controls placental lipolysis.JCI insight · 2023Article
- Article
- Computational Studies of Lipid Droplets.The journal of physical chemistry. B · 2022Review
- Structural and functional insights into ABHD5, a ligand-regulated lipase co-activator.Scientific reports · 2022Article
- The CYTOLD and ERTOLD pathways for lipid droplet-protein targeting.Trends in biochemical sciences · 2022Review
- Molecular Modeling of ABHD5 Structure and Ligand Recognition.Frontiers in molecular biosciences · 2022Article
- Adipose Triglyceride Lipase in Hepatic Physiology and Pathophysiology.Biomolecules · 2021Review
- Lipolysis: cellular mechanisms for lipid mobilization from fat stores.Nature metabolism · 2021Review
- Validating an artificial organelle: Studies of lipid droplet-specific proteins on adiposome platform.iScience · 2021Article
- Elevated S-adenosylhomocysteine induces adipocyte dysfunction to promote alcohol-associated liver steatosis.Scientific reports · 2021Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
10 authors.
Funding
Abstract
Triacylglycerols (TGs) stored in lipid droplets (LDs) are hydrolyzed in a highly regulated metabolic process called lipolysis to free fatty acids that serve as energy substrates for β-oxidation, precursors for membrane lipids and signaling molecules. Comparative gene identification-58 (CGI-58) stimulates the enzymatic activity of adipose triglyceride lipase (ATGL), which catalyzes the hydrolysis of TGs to diacylglycerols and free fatty acids. In adipose tissue, protein-protein interactions between CGI-58 and the LD coating protein perilipin 1 restrain the ability of CGI-58 to activate ATGL under basal conditions. Phosphorylation of perilipin 1 disrupts these interactions and mobilizes CGI-58 for the activation of ATGL. We have previously demonstrated that the removal of a peptide at the N terminus (residues 10-31) of CGI-58 abrogates CGI-58 localization to LDs and CGI-58-mediated activation of ATGL. Here, we show that this tryptophan-rich N-terminal peptide serves as an independent LD anchor, with its three tryptophans serving as focal points of the left (harboring Trp(21) and Trp(25)) and right (harboring Trp(29)) anchor arms. The solution state NMR structure of a peptide comprising the LD anchor bound to dodecylphosphocholine micelles as LD mimic reveals that the left arm forms a concise hydrophobic core comprising tryptophans Trp(21) and Trp(25) and two adjacent leucines. Trp(29) serves as the core of a functionally independent anchor arm. Consequently, simultaneous tryptophan alanine permutations in both arms abolish localization and activity of CGI-58 as opposed to tryptophan substitutions that occur in only one arm.
Indexed as
Identifiers
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.