ArticlePloS one2011
Interaction between the triglyceride lipase ATGL and the Arf1 activator GBF1.
Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 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.
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.
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Who cites it
44 citing papers in PubMed, 62 citations in OpenAlex.
- Perilipin 3 Differentially Regulates Skeletal Muscle Lipid Oxidation in Active, Sedentary, and Type 2 Diabetic Males.The Journal of clinical endocrinology and metabolism · 2015Trial
- Mitochondrial dysfunction and lipid droplet dynamics in MASH: HSD17B13 as a therapeutic target.Frontiers in cell and developmental biology · 2026Review
- Arfs on the Golgi: four conductors, one orchestra.Frontiers in molecular biosciences · 2025Review
- LET-767 determines lipid droplet protein targeting and lipid homeostasis.The Journal of cell biology · 2024Article
- Mutational scanning pinpoints distinct binding sites of key ATGL regulators in lipolysis.Nature communications · 2024Article
- Site-specific phosphorylations of the Arf activator GBF1 differentially regulate GBF1 function in Golgi homeostasis and secretion versus cytokinesis.Scientific reports · 2023Article
- Arf1 coordinates fatty acid metabolism and mitochondrial homeostasis.Nature cell biology · 2023Article
- Dynamic Regulation of Lipid Droplet Biogenesis in Plant Cells and Proteins Involved in the Process.International journal of molecular sciences · 2023Review
- Article
- Receptors that bind to PEDF and their therapeutic roles in retinal diseases.Frontiers in endocrinology · 2023Review
- Identification of motifs and mechanisms for lipid droplet targeting of the lipolytic inhibitors G0S2 and HIG2.Journal of cell science · 2022Article
- Identification of two pathways mediating protein targeting from ER to lipid droplets.Nature cell biology · 2022Article
- The multifaceted roles of ER and Golgi in metabolic cardiomyopathy.Frontiers in cardiovascular medicine · 2022Review
- Lipolysis: cellular mechanisms for lipid mobilization from fat stores.Nature metabolism · 2021Review
- Picornaviruses: A View from 3A.Viruses · 2021Review
- Viral protein engagement of GBF1 induces host cell vulnerability through synthetic lethality.bioRxiv : the preprint server for biology · 2020Article
- OSBPL2 Is Required for the Binding of COPB1 to ATGL and the Regulation of Lipid Droplet Lipolysis.iScience · 2020Article
- Role of the Guanine Nucleotide Exchange Factor GBF1 in the Replication of RNA Viruses.Viruses · 2020Review
- The ATGL lipase cooperates with ABHD5 to mobilize lipids for hepatitis C virus assembly.PLoS pathogens · 2020Article
- The Lipolysome-A Highly Complex and Dynamic Protein Network Orchestrating Cytoplasmic Triacylglycerol Degradation.Metabolites · 2020Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
Abstract
The Arf1 exchange factor GBF1 (Golgi Brefeldin A resistance factor 1) and its effector COPI are required for delivery of ATGL (adipose triglyceride lipase) to lipid droplets (LDs). Using yeast two hybrid, co-immunoprecipitation in mammalian cells and direct protein binding approaches, we report here that GBF1 and ATGL interact directly and in cells, through multiple contact sites on each protein. The C-terminal region of ATGL interacts with N-terminal domains of GBF1, including the catalytic Sec7 domain, but not with full-length GBF1 or its entire N-terminus. The N-terminal lipase domain of ATGL (called the patatin domain) interacts with two C-terminal domains of GBF1, HDS (Homology downstream of Sec7) 1 and HDS2. These two domains of GBF1 localize to lipid droplets when expressed alone in cells, but not to the Golgi, unlike the full-length GBF1 protein, which localizes to both. We suggest that interaction of GBF1 with ATGL may be involved in the membrane trafficking pathway mediated by GBF1, Arf1 and COPI that contributes to the localization of ATGL to lipid droplets.
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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.