Interaction between the Triglyceride Lipase ATGL and the Arf1 Activator GBF1
Copyright policy )Interaction between the Triglyceride Lipase ATGL and the Arf1 Activator GBF1
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.
- Centre national de la recherche scientifique France
- National Institute of Health Pakistan
- King Abdullah University of Science and Technology Saudi Arabia
- National Institute of Child Health and Human Development United States
- National Institute of Health (NIH/NICHD) United States
adipose triglyceride lipase, GBF1 protein, fat droplet, protein binding, immunoprecipitation, Protein Interaction Mapping, guanine nucleotide exchange factor, Guanine Nucleotide Exchange Factors, protein tertiary structure, Microscopy, Immunoelectron, Microscopy, Q, R, coat protein complex I, protein domain, Lipids, unclassified drug, enzyme activity, Golgi complex, Protein Transport, protein protein interaction, Mammalia, protein transport, Medicine, two hybrid system, HeLa cell, signal transduction, Research Article, Protein Binding, intracellular transport, biocatalysis, PNPLA2 protein, membrane transport, Science, protein localization, chemistry, lipid, immunoelectron microscopy, Two-Hybrid System Techniques, Humans, Immunoprecipitation, controlled study, human, cell protein, protein expression, Immunoelectron, carboxy terminal sequence, Golgi Brefeldin A resistance factor 1 protein, Lipase, triacylglycerol lipase, Protein Structure, Tertiary, adenosine diphosphate ribosylation factor 1, protein analysis, Biocatalysis, amino terminal sequence, ADP-Ribosylation Factor 1, metabolism, HeLa Cells
adipose triglyceride lipase, GBF1 protein, fat droplet, protein binding, immunoprecipitation, Protein Interaction Mapping, guanine nucleotide exchange factor, Guanine Nucleotide Exchange Factors, protein tertiary structure, Microscopy, Immunoelectron, Microscopy, Q, R, coat protein complex I, protein domain, Lipids, unclassified drug, enzyme activity, Golgi complex, Protein Transport, protein protein interaction, Mammalia, protein transport, Medicine, two hybrid system, HeLa cell, signal transduction, Research Article, Protein Binding, intracellular transport, biocatalysis, PNPLA2 protein, membrane transport, Science, protein localization, chemistry, lipid, immunoelectron microscopy, Two-Hybrid System Techniques, Humans, Immunoprecipitation, controlled study, human, cell protein, protein expression, Immunoelectron, carboxy terminal sequence, Golgi Brefeldin A resistance factor 1 protein, Lipase, triacylglycerol lipase, Protein Structure, Tertiary, adenosine diphosphate ribosylation factor 1, protein analysis, Biocatalysis, amino terminal sequence, ADP-Ribosylation Factor 1, metabolism, HeLa Cells
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