Interaction between Triglyceride Lipase ATGL and Arf1 Activator GBF1
Author Information
Author(s): Emy Njoh Ellong, Soni Krishnakant G., Bui Quynh-Trang, Sougrat Rachid, Golinelli-Cohen Marie-Pierre, Jackson Catherine L.
Primary Institution: Laboratoire d'Enzymologie et Biochimie Structurales, CNRS, Gif-sur-Yvette, France; Cell Biology and Metabolism Program, Eunice Kennedy Shriver National Institute of Child Health and Human Development, NIH, Bethesda, Maryland, USA
Hypothesis
Does GBF1 interact with ATGL and play a role in its localization to lipid droplets?
Conclusion
The study demonstrates that GBF1 directly interacts with ATGL and is essential for its delivery to lipid droplets.
Supporting Evidence
- GBF1 and ATGL interact directly through multiple contact sites.
- The C-terminal region of ATGL interacts with the N-terminal domains of GBF1.
- Depletion of GBF1 results in larger lipid droplets in HeLa cells.
Takeaway
This study found that a protein called GBF1 helps another protein, ATGL, get to where it needs to be in the cell to do its job with fat.
Methodology
The study used yeast two-hybrid screening, co-immunoprecipitation in mammalian cells, and direct protein binding assays to investigate the interaction between GBF1 and ATGL.
Limitations
The interactions observed may not fully represent physiological conditions due to the experimental setup.
Digital Object Identifier (DOI)
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