Program in Systems Biology; Program in Molecular Medicine
Amino Acids, Peptides, and Proteins | Biochemistry | Cellular and Molecular Physiology | Fungi | Genetic Phenomena | Lipids
Ectopic lipid accumulation in lipid droplets (LD) has been linked to many metabolic diseases. In this study, DHS-3::GFP was used as a LD marker in C. elegans and a forward genetic screen was carried out to find novel LD regulators. There were 140 mutant alleles identified which were divided into four phenotypic categories: enlarged, aggregated, aggregated and small, and decreased. After genetic mapping, mutations in three known LD regulatory genes (maoc-1, dhs-28, daf-22) and a peroxisome-related gene (acox-3) were found to enlarge LDs, demonstrating the reliability of using DHS-3 as a living marker. In the screen, the cytoskeleton protein C27H5.2 was found to be involved in LD aggregation, as was the LD resident/structure-like protein, MDT-28/PLIN-1. Using yeast two-hybrid screening and pull-down assays, MDT-28/PLIN-1 was found to bind to DLC-1 (dynein light chain). Fluorescence imaging confirmed that MDT-28/PLIN-1 mediated the interaction between DHS-3 labeled LDs and DLC-1 labeled microtubules. Furthermore, MDT-28/PLIN-1 was directly bound to DLC-1 through its amino acids 1-210 and 275-415. Taken together, our results suggest that MDT-28/PLIN-1 is involved in the regulation of LD distribution through its interaction with microtubule-related proteins.
Biochemistry, Multivesicular bodies, Organelles
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DOI of Published Version
Sci Rep. 2019 Oct 17;9(1):14902. doi: 10.1038/s41598-019-51399-z. Link to article on publisher's site
Xie K, Zhang P, Na H, Liu Y, Zhang H, Liu P. (2019). MDT-28/PLIN-1 mediates lipid droplet-microtubule interaction via DLC-1 in Caenorhabditis elegans. Open Access Publications by UMMS Authors. https://doi.org/10.1038/s41598-019-51399-z. Retrieved from https://escholarship.umassmed.edu/oapubs/4031
Creative Commons License
This work is licensed under a Creative Commons Attribution 4.0 License.