Lipids are an important form of energy storage in the body, and it is very important to maintain the balance of lipid metabolism in the human body. Disorders of lipid metabolism can lead to diseases such as hyperlipidemia, insulin resistance, diabetes and fatty liver. In cells, lipids are mainly stored in lipid droplets in the form of neutral lipids such as triglycerides and cholesterol esters. PAT family proteins are a class of highly conserved proteins that are specifically localized on the surface of lipid droplets. Previous work found that PAT family proteins are involved in the regulation of lipolysis. However, it is still not clear how the PAT family of protein members divide the work to coordinate lipolysis.
Huang Xun's laboratory of the Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, using Drosophila as a model organism, found that the only two PAT family proteins Plin1 and Plin2 in Drosophila have the same and opposite regulatory functions on lipolysis. The phenotype analysis of Plin1 and Plin2 mutants and overexpressing line adipocytes revealed that Plin1 promoted lipolysis, while Plin2 inhibited lipolysis. Further research found that Plin1 is necessary for the localization of lipase HSL from the cytoplasm to the surface of lipid droplets. In Plin1 and Plin2 double mutant adipocytes, the lipid droplet size and lipid content were significantly lower than those of Plin1 and Plin2 single mutant, indicating that Plin1 also has the function of inhibiting lipolysis. The study also found that the unique C-terminal region of Plin1 determines the difference in function between Plin2 and Plin2.
This study revealed the complex function of Drosophila PAT family proteins in lipolysis, and provided a strong theoretical basis for the subsequent analysis of the evolutionary function of PAT family proteins.
Related research papers were published online in the Journal of Cell Science on April 14. Bi Junfeng and Xiang Yanhui, PhD students in Huang Xun's laboratory, are co-first authors of the paper. The research was completed in cooperation with the Ronald P. Kühnlein laboratory of the Max Planck Institute for Biophysical Chemistry in Germany, and was supported by the Chinese Academy of Sciences, the Ministry of Science and Technology and the National Natural Science Foundation of China.
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