Thematic review series: Adipocyte Biology. The perilipin family of structural lipid droplet proteins: stabilization of lipid droplets and control of lipolysis Published, JLR Papers in Press,…

By D. Brasaemle. Journal of Lipid Research, 2007

855 citations recorded by the source corpus.

The majority of eukaryotic cells synthesize neutral lipids and package them into cytosolic lipid droplets. In vertebrates, triacylglycerol-rich lipid droplets of adipocytes provide a major energy storage depot for the body, whereas cholesteryl ester-rich droplets of many other cells provide building materials for local membrane synthesis and repair. These lipid droplets are coated with one or more of five members of the perilipin family of proteins: adipophilin, TIP47, OXPAT/MLDP, S3-12, and perilipin. Members of this family share varying levels of sequence similarity, lipid droplet association, and functions in stabilizing lipid droplets. The most highly studied member of the family, perilipin, is the most abundant protein on the surfaces of adipocyte lipid droplets, and the major substrate for cAMP-dependent protein kinase [protein kinase A (PKA)] in lipolytically stimulated adipocytes. Perilipin serves important functions in the regulation of basal and hormonally stimulated lipolysis. Under basal conditions, perilipin restricts the access of cytosolic lipases to lipid droplets and thus promotes triacylglycerol storage. In times of energy deficit, perilipin is phosphorylated by PKA and facilitates maximal lipolysis by hormone-sensitive lipase and adipose triglyceride lipase. A model is discussed whereby perilipin serves as a dynamic scaffold to coordinate the access of enzymes to the lipid droplet in a manner that is responsive to the metabolic status of the adipocyte.

Subfields: Biochemistry, Molecular Biology, Plant Science

View Paper: https://www.semanticscholar.org/paper/efc5aa46389d1d8f1de6f8aae28dc5ca910d5fde

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In Biochemistry

1. Max C. Petersen
2. M. Czech
3. B. Neuschwander‐Tetri
4. Gerald I. Shulman
5. E. Arrese
6. J. Soulages

In Molecular Biology

1. Max C. Petersen
2. Gerald I. Shulman
3. M. Czech
4. B. Neuschwander‐Tetri
5. E. Arrese
6. J. Soulages
7. Ralph DeFronzo

In Plant Science

1. B. Neuschwander‐Tetri
2. Gerald I. Shulman
3. E. Arrese
4. J. Soulages
5. Max C. Petersen

Citations in the corpus

• INSECT FAT BODY: ENERGY, METABOLISM, AND REGULATION (2010, background): “This process seems to be controlled by evolutionarily conserved proteins from the PAT family, which is a group of proteins that share sequence similarity and localize to lipid droplets (24,26).”
• Mechanisms of Insulin Action and Insulin Resistance. (2018, background): “PLIN1 is highly expressed in white adipocytes and is phosphorylated by PKA at several serine residues (93, 531, 946).”
• Adipocyte dysfunctions linking obesity to insulin resistance and type 2 diabetes (2008, background): “The perilipin family of lipid-droplet proteins is involved in packaging of fat droplets and control of lipolysi”
• Hepatic lipotoxicity and the pathogenesis of nonalcoholic steatohepatitis: The central role of nontriglyceride fatty acid metabolites (2010, background): “The tissue specificity and regulation of these pathways has been reviewed.(66,69,70,72) ACSL, acyl-CoA synthase; AGPAT, acyl-glycerolphosphate acyltransferase; ATGL, adipose triglyceride lipase; CPT, choline phosphotransferase; DAGK, diacylglycerol kinase; DGATs, diacylglycerol acyltransferases; GPA”