The perilipin family of structural lipid droplet proteins: stabilization of lipid droplets and control of lipolysis

被引:772
作者
Brasaemle, Dawn L. [1 ]
机构
[1] State Univ New Jersey, Rutgers Ctr Lipids Res, Dept Nutr Sci, New Brunswick, NJ 08901 USA
关键词
adipophilin; adipose differentiation-related protein; TIP47; hormone-sensitive lipase; adipose triglyceride lipase; triacylglycerol; cAMP-dependent protein kinase; adipocyte;
D O I
10.1194/jlr.R700014-JLR200
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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 hormonesensitive 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.
引用
收藏
页码:2547 / 2559
页数:13
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