PMID:15136565

Citation	Yamaguchi, T, Omatsu, N, Matsushita, S and Osumi, T (2004) CGI-58 interacts with perilipin and is localized to lipid droplets. Possible involvement of CGI-58 mislocalization in Chanarin-Dorfman syndrome. J. Biol. Chem. 279:30490-7
Abstract	Lipid droplets (LDs) are a class of ubiquitous cellular organelles that are involved in lipid storage and metabolism. Although the mechanisms of the biogenesis of LDs are still unclear, a set of proteins called the PAT domain family have been characterized as factors associating with LDs. Perilipin, a member of this family, is expressed exclusively in the adipose tissue and regulates the breakdown of triacylglycerol in LDs via its phosphorylation. In this study, we used a yeast two-hybrid system to examine the potential function of perilipin. We found direct interaction between perilipin and CGI-58, a deficiency of which correlated with the pathogenesis of Chanarin-Dorfman syndrome (CDS). Endogenous CGI-58 was distributed predominantly on the surface of LDs in differentiated 3T3-L1 cells, and its expression increased during adipocyte differentiation. Overexpressed CGI-58 tagged with GFP gathered at the surface of LDs and colocalized with perilipin. This interaction seems physiologically important because CGI-58 mutants carrying an amino acid substitution identical to that found in CDS lost the ability to be recruited to LDs. These mutations significantly weakened the binding of CGI-58 with perilipin, indicating that the loss of this interaction is involved in the etiology of CDS. Furthermore, we identified CGI-58 as a binding partner of ADRP, another PAT domain protein expressed ubiquitously, by yeast two-hybrid assay. GFP-CGI-58 expressed in non-differentiated 3T3-L1 or CHO-K1 cells was colocalized with ADRP, and the CGI-58 mutants were not recruited to LDs carrying ADRP, indicating that CGI-58 may also cooperate with ADRP.
Links	PubMed Online version:10.1074/jbc.M403920200
Keywords	1-Acylglycerol-3-Phosphate O-Acyltransferase; 3T3-L1 Cells; Adipocytes/metabolism; Amino Acid Sequence; Animals; Blotting, Western; CHO Cells; Carrier Proteins; Cell Differentiation; Cloning, Molecular; Cricetinae; Cytosol/metabolism; DNA, Complementary/metabolism; Esterases/chemistry; Esterases/metabolism; Genetic Vectors; Glutathione Transferase/metabolism; Humans; Lipase/chemistry; Lipase/metabolism; Lipid Metabolism; Lipids/chemistry; Membrane Proteins/metabolism; Mice; Microscopy, Fluorescence; Molecular Sequence Data; Mutation; Phosphoproteins/chemistry; Phosphoproteins/metabolism; Phosphorylation; Plasmids/metabolism; Point Mutation; Protein Binding; Protein Structure, Tertiary; RNA, Messenger/metabolism; Rats; Recombinant Proteins/chemistry; Sequence Homology, Amino Acid; Syndrome; Time Factors; Transfection; Triglycerides/chemistry; Two-Hybrid System Techniques
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