Journal
CURRENT OPINION IN LIPIDOLOGY
Volume 22, Issue 3, Pages 149-158Publisher
LIPPINCOTT WILLIAMS & WILKINS
DOI: 10.1097/MOL.0b013e328346230e
Keywords
alpha beta-hydrolase; adipose triglyceride lipase activation; lipid metabolism; lysophosphatidic acid acyltransferase
Funding
- Austrian Federal Ministry of Science and Research
- FFG
- SFB LIPOTOX [F30]
- 'DK Molecular Enzymology' [W901-B05]
- Austrian Science Fund (FWF)
- [P22170]
- Austrian Science Fund (FWF) [P22170] Funding Source: Austrian Science Fund (FWF)
- Austrian Science Fund (FWF) [W 901, F 3002, P 22170, Z 136] Funding Source: researchfish
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Purpose of review Comparative gene identification-58 (CGI-58) is an important player in lipid metabolism. It acts as activator of triglyceride hydrolases and as acyl-CoA-dependent lysophosphatidic acid acyltransferase. This review aims at establishing a structure-function relationship of this still rather enigmatic protein based on recent studies characterizing different functions of CGI-58. Recent findings Novel studies confirm the important regulatory role of CGI-58 as activator of the triglyceride hydrolase adipose triglyceride lipase. New evidence, corroborated by the characterization of a CGI-58 knockout mouse model, also suggests the existence of yet unknown lipases that are activated by CGI-58. Additionally, CGI-58 was identified to exert acyl-CoA-dependent lysophosphatidic acid acyltransferase activity, which implies possible roles in triglyceride or phospholipid synthesis or signaling processes. Unlike mammalian CGI-58 proteins, orthologs from plants and yeast additionally act as weak triglyceride and phospholipid hydrolases. A first three-dimensional model was calculated and allows preliminary structural considerations for the functions of CGI-58. Summary Despite important progress concerning the different biochemical functions of CGI-58, the physiological importance of these activities requires better characterization. Furthermore, three-dimensional structural data for CGI-58 are required to unveil the molecular mechanism of how CGI-58 acts as activator of lipases and exerts its enzymatic functions.
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