Recent insights into the structure and function of comparative gene identification-58.

ABSTRACT: 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.

SUBMITTER: Oberer M 

PROVIDER: S-EPMC5808844 | biostudies-literature | 2011 Jun

REPOSITORIES: biostudies-literature