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Journal of Lipid Research, Vol. 50, S63-S68, April 2009
Mammalian patatin domain containing proteins: a family with diverse lipolytic activities involved in multiple biological functions
Institute of Molecular Biosciences, University of Graz, 8010 Graz, Austria This research was supported by the grant GOLD - Genomics of Lipid-Associated Disorders, which is part of the Austrian Genome Project GEN-AU Genome research in Austria funded by the Austrian Ministry of Science and Research and by the Austrian Science Foundation (FWF) grant W901-B05DK (Doktoratskolleg Molecular Enzymology) and F30-B05 (SFB Lipotox). Published, JLR Papers in Press, November 23, 2008.
1 To whom correspondence should be addressed. e-mail: rudolf.zechner{at}uni-graz.at
The human genome expresses nine patatin-like phospholipase domain containing proteins (PNPLA1–9). Members of this family share a protein domain discovered initially in patatin, the most abundant protein of the potato tuber. Patatin is a lipid hydrolase with an unusual folding topology that differs from classical lipases. Mammalian PNPLAs include lipid hydrolases with specificities for diverse substrates such as triacylglycerols, phospholipids, and retinol esters. Analysis of induced mutant mouse models and the clinical phenotype of patients with mutations revealed important insights into the physiological role of several members of the PNPLA family. This review aims to summarize current knowledge of PNPLA proteins and to document their emerging importance in lipid and energy homeostasis.
Supplementary key words PNPLA ATGL adiponutrin GS2 GS2-like NTE NRE iPLA2 Abbreviations: ABHD5,
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