title: Mammalian patatin domain containing proteins: a family with diverse lipolytic activities involved in multiple biological functions.
abstract: 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.
authors.affiliation: Institute of Molecular Biosciences, University of Graz, 8010 Graz, Austria.
authors.forename: Petra C
authors.initials: PC
authors.lastname: Kienesberger
authors.forename: Monika
authors.initials: M
authors.lastname: Oberer
authors.forename: Achim
authors.initials: A
authors.lastname: Lass
authors.forename: Rudolf
authors.initials: R
authors.lastname: Zechner
mesh_terms: D000818:Animals; D001686:Biological Phenomena; D006801:Humans; D015603:Keratinocytes / Q000201:enzymology; D008049:Lipase / Q000737:chemistry / Q000145:classification / Q000235:genetics / Q000378:metabolism*; D008066:Lipolysis; D008322:Mammals / Q000145:classification / Q000235:genetics / Q000378:metabolism*; D014280:Triglycerides / Q000378:metabolism
chemical_list: D014280:Triglycerides; D008049:Lipase