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Originally published In Press as doi:10.1194/jlr.R800082-JLR200 on November 23, 2008

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Journal of Lipid Research, Vol. 50, S63-S68, April 2009
Copyright © 2009 by American Society for Biochemistry and Molecular Biology


Enzymology

Mammalian patatin domain containing proteins: a family with diverse lipolytic activities involved in multiple biological functions

Petra C. Kienesberger, Monika Oberer, Achim Lass and Rudolf Zechner1

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


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.

Supplementary key words PNPLA • ATGL • adiponutrin • GS2 • GS2-like • NTE • NRE • iPLA2{gamma} • PLA2G6

Abbreviations: ABHD5, {alpha}/β hydrolase domain containing-5; ATGL, adipose triglyceride lipase; BAT, brown adipose tissue; BMSC, bone marrow stromal cell; CGI-58, comparative gene identification-58; ER, endoplasmic reticulum; FA, fatty acid; GS2, gene sequence-2; HSL, hormone-sensitive lipase; INAD, infantile neuroaxonal dystrophy; iPLA2, calcium-independent phospholipase A2; ko, knockout; LPC, lysophosphatidylcholine; NBIA, neurodegeneration with brain iron accumulation; NRE, neuropathy target esterase-related esterase; NTE, neuropathy target esterase; PC, phosphatidylcholine; PLA, phospholipase A; PLA2G6, phospholipase A2 group VI; PNPLA, patatin-like phospholipase domain containing; RE, retinol ester; TG, triacylglycerol; WAT, white adipose tissue


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Related Webpages:

JLR 50th Anniversary Collections
Anniversary Collection:: Enzymology

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Am. J. Physiol. Endocrinol. Metab.Home page
M. Schweiger, A. Lass, R. Zimmermann, T. O. Eichmann, and R. Zechner
Neutral lipid storage disease: genetic disorders caused by mutations in adipose triglyceride lipase/PNPLA2 or CGI-58/ABHD5
Am J Physiol Endocrinol Metab, August 1, 2009; 297(2): E289 - E296.
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