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Review
. 2009 Apr;50 Suppl(Suppl):S63-8.
doi: 10.1194/jlr.R800082-JLR200. Epub 2008 Nov 23.

V体育2025版 - Mammalian patatin domain containing proteins: a family with diverse lipolytic activities involved in multiple biological functions

Petra C Kienesberger  1 , Monika Oberer, Achim Lass, Rudolf Zechner
Affiliations
Review

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

Petra C Kienesberger et al. J Lipid Res. 2009 Apr.

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. VSports手机版.

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Figures

Fig. 1.
Fig. 1.
Phylogenetic relationship and structural comparison of proteins within the PNPLA family. The patatin domain in the full-length PNPLA proteins is shown as red box, the vertical line indicates the predicted active site serine. Numbers on the right denote protein lengths in amino acids.
See this image and copyright information in PMC

References

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