Colaco-Gaspar_2023_Biochim.Biophys.Acta.Mol.Cell.Biol.Lipids__159410

Reference

Title : PNPLA-mediated lipid hydrolysis and transacylation - At the intersection of catabolism and anabolism - Colaco-Gaspar_2023_Biochim.Biophys.Acta.Mol.Cell.Biol.Lipids__159410
Author(s) : Colaco-Gaspar M , Hofer P , Oberer M , Zechner R
Ref : Biochimica & Biophysica Acta Molecular & Cellular Biology Lipids , :159410 , 2023
Abstract :

Patatin-like phospholipase domain containing proteins (PNPLAs) play diverse roles in lipid metabolism. In this review, we focus on the enzymatic properties and predicted 3D structures of PNPLA1-5, PNPLA2-4 exert both catabolic and anabolic functions. Whereas PNPLA1 is predominantly expressed in the epidermis and involved in sphingolipid biosynthesis, PNPLA2 and 4 are ubiquitously expressed and exhibit several enzymatic activities, including hydrolysis and transacylation of various (glycero-)lipid species. This review summarizes known biological roles for PNPLA-mediated hydrolysis and transacylation reactions and highlights open questions concerning their physiological function.

PubMedSearch : Colaco-Gaspar_2023_Biochim.Biophys.Acta.Mol.Cell.Biol.Lipids__159410
PubMedID: 37951382

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Citations formats

Colaco-Gaspar M, Hofer P, Oberer M, Zechner R (2023)
PNPLA-mediated lipid hydrolysis and transacylation - At the intersection of catabolism and anabolism
Biochimica & Biophysica Acta Molecular & Cellular Biology Lipids :159410

Colaco-Gaspar M, Hofer P, Oberer M, Zechner R (2023)
Biochimica & Biophysica Acta Molecular & Cellular Biology Lipids :159410