PNPLA-mediated lipid hydrolysis and transacylation - At the intersection of catabolism and anabolism
- PMID: 37951382
- DOI: 10.1016/j.bbalip.2023.159410
PNPLA-mediated lipid hydrolysis and transacylation - At the intersection of catabolism and anabolism
Erratum in
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Corrigendum to "PNPLA-mediated lipid hydrolysis and transacylation - At the intersection of catabolism and anabolism" [Biochim. Biophys. Acta (BBA) - Mol. Cell Biol. Lipids volume 1869, issue 2, March 2024, 159,410].Biochim Biophys Acta Mol Cell Biol Lipids. 2024 May;1869(4):159481. doi: 10.1016/j.bbalip.2024.159481. Epub 2024 Mar 15. Biochim Biophys Acta Mol Cell Biol Lipids. 2024. PMID: 38490127 No abstract available.
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.
Keywords: ATGL; Acyltransferase; Adiponutrin; Lipase; Lipid remodeling; Lipolysis; PNPLA; Transacylation.
Copyright © 2023 The Authors. Published by Elsevier B.V. All rights reserved.
Conflict of interest statement
Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.
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