PNPLA-mediated lipid hydrolysis and transacylation - At the intersection of catabolism and anabolism

Biochim Biophys Acta Mol Cell Biol Lipids. 2024 Mar;1869(2):159410. doi: 10.1016/j.bbalip.2023.159410. Epub 2023 Nov 9.

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.

Publication types

  • Review
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Epidermis / metabolism
  • Hydrolysis
  • Lipase* / metabolism
  • Lipid Metabolism*
  • Lipids

Substances

  • Lipase
  • Lipids