Update and nomenclature proposal for mammalian lysophospholipid acyltransferases, which create membrane phospholipid diversity

• Published in: The Journal of biological chemistry Vol. 298; no. 1; p. 101470
• Main Authors: Valentine, William J., Yanagida, Keisuke, Kawana, Hiroki, Kono, Nozomu, Noda, Nobuo N., Aoki, Junken, Shindou, Hideo
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 01.01.2022; American Society for Biochemistry and Molecular Biology
• Subjects: 1-Acylglycerophosphocholine O-Acyltransferase - classification; 1-Acylglycerophosphocholine O-Acyltransferase - metabolism; Animals; cellular membrane; enzyme nomenclature; glycerophospholipid; Glycerophospholipids - metabolism; Humans; JBC Reviews; LPLAT; Lysophospholipids - metabolism; Terminology as Topic; PS; G3P; HHAT; LPSAT; NCBI; CHP1; cellular membrane; AGPAT; SOAT; ER; LPLAT; GNPAT; LCL; pLDDT; glycerophospholipid; GOAT; DHA; LPA; srebp; LPC; LPE; LPG; LPI; PLA; LPL; WAT; LPS; MBOAT; PORCN; enzyme nomenclature; PAFR; sn; LPEAT; LPGAT; KO; LPAAT; LCLAT; LPCAT; CGL; CL; DGAT; CDP-DAG; DAG; LPIAT; COX; PA; PC; PAF; BAT; PE; NEM; PG; PI; TAG; PL; GPAT; PAP
• ISSN: 0021-9258; 1083-351X
• DOI: 10.1016/j.jbc.2021.101470

The diversity of glycerophospholipid species in cellular membranes is immense and affects various biological functions. Glycerol-3-phosphate acyltransferases (GPATs) and lysophospholipid acyltransferases (LPLATs), in concert with phospholipase A1/2s enzymes, contribute to this diversity via selective esterification of fatty acyl chains at the sn-1 or sn-2 positions of membrane phospholipids. These enzymes are conserved across all kingdoms, and in mammals four GPATs of the 1-acylglycerol-3-phosphate O-acyltransferase (AGPAT) family and at least 14 LPLATs, either of the AGPAT or the membrane-bound O-acyltransferase (MBOAT) families, have been identified. Here we provide an overview of the biochemical and biological activities of these mammalian enzymes, including their predicted structures, involvements in human diseases, and essential physiological roles as revealed by gene-deficient mice. Recently, the nomenclature used to refer to these enzymes has generated some confusion due to the use of multiple names to refer to the same enzyme and instances of the same name being used to refer to completely different enzymes. Thus, this review proposes a more uniform LPLAT enzyme nomenclature, as well as providing an update of recent advances made in the study of LPLATs, continuing from our JBC mini review in 2009.