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

William J Valentine; Keisuke Yanagida; Hiroki Kawana; Nozomu Kono; Nobuo N Noda; Junken Aoki; Hideo Shindou

doi:10.1016/j.jbc.2021.101470

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

J Biol Chem. 2022 Jan;298(1):101470. doi: 10.1016/j.jbc.2021.101470. Epub 2021 Dec 7.

Authors

William J Valentine¹, Keisuke Yanagida², Hiroki Kawana³, Nozomu Kono³, Nobuo N Noda⁴, Junken Aoki³, Hideo Shindou⁵

Affiliations

¹ Department of Lipid Signaling, National Center for Global Health and Medicine (NCGM), Shinjuku-ku, Tokyo, Japan; Department of Molecular Therapy, National Institute of Neuroscience, National Center of Neurology and Psychiatry (NCNP), Kodaira, Tokyo, Japan.
² Department of Lipid Signaling, National Center for Global Health and Medicine (NCGM), Shinjuku-ku, Tokyo, Japan.
³ Department of Health Chemistry, Graduate School of Pharmaceutical Sciences, The University of Tokyo, Bunkyo-ku, Tokyo, Japan.
⁴ Institute of Microbial Chemistry (BIKAKEN), Microbial Chemistry Research Foundation, Shinagawa-ku, Tokyo, Japan.
⁵ Department of Lipid Signaling, National Center for Global Health and Medicine (NCGM), Shinjuku-ku, Tokyo, Japan; Department of Lipid Medical Science, Graduate School of Medicine, The University of Tokyo, Bunkyo-ku, Tokyo, Japan. Electronic address: hshindou@ri.ncgm.go.jp.

Abstract

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 A_1/2s 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.

Keywords: LPLAT; cellular membrane; enzyme nomenclature; glycerophospholipid.

Publication types

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

MeSH terms

1-Acylglycerophosphocholine O-Acyltransferase* / classification
1-Acylglycerophosphocholine O-Acyltransferase* / metabolism
Animals
Glycerophospholipids* / metabolism
Humans
Lysophospholipids* / metabolism
Terminology as Topic

Substances

Glycerophospholipids
Lysophospholipids
1-Acylglycerophosphocholine O-Acyltransferase