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

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 selectiv...

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Published inThe 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
LanguageEnglish
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
Online AccessGet full text

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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 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.
AbstractList 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.
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 s 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.
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 1/2 s 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.
ArticleNumber 101470
Author Shindou, Hideo
Yanagida, Keisuke
Valentine, William J.
Kono, Nozomu
Noda, Nobuo N.
Kawana, Hiroki
Aoki, Junken
Author_xml – sequence: 1
  givenname: William J.
  surname: Valentine
  fullname: Valentine, William J.
  organization: Department of Lipid Signaling, National Center for Global Health and Medicine (NCGM), Shinjuku-ku, Tokyo, Japan
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  givenname: Keisuke
  surname: Yanagida
  fullname: Yanagida, Keisuke
  organization: Department of Lipid Signaling, National Center for Global Health and Medicine (NCGM), Shinjuku-ku, Tokyo, Japan
– sequence: 3
  givenname: Hiroki
  surname: Kawana
  fullname: Kawana, Hiroki
  organization: Department of Health Chemistry, Graduate School of Pharmaceutical Sciences, The University of Tokyo, Bunkyo-ku, Tokyo, Japan
– sequence: 4
  givenname: Nozomu
  surname: Kono
  fullname: Kono, Nozomu
  organization: Department of Health Chemistry, Graduate School of Pharmaceutical Sciences, The University of Tokyo, Bunkyo-ku, Tokyo, Japan
– sequence: 5
  givenname: Nobuo N.
  surname: Noda
  fullname: Noda, Nobuo N.
  organization: Institute of Microbial Chemistry (BIKAKEN), Microbial Chemistry Research Foundation, Shinagawa-ku, Tokyo, Japan
– sequence: 6
  givenname: Junken
  surname: Aoki
  fullname: Aoki, Junken
  organization: Department of Health Chemistry, Graduate School of Pharmaceutical Sciences, The University of Tokyo, Bunkyo-ku, Tokyo, Japan
– sequence: 7
  givenname: Hideo
  surname: Shindou
  fullname: Shindou, Hideo
  email: hshindou@ri.ncgm.go.jp
  organization: Department of Lipid Signaling, National Center for Global Health and Medicine (NCGM), Shinjuku-ku, Tokyo, Japan
BackLink https://www.ncbi.nlm.nih.gov/pubmed/34890643$$D View this record in MEDLINE/PubMed
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Issue 1
Keywords 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
Language English
License This is an open access article under the CC BY license.
Copyright © 2021 The Authors. Published by Elsevier Inc. All rights reserved.
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Snippet The diversity of glycerophospholipid species in cellular membranes is immense and affects various biological functions. Glycerol-3-phosphate acyltransferases...
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SubjectTerms 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
Title Update and nomenclature proposal for mammalian lysophospholipid acyltransferases, which create membrane phospholipid diversity
URI https://dx.doi.org/10.1016/j.jbc.2021.101470
https://www.ncbi.nlm.nih.gov/pubmed/34890643
https://search.proquest.com/docview/2618907911
https://pubmed.ncbi.nlm.nih.gov/PMC8753187
Volume 298
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