scholarly journals Lysophospholipid acyltransferases and leukotriene biosynthesis: intersection of the Lands cycle and the arachidonate PI cycle

2019 ◽  
Vol 60 (2) ◽  
pp. 219-226 ◽  
Author(s):  
Robert C. Murphy ◽  
Giancarlo Folco
Keyword(s):  
Lysophospholipid Acyltransferases

Characterization and expression analysis of GPAT gene family in maize

2019 ◽  
Vol 99 (5) ◽  
pp. 577-588
Author(s):  
Xiaoxuan Xu ◽  
Bowei Yan ◽  
Ying Zhao ◽  
Feng Wang ◽  
Xunchao Zhao ◽  
...  
Keyword(s):  
Gene Family ◽  
Stress Responses ◽  
Developmental Stages ◽  
Expression Profiles ◽  
Cold Treatment ◽  
Oil Production ◽  
Initial Step ◽  
Field Crops ◽  
Lysophospholipid Acyltransferases ◽  
Elevated Expression

Glycerol-3-phosphate acyltransferase (GPAT) catalyzes the initial step of glycerolipids biosynthesis and contributes to oil production, membrane stabilization, and stress responses in plants. In major field crops, little information on the GPAT gene family and their potential stress-related functions were available. In this study, 15 GPAT gene family members were identified from the maize genome and designated as ZmGPAT1–ZmGPAT14 and ZMS1. The ZmGPAT proteins contained 371–557 amino acids and had a molecular weight between 42.7 and 61.2 kDa. Phylogenetic analysis revealed that ZmGPATs fell into four clusters. All 15 ZmGPAT proteins possessed conserved PlsC/LPLAT (phosphate acyltransferases/lysophospholipid acyltransferases) domains and featured multiple acyltransferase motifs. The expression profiles of ZmGPAT genes were different in various tissues of maize and the elevated expression of several ZmGPAT genes occurred at early seed developmental stages. In response to environmental stresses, differential expression of ZmGPATs had been observed, highlighted by the significant induction of transcripts accumulation of some ZmGPATs under cold treatment. This study will help to better understand the potential roles of GPAT in oil production and development and abiotic stress responses in field crops.

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

2021 ◽  
pp. 101470
Author(s):  
William J. Valentine ◽  
Keisuke Yanagida ◽  
Hiroki Kawana ◽  
Nozomu Kono ◽  
Nobuo N. Noda ◽  
...  
Keyword(s):  
Membrane Phospholipid ◽  
Lysophospholipid Acyltransferases

scholarly journals An accurate and versatile method for determining the acyl group-introducing position of lysophospholipid acyltransferases

2019 ◽  
Vol 1864 (7) ◽  
pp. 1053-1060
Author(s):  
Hiroki Kawana ◽  
Kuniyuki Kano ◽  
Hideo Shindou ◽  
Asuka Inoue ◽  
Takao Shimizu ◽  
...  
Keyword(s):  
Lysophospholipid Acyltransferases

scholarly journals Control of free arachidonic acid levels by phospholipases A2 and lysophospholipid acyltransferases

2009 ◽  
Vol 1791 (12) ◽  
pp. 1103-1113 ◽  
Author(s):  
Gema Pérez-Chacón ◽  
Alma M. Astudillo ◽  
David Balgoma ◽  
María A. Balboa ◽  
Jesús Balsinde
Keyword(s):  
Arachidonic Acid ◽  
Phospholipases A2 ◽  
Lysophospholipid Acyltransferases ◽  
Free Arachidonic Acid

scholarly journals Drosophila Lysophospholipid Acyltransferases Are Specifically Required for Germ Cell Development

2009 ◽  
Vol 20 (24) ◽  
pp. 5224-5235 ◽  
Author(s):  
Josefa Steinhauer ◽  
Miguel A. Gijón ◽  
Wayne R. Riekhof ◽  
Dennis R. Voelker ◽  
Robert C. Murphy ◽  
...  
Keyword(s):  
Germ Cell ◽  
Unsaturated Fatty Acids ◽  
Fatty Acid Content ◽  
Cell Development ◽  
Adult Males ◽  
Triple Mutant ◽  
Germline Development ◽  
Diverse Range ◽  
Germ Cell Development ◽  
Lysophospholipid Acyltransferases

Enzymes of the membrane-bound O-acyltransferase (MBOAT) family add fatty acyl chains to a diverse range of protein and lipid substrates. A chromosomal translocation disrupting human MBOAT1 results in a novel syndrome characterized by male sterility and brachydactyly. We have found that the Drosophila homologues of MBOAT1, Oysgedart (Oys), Nessy (Nes), and Farjavit (Frj), are lysophospholipid acyltransferases. When expressed in yeast, these MBOATs esterify specific lysophospholipids preferentially with unsaturated fatty acids. Generating null mutations for each gene allowed us to identify redundant functions for Oys and Nes in two distinct aspects of Drosophila germ cell development. Embryos lacking both oys and nes show defects in the ability of germ cells to migrate into the mesoderm, a process guided by lipid signals. In addition, oys nes double mutant adult males are sterile due to specific defects in spermatid individualization. oys nes mutant testes, as well as single, double, and triple mutant whole adult animals, show an increase in the saturated fatty acid content of several phospholipid species. Our findings suggest that lysophospholipid acyltransferase activity is essential for germline development and could provide a mechanistic explanation for the etiology of the human MBOAT1 mutation.

scholarly journals Regulation of the yeast triacylglycerol lipases Tgl4p and Tgl5p by the presence/absence of nonpolar lipids

2016 ◽  
Vol 27 (13) ◽  
pp. 2014-2024 ◽  
Author(s):  
Isabella Klein ◽  
Lisa Klug ◽  
Claudia Schmidt ◽  
Martina Zandl ◽  
Martina Korber ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Lipid Droplets ◽  
Lipolytic Activity ◽  
Wild Type ◽  
Yeast Saccharomyces Cerevisiae ◽  
Steryl Esters ◽  
Lysophospholipid Acyltransferases ◽  
Nonpolar Lipids ◽  
The Stability ◽  
In Cells

Tgl3p, Tgl4p, and Tgl5p are the major triacylglycerol lipases of the yeast Saccharomyces cerevisiae. Recently we demonstrated that properties of Tgl3p are regulated by the formation of nonpolar lipids. The present study extends these investigations to the two other yeast triacylglycerol lipases, Tgl4p and Tgl5p. We show that Tgl4p and Tgl5p, which are localized to lipid droplets in wild type, are partially retained in the endoplasmic reticulum in cells lacking triacylglycerols and localize exclusively to the endoplasmic reticulum in a mutant devoid of lipid droplets. In cells lacking steryl esters, the subcellular distribution of Tgl4p and Tgl5p is unaffected, but Tgl5p becomes unstable, whereas the stability of Tgl4p increases. In cells lacking nonpolar lipids, Tgl4p and Tgl5p lose their lipolytic activity but retain their side activity as lysophospholipid acyltransferases. To investigate the regulatory network of yeast triacylglycerol lipases in more detail, we also examined properties of Tgl3p, Tgl4p, and Tgl5p, respectively, in the absence of the other lipases. Surprisingly, lack of two lipases did not affect expression, localization, and stability of the remaining Tgl protein. These results suggest that Tgl3p, Tgl4p, and Tgl5p, although they exhibit similar functions, act as independent entities.

Lysophospholipid Acyltransferases

2015 ◽  
pp. 3-21
Author(s):  
Hideo Shindou ◽  
Takeshi Harayama ◽  
Daisuke Hishikawa
Keyword(s):  
Lysophospholipid Acyltransferases
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