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Lysophosphatidic acid acyltransferases: a link with intracellular protein trafficking in Arabidopsis root cells?

Abstract Phosphatidic acid (PA) and lysophosphatidic acid acyltransferases (LPAATs) might be critical for the secretory pathway. Four extra-plastidial LPAATs (LPAAT2, 3, 4, and 5) were identified in Arabidopsis thaliana. These AtLPAATs display a specific enzymatic activity converting lysophosphatidi...

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Published in:Journal of experimental botany 2022-03, Vol.73 (5), p.1327-1343
Main Authors: Wattelet-Boyer, Valérie, Le Guédard, Marina, Dittrich-Domergue, Franziska, Maneta-Peyret, Lilly, Kriechbaumer, Verena, Boutté, Yohann, Bessoule, Jean-Jacques, Moreau, Patrick
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container_title Journal of experimental botany
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creator Wattelet-Boyer, Valérie
Le Guédard, Marina
Dittrich-Domergue, Franziska
Maneta-Peyret, Lilly
Kriechbaumer, Verena
Boutté, Yohann
Bessoule, Jean-Jacques
Moreau, Patrick
description Abstract Phosphatidic acid (PA) and lysophosphatidic acid acyltransferases (LPAATs) might be critical for the secretory pathway. Four extra-plastidial LPAATs (LPAAT2, 3, 4, and 5) were identified in Arabidopsis thaliana. These AtLPAATs display a specific enzymatic activity converting lysophosphatidic acid to PA and are located in the endomembrane system. We investigate a putative role for AtLPAATs 3, 4, and 5 in the secretory pathway of root cells through genetical (knockout mutants), biochemical (activity inhibitor, lipid analyses), and imaging (live and immuno-confocal microscopy) approaches. Treating a lpaat4;lpaat5 double mutant with the LPAAT inhibitor CI976 produced a significant decrease in primary root growth. The trafficking of the auxin transporter PIN2 was disturbed in this lpaat4;lpaat5 double mutant treated with CI976, whereas trafficking of H+-ATPases was unaffected. The lpaat4;lpaat5 double mutant is sensitive to salt stress, and the trafficking of the aquaporin PIP2;7 to the plasma membrane in the lpaat4;lpaat5 double mutant treated with CI976 was reduced. We measured the amounts of neo-synthesized PA in roots, and found a decrease in PA only in the lpaat4;lpaat5 double mutant treated with CI976, suggesting that the protein trafficking impairment was due to a critical PA concentration threshold. Phosphatidic acid produced by lysophosphatidic acid acyltransferases has an impact on the efficiency of the intracellular trafficking of some proteins in Arabidopsis thalianaroot cells.
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Four extra-plastidial LPAATs (LPAAT2, 3, 4, and 5) were identified in Arabidopsis thaliana. These AtLPAATs display a specific enzymatic activity converting lysophosphatidic acid to PA and are located in the endomembrane system. We investigate a putative role for AtLPAATs 3, 4, and 5 in the secretory pathway of root cells through genetical (knockout mutants), biochemical (activity inhibitor, lipid analyses), and imaging (live and immuno-confocal microscopy) approaches. Treating a lpaat4;lpaat5 double mutant with the LPAAT inhibitor CI976 produced a significant decrease in primary root growth. The trafficking of the auxin transporter PIN2 was disturbed in this lpaat4;lpaat5 double mutant treated with CI976, whereas trafficking of H+-ATPases was unaffected. The lpaat4;lpaat5 double mutant is sensitive to salt stress, and the trafficking of the aquaporin PIP2;7 to the plasma membrane in the lpaat4;lpaat5 double mutant treated with CI976 was reduced. 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subjects Acyltransferases - genetics
Acyltransferases - metabolism
Arabidopsis - genetics
Arabidopsis - metabolism
Arabidopsis Proteins - genetics
Arabidopsis Proteins - metabolism
Biochemistry
Biochemistry, Molecular Biology
Botanics
Indoleacetic Acids - metabolism
Life Sciences
Protein Transport
Vegetal Biology
title Lysophosphatidic acid acyltransferases: a link with intracellular protein trafficking in Arabidopsis root cells?
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