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

© The Author(s) 2021. Published by Oxford University Press on behalf of the Society for Experimental Biology. All rights reserved. For permissions, please email: journals.permissionsoup.com.

Bibliographische Detailangaben
Veröffentlicht in:Journal of experimental botany. - 1985. - 73(2022), 5 vom: 02. März, Seite 1327-1343
1. Verfasser: Wattelet-Boyer, Valérie (VerfasserIn)
Weitere Verfasser: Le Guédard, Marina, Dittrich-Domergue, Franziska, Maneta-Peyret, Lilly, Kriechbaumer, Verena, Boutté, Yohann, Bessoule, Jean-Jacques, Moreau, Patrick
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2022
Zugriff auf das übergeordnete Werk:Journal of experimental botany
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Arabidopsis PIN2 PIP2;7 lysophosphatidic acid lysophosphatidic acid acyltransferase phosphatidic acid roots secretory pathway mehr... Arabidopsis Proteins Indoleacetic Acids Acyltransferases EC 2.3.- 2-acylglycerophosphate acyltransferase EC 2.3.1.52
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520 |a 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 
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650 4 |a PIN2 
650 4 |a PIP2;7 
650 4 |a lysophosphatidic acid 
650 4 |a lysophosphatidic acid acyltransferase 
650 4 |a phosphatidic acid 
650 4 |a roots 
650 4 |a secretory pathway 
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650 7 |a Indoleacetic Acids  |2 NLM 
650 7 |a Acyltransferases  |2 NLM 
650 7 |a EC 2.3.-  |2 NLM 
650 7 |a 2-acylglycerophosphate acyltransferase  |2 NLM 
650 7 |a EC 2.3.1.52  |2 NLM 
700 1 |a Le Guédard, Marina  |e verfasserin  |4 aut 
700 1 |a Dittrich-Domergue, Franziska  |e verfasserin  |4 aut 
700 1 |a Maneta-Peyret, Lilly  |e verfasserin  |4 aut 
700 1 |a Kriechbaumer, Verena  |e verfasserin  |4 aut 
700 1 |a Boutté, Yohann  |e verfasserin  |4 aut 
700 1 |a Bessoule, Jean-Jacques  |e verfasserin  |4 aut 
700 1 |a Moreau, Patrick  |e verfasserin  |4 aut 
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