Reassessing the role of phospholipase D in the Arabidopsis wounding response
Plants respond to wounding by means of a multitude of reactions, with the purpose of stifling herbivore assault. Phospholipase D (PLD) has previously been implicated in the wounding response. Arabidopsis (Arabidopsis thaliana) AtPLDα1 has been proposed to be activated in intact cells, and the phosph...
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creator | BARGMANN, BASTIAAN O.R LAXALT, ANA M RIET, BAS TER TESTERINK, CHRISTA MERQUIOL, EMMANUELLE MOSBLECH, ALINA LEON-REYES, ANTONIO PIETERSE, CORNÉ M.J HARING, MICHEL A HEILMANN, INGO BARTELS, DOROTHEA MUNNIK, TEUN |
description | Plants respond to wounding by means of a multitude of reactions, with the purpose of stifling herbivore assault. Phospholipase D (PLD) has previously been implicated in the wounding response. Arabidopsis (Arabidopsis thaliana) AtPLDα1 has been proposed to be activated in intact cells, and the phosphatidic acid (PA) it produces to serve as a precursor for jasmonic acid (JA) synthesis and to be required for wounding-induced gene expression. Independently, PLD activity has been reported to have a bearing on wounding-induced MAPK activation. However, which PLD isoforms are activated, where this activity takes place (in the wounded or non-wounded cells) and what exactly the consequences are is a question that has not been comprehensively addressed. Here, we show that PLD activity during the wounding response is restricted to the ruptured cells using ³²Pi-labelled phospholipid analyses of Arabidopsis pld knock-out mutants and PLD-silenced tomato cell-suspension cultures. pldα1 knock-out lines have reduced wounding-induced PA production, and the remainder is completely eliminated in a pldα1/δ double knock-out line. Surprisingly, wounding-induced protein kinase activation, AtLOX2 gene expression and JA biosynthesis were not affected in these knock-out lines. Moreover, larvae of the Cabbage White butterfly (Pieris rapae) grew equally well on wild-type and the pld knock-out mutants. |
doi_str_mv | 10.1111/j.1365-3040.2009.01962.x |
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Phospholipase D (PLD) has previously been implicated in the wounding response. Arabidopsis (Arabidopsis thaliana) AtPLDα1 has been proposed to be activated in intact cells, and the phosphatidic acid (PA) it produces to serve as a precursor for jasmonic acid (JA) synthesis and to be required for wounding-induced gene expression. Independently, PLD activity has been reported to have a bearing on wounding-induced MAPK activation. However, which PLD isoforms are activated, where this activity takes place (in the wounded or non-wounded cells) and what exactly the consequences are is a question that has not been comprehensively addressed. Here, we show that PLD activity during the wounding response is restricted to the ruptured cells using ³²Pi-labelled phospholipid analyses of Arabidopsis pld knock-out mutants and PLD-silenced tomato cell-suspension cultures. pldα1 knock-out lines have reduced wounding-induced PA production, and the remainder is completely eliminated in a pldα1/δ double knock-out line. Surprisingly, wounding-induced protein kinase activation, AtLOX2 gene expression and JA biosynthesis were not affected in these knock-out lines. Moreover, larvae of the Cabbage White butterfly (Pieris rapae) grew equally well on wild-type and the pld knock-out mutants.</description><identifier>ISSN: 0140-7791</identifier><identifier>EISSN: 1365-3040</identifier><identifier>DOI: 10.1111/j.1365-3040.2009.01962.x</identifier><identifier>PMID: 19220780</identifier><identifier>CODEN: PLCEDV</identifier><language>eng</language><publisher>Oxford, UK: Oxford, UK : Blackwell Publishing Ltd</publisher><subject>Animals ; Arabidopsis - enzymology ; Arabidopsis - genetics ; Arabidopsis - physiology ; Arabidopsis Proteins - genetics ; Arabidopsis Proteins - metabolism ; Arabidopsis thaliana ; Biological and medical sciences ; Brassica ; Butterflies - physiology ; Cells, Cultured ; Cyclopentanes - metabolism ; Fundamental and applied biological sciences. Psychology ; Gene Expression Regulation, Plant ; Gene Knockout Techniques ; jasmonic acid ; Larva - physiology ; Lycopersicon esculentum ; Lycopersicon esculentum - enzymology ; Lycopersicon esculentum - genetics ; Lycopersicon esculentum - physiology ; Oxylipins - metabolism ; phosphatidic acid ; Phosphatidic Acids - metabolism ; Phospholipase D - genetics ; Phospholipase D - metabolism ; Pieris rapae ; PLD ; Protein Kinases - metabolism</subject><ispartof>Plant, cell and environment, 2009-07, Vol.32 (7), p.837-850</ispartof><rights>2009 Blackwell Publishing Ltd</rights><rights>2009 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4522-88890b52810d45cc6f28436dfbaa7dbe9e4e79e057cda440fc793a241673d4533</citedby><cites>FETCH-LOGICAL-c4522-88890b52810d45cc6f28436dfbaa7dbe9e4e79e057cda440fc793a241673d4533</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1111%2Fj.1365-3040.2009.01962.x$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1111%2Fj.1365-3040.2009.01962.x$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,780,784,1416,1432,27923,27924,45573,45574,46408,46832</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=21538550$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/19220780$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>BARGMANN, BASTIAAN O.R</creatorcontrib><creatorcontrib>LAXALT, ANA M</creatorcontrib><creatorcontrib>RIET, BAS TER</creatorcontrib><creatorcontrib>TESTERINK, CHRISTA</creatorcontrib><creatorcontrib>MERQUIOL, EMMANUELLE</creatorcontrib><creatorcontrib>MOSBLECH, ALINA</creatorcontrib><creatorcontrib>LEON-REYES, ANTONIO</creatorcontrib><creatorcontrib>PIETERSE, CORNÉ M.J</creatorcontrib><creatorcontrib>HARING, MICHEL A</creatorcontrib><creatorcontrib>HEILMANN, INGO</creatorcontrib><creatorcontrib>BARTELS, DOROTHEA</creatorcontrib><creatorcontrib>MUNNIK, TEUN</creatorcontrib><title>Reassessing the role of phospholipase D in the Arabidopsis wounding response</title><title>Plant, cell and environment</title><addtitle>Plant Cell Environ</addtitle><description>Plants respond to wounding by means of a multitude of reactions, with the purpose of stifling herbivore assault. Phospholipase D (PLD) has previously been implicated in the wounding response. Arabidopsis (Arabidopsis thaliana) AtPLDα1 has been proposed to be activated in intact cells, and the phosphatidic acid (PA) it produces to serve as a precursor for jasmonic acid (JA) synthesis and to be required for wounding-induced gene expression. Independently, PLD activity has been reported to have a bearing on wounding-induced MAPK activation. However, which PLD isoforms are activated, where this activity takes place (in the wounded or non-wounded cells) and what exactly the consequences are is a question that has not been comprehensively addressed. Here, we show that PLD activity during the wounding response is restricted to the ruptured cells using ³²Pi-labelled phospholipid analyses of Arabidopsis pld knock-out mutants and PLD-silenced tomato cell-suspension cultures. pldα1 knock-out lines have reduced wounding-induced PA production, and the remainder is completely eliminated in a pldα1/δ double knock-out line. Surprisingly, wounding-induced protein kinase activation, AtLOX2 gene expression and JA biosynthesis were not affected in these knock-out lines. 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Psychology</subject><subject>Gene Expression Regulation, Plant</subject><subject>Gene Knockout Techniques</subject><subject>jasmonic acid</subject><subject>Larva - physiology</subject><subject>Lycopersicon esculentum</subject><subject>Lycopersicon esculentum - enzymology</subject><subject>Lycopersicon esculentum - genetics</subject><subject>Lycopersicon esculentum - physiology</subject><subject>Oxylipins - metabolism</subject><subject>phosphatidic acid</subject><subject>Phosphatidic Acids - metabolism</subject><subject>Phospholipase D - genetics</subject><subject>Phospholipase D - metabolism</subject><subject>Pieris rapae</subject><subject>PLD</subject><subject>Protein Kinases - metabolism</subject><issn>0140-7791</issn><issn>1365-3040</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2009</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkE1v1DAQhi0EotvCX4Bc4JYw_ortA4dqKQVpJRDQs-U4TutVNg6ertr-e5zuqhzBkmXL8zye0UtIRaGhZX3YNpS3suYgoGEApgFqWtbcPyOrp8JzsgIqoFbK0BNyirgFKA_KvCQn1DAGSsOKbH4EhxgQ43Rd3d6EKqcxVGmo5puEZY9xdhiqT1WcHsvn2XWxTzNGrO7SfuoXLwec04ThFXkxuBHD6-N5Rq4-X_xaf6k33y6_rs83tReSsVprbaCTTFPohfS-HZgWvO2HzjnVd8EEEZQJIJXvnRAweGW4Y4K2iheB8zPy_vDvnNPvfcBbu4vowzi6KaQ92lZJAVLQf4IlO8VapgqoD6DPCTGHwc457lx-sBTsErnd2iVZuyS7aMY-Rm7vi_rm2GPf7UL_VzxmXIB3R8Chd-OQ3eQjPnGMSq6lXLiPB-4ujuHhvwew39cXy634bw_-4JJ117n0uPrJgHKgLdesTPIHopakow</recordid><startdate>200907</startdate><enddate>200907</enddate><creator>BARGMANN, BASTIAAN O.R</creator><creator>LAXALT, ANA M</creator><creator>RIET, BAS TER</creator><creator>TESTERINK, CHRISTA</creator><creator>MERQUIOL, EMMANUELLE</creator><creator>MOSBLECH, ALINA</creator><creator>LEON-REYES, ANTONIO</creator><creator>PIETERSE, CORNÉ M.J</creator><creator>HARING, MICHEL A</creator><creator>HEILMANN, INGO</creator><creator>BARTELS, DOROTHEA</creator><creator>MUNNIK, TEUN</creator><general>Oxford, UK : Blackwell Publishing Ltd</general><general>Blackwell Publishing Ltd</general><general>Blackwell</general><scope>FBQ</scope><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7SS</scope><scope>7X8</scope></search><sort><creationdate>200907</creationdate><title>Reassessing the role of phospholipase D in the Arabidopsis wounding response</title><author>BARGMANN, BASTIAAN O.R ; LAXALT, ANA M ; RIET, BAS TER ; TESTERINK, CHRISTA ; MERQUIOL, EMMANUELLE ; MOSBLECH, ALINA ; LEON-REYES, ANTONIO ; PIETERSE, CORNÉ M.J ; HARING, MICHEL A ; HEILMANN, INGO ; BARTELS, DOROTHEA ; MUNNIK, TEUN</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4522-88890b52810d45cc6f28436dfbaa7dbe9e4e79e057cda440fc793a241673d4533</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2009</creationdate><topic>Animals</topic><topic>Arabidopsis - enzymology</topic><topic>Arabidopsis - genetics</topic><topic>Arabidopsis - physiology</topic><topic>Arabidopsis Proteins - genetics</topic><topic>Arabidopsis Proteins - metabolism</topic><topic>Arabidopsis thaliana</topic><topic>Biological and medical sciences</topic><topic>Brassica</topic><topic>Butterflies - physiology</topic><topic>Cells, Cultured</topic><topic>Cyclopentanes - metabolism</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gene Expression Regulation, Plant</topic><topic>Gene Knockout Techniques</topic><topic>jasmonic acid</topic><topic>Larva - physiology</topic><topic>Lycopersicon esculentum</topic><topic>Lycopersicon esculentum - enzymology</topic><topic>Lycopersicon esculentum - genetics</topic><topic>Lycopersicon esculentum - physiology</topic><topic>Oxylipins - metabolism</topic><topic>phosphatidic acid</topic><topic>Phosphatidic Acids - metabolism</topic><topic>Phospholipase D - genetics</topic><topic>Phospholipase D - metabolism</topic><topic>Pieris rapae</topic><topic>PLD</topic><topic>Protein Kinases - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>BARGMANN, BASTIAAN O.R</creatorcontrib><creatorcontrib>LAXALT, ANA M</creatorcontrib><creatorcontrib>RIET, BAS TER</creatorcontrib><creatorcontrib>TESTERINK, CHRISTA</creatorcontrib><creatorcontrib>MERQUIOL, EMMANUELLE</creatorcontrib><creatorcontrib>MOSBLECH, ALINA</creatorcontrib><creatorcontrib>LEON-REYES, ANTONIO</creatorcontrib><creatorcontrib>PIETERSE, CORNÉ M.J</creatorcontrib><creatorcontrib>HARING, MICHEL A</creatorcontrib><creatorcontrib>HEILMANN, INGO</creatorcontrib><creatorcontrib>BARTELS, DOROTHEA</creatorcontrib><creatorcontrib>MUNNIK, TEUN</creatorcontrib><collection>AGRIS</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Entomology Abstracts (Full archive)</collection><collection>MEDLINE - Academic</collection><jtitle>Plant, cell and environment</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>BARGMANN, BASTIAAN O.R</au><au>LAXALT, ANA M</au><au>RIET, BAS TER</au><au>TESTERINK, CHRISTA</au><au>MERQUIOL, EMMANUELLE</au><au>MOSBLECH, ALINA</au><au>LEON-REYES, ANTONIO</au><au>PIETERSE, CORNÉ M.J</au><au>HARING, MICHEL A</au><au>HEILMANN, INGO</au><au>BARTELS, DOROTHEA</au><au>MUNNIK, TEUN</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Reassessing the role of phospholipase D in the Arabidopsis wounding response</atitle><jtitle>Plant, cell and environment</jtitle><addtitle>Plant Cell Environ</addtitle><date>2009-07</date><risdate>2009</risdate><volume>32</volume><issue>7</issue><spage>837</spage><epage>850</epage><pages>837-850</pages><issn>0140-7791</issn><eissn>1365-3040</eissn><coden>PLCEDV</coden><abstract>Plants respond to wounding by means of a multitude of reactions, with the purpose of stifling herbivore assault. Phospholipase D (PLD) has previously been implicated in the wounding response. Arabidopsis (Arabidopsis thaliana) AtPLDα1 has been proposed to be activated in intact cells, and the phosphatidic acid (PA) it produces to serve as a precursor for jasmonic acid (JA) synthesis and to be required for wounding-induced gene expression. Independently, PLD activity has been reported to have a bearing on wounding-induced MAPK activation. However, which PLD isoforms are activated, where this activity takes place (in the wounded or non-wounded cells) and what exactly the consequences are is a question that has not been comprehensively addressed. Here, we show that PLD activity during the wounding response is restricted to the ruptured cells using ³²Pi-labelled phospholipid analyses of Arabidopsis pld knock-out mutants and PLD-silenced tomato cell-suspension cultures. pldα1 knock-out lines have reduced wounding-induced PA production, and the remainder is completely eliminated in a pldα1/δ double knock-out line. Surprisingly, wounding-induced protein kinase activation, AtLOX2 gene expression and JA biosynthesis were not affected in these knock-out lines. Moreover, larvae of the Cabbage White butterfly (Pieris rapae) grew equally well on wild-type and the pld knock-out mutants.</abstract><cop>Oxford, UK</cop><pub>Oxford, UK : Blackwell Publishing Ltd</pub><pmid>19220780</pmid><doi>10.1111/j.1365-3040.2009.01962.x</doi><tpages>14</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Animals Arabidopsis - enzymology Arabidopsis - genetics Arabidopsis - physiology Arabidopsis Proteins - genetics Arabidopsis Proteins - metabolism Arabidopsis thaliana Biological and medical sciences Brassica Butterflies - physiology Cells, Cultured Cyclopentanes - metabolism Fundamental and applied biological sciences. Psychology Gene Expression Regulation, Plant Gene Knockout Techniques jasmonic acid Larva - physiology Lycopersicon esculentum Lycopersicon esculentum - enzymology Lycopersicon esculentum - genetics Lycopersicon esculentum - physiology Oxylipins - metabolism phosphatidic acid Phosphatidic Acids - metabolism Phospholipase D - genetics Phospholipase D - metabolism Pieris rapae PLD Protein Kinases - metabolism |
title | Reassessing the role of phospholipase D in the Arabidopsis wounding response |
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