Reassessing the role of phospholipase D in the Arabidopsis wounding response

Autores
Bargmann, Bastiaan O. R.; Laxalt, Ana Maria; 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
Año de publicación
2009
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
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) AtPLDa1 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. plda1 knock-out lines have reduced wounding-induced PA production, and the remainder is completely eliminated in a plda1/d 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.
Fil: Bargmann, Bastiaan O. R.. University of Amsterdam; Países Bajos
Fil: Laxalt, Ana Maria. University of Amsterdam; Países Bajos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigaciones Biológicas y Tecnológicas. Universidad Nacional de Córdoba. Facultad de Ciencias Exactas, Físicas y Naturales. Instituto de Investigaciones Biológicas y Tecnológicas; Argentina
Fil: Riet, Bas Ter. University of Amsterdam; Países Bajos
Fil: Testerink, Christa. University of Amsterdam; Países Bajos
Fil: Merquiol, Emmanuelle. Vrije Universiteit Amsterdam; Países Bajos
Fil: Mosblech, Alina. Georg August University; Alemania
Fil: Leon Reyes, Antonio. Utrecht University; Países Bajos
Fil: Pieterse, Corné M. J.. Utrecht University; Países Bajos
Fil: Haring, Michel A.. University of Amsterdam; Países Bajos
Fil: Heilmann, Ingo. Georg August University; Alemania
Fil: Bartels, Dorothea. Vrije Universiteit Amsterdam; Países Bajos
Fil: Munnik, Teun. Universitat Bonn; Alemania
Materia
phospholipase D
wounding
signalling
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/105128

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oai_identifier_str oai:ri.conicet.gov.ar:11336/105128
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repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Reassessing the role of phospholipase D in the Arabidopsis wounding responseBargmann, Bastiaan O. R.Laxalt, Ana MariaRiet, Bas TerTesterink, ChristaMerquiol, EmmanuelleMosblech, AlinaLeon Reyes, AntonioPieterse, Corné M. J.Haring, Michel A.Heilmann, IngoBartels, DorotheaMunnik, Teunphospholipase Dwoundingsignallinghttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Plants 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) AtPLDa1 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. plda1 knock-out lines have reduced wounding-induced PA production, and the remainder is completely eliminated in a plda1/d 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.Fil: Bargmann, Bastiaan O. R.. University of Amsterdam; Países BajosFil: Laxalt, Ana Maria. University of Amsterdam; Países Bajos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigaciones Biológicas y Tecnológicas. Universidad Nacional de Córdoba. Facultad de Ciencias Exactas, Físicas y Naturales. Instituto de Investigaciones Biológicas y Tecnológicas; ArgentinaFil: Riet, Bas Ter. University of Amsterdam; Países BajosFil: Testerink, Christa. University of Amsterdam; Países BajosFil: Merquiol, Emmanuelle. Vrije Universiteit Amsterdam; Países BajosFil: Mosblech, Alina. Georg August University; AlemaniaFil: Leon Reyes, Antonio. Utrecht University; Países BajosFil: Pieterse, Corné M. J.. Utrecht University; Países BajosFil: Haring, Michel A.. University of Amsterdam; Países BajosFil: Heilmann, Ingo. Georg August University; AlemaniaFil: Bartels, Dorothea. Vrije Universiteit Amsterdam; Países BajosFil: Munnik, Teun. Universitat Bonn; AlemaniaWiley Blackwell Publishing, Inc2009-07info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/105128Bargmann, Bastiaan O. R.; Laxalt, Ana Maria; Riet, Bas Ter; Testerink, Christa; Merquiol, Emmanuelle; et al.; Reassessing the role of phospholipase D in the Arabidopsis wounding response; Wiley Blackwell Publishing, Inc; Plant, Cell and Environment; 32; 7; 7-2009; 837-8500140-7791CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1111/j.1365-3040.2009.01962.xinfo:eu-repo/semantics/altIdentifier/url/https://onlinelibrary.wiley.com/doi/full/10.1111/j.1365-3040.2009.01962.xinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T10:11:13Zoai:ri.conicet.gov.ar:11336/105128instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-03 10:11:13.981CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Reassessing the role of phospholipase D in the Arabidopsis wounding response
title Reassessing the role of phospholipase D in the Arabidopsis wounding response
spellingShingle Reassessing the role of phospholipase D in the Arabidopsis wounding response
Bargmann, Bastiaan O. R.
phospholipase D
wounding
signalling
title_short Reassessing the role of phospholipase D in the Arabidopsis wounding response
title_full Reassessing the role of phospholipase D in the Arabidopsis wounding response
title_fullStr Reassessing the role of phospholipase D in the Arabidopsis wounding response
title_full_unstemmed Reassessing the role of phospholipase D in the Arabidopsis wounding response
title_sort Reassessing the role of phospholipase D in the Arabidopsis wounding response
dc.creator.none.fl_str_mv Bargmann, Bastiaan O. R.
Laxalt, Ana Maria
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 Bargmann, Bastiaan O. R.
author_facet Bargmann, Bastiaan O. R.
Laxalt, Ana Maria
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_role author
author2 Laxalt, Ana Maria
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
author2_role author
author
author
author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv phospholipase D
wounding
signalling
topic phospholipase D
wounding
signalling
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv 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) AtPLDa1 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. plda1 knock-out lines have reduced wounding-induced PA production, and the remainder is completely eliminated in a plda1/d 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.
Fil: Bargmann, Bastiaan O. R.. University of Amsterdam; Países Bajos
Fil: Laxalt, Ana Maria. University of Amsterdam; Países Bajos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigaciones Biológicas y Tecnológicas. Universidad Nacional de Córdoba. Facultad de Ciencias Exactas, Físicas y Naturales. Instituto de Investigaciones Biológicas y Tecnológicas; Argentina
Fil: Riet, Bas Ter. University of Amsterdam; Países Bajos
Fil: Testerink, Christa. University of Amsterdam; Países Bajos
Fil: Merquiol, Emmanuelle. Vrije Universiteit Amsterdam; Países Bajos
Fil: Mosblech, Alina. Georg August University; Alemania
Fil: Leon Reyes, Antonio. Utrecht University; Países Bajos
Fil: Pieterse, Corné M. J.. Utrecht University; Países Bajos
Fil: Haring, Michel A.. University of Amsterdam; Países Bajos
Fil: Heilmann, Ingo. Georg August University; Alemania
Fil: Bartels, Dorothea. Vrije Universiteit Amsterdam; Países Bajos
Fil: Munnik, Teun. Universitat Bonn; Alemania
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) AtPLDa1 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. plda1 knock-out lines have reduced wounding-induced PA production, and the remainder is completely eliminated in a plda1/d 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.
publishDate 2009
dc.date.none.fl_str_mv 2009-07
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/105128
Bargmann, Bastiaan O. R.; Laxalt, Ana Maria; Riet, Bas Ter; Testerink, Christa; Merquiol, Emmanuelle; et al.; Reassessing the role of phospholipase D in the Arabidopsis wounding response; Wiley Blackwell Publishing, Inc; Plant, Cell and Environment; 32; 7; 7-2009; 837-850
0140-7791
CONICET Digital
CONICET
url http://hdl.handle.net/11336/105128
identifier_str_mv Bargmann, Bastiaan O. R.; Laxalt, Ana Maria; Riet, Bas Ter; Testerink, Christa; Merquiol, Emmanuelle; et al.; Reassessing the role of phospholipase D in the Arabidopsis wounding response; Wiley Blackwell Publishing, Inc; Plant, Cell and Environment; 32; 7; 7-2009; 837-850
0140-7791
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1111/j.1365-3040.2009.01962.x
info:eu-repo/semantics/altIdentifier/url/https://onlinelibrary.wiley.com/doi/full/10.1111/j.1365-3040.2009.01962.x
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Wiley Blackwell Publishing, Inc
publisher.none.fl_str_mv Wiley Blackwell Publishing, Inc
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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