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
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/105128
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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 |
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CONICET Digital (CONICET) |
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CONICET Digital (CONICET) |
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Consejo Nacional de Investigaciones Científicas y Técnicas |
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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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1842270150946979840 |
score |
13.13397 |