6533b85cfe1ef96bd12bc8b2

RESEARCH PRODUCT

Integrated signaling network involving calcium, nitric oxide, active oxygen species but not mitogen-activated protein kinases in BcPG1-elicited grapevine defenses.

Marc BentéjacDavid WendehenneAlain PuginBenoît PoinssotElodie Vandelle

subject

0106 biological sciencesMAPK/ERK pathwayTime FactorsPhysiology[SDV]Life Sciences [q-bio]Phenylalanine ammonia-lyase01 natural sciencesNitric oxideFungal Proteins03 medical and health scienceschemistry.chemical_compounddepolarizationGene Expression Regulation Plantplant defensenitric oxideVitisdépolarisationProtein kinase ACells Cultured030304 developmental biology0303 health scienceselicitorbiologyelicitor; grapevine; plant defense; nitric oxideKinaseGeneral MedicinePlants Genetically ModifiedElicitorgrapevinechemistryBiochemistryMitogen-activated protein kinasebiology.proteinCalciumBotrytisMitogen-Activated Protein KinasesSignal transductionbotrytis cinereavigneReactive Oxygen SpeciesAgronomy and Crop ScienceSignal Transduction010606 plant biology & botany

description

We have already reported the identification of the endopolygalacturonase 1 (BcPG1) from Botrytis cinerea as a potent elicitor of defense responses in grapevine, independently of its enzymatic activity. The aim of the present study is the analysis of the signaling pathways triggered by BcPG1 in grapevine cells. Our data indicate that BcPG1 induces a Ca2+ entry from the apoplasm, which triggers a phosphorylation-dependent nitric oxide (NO) production via an enzyme probably related to a NO synthase. Then NO is involved in i) cytosolic calcium homeostasis, by activating Ca2+ release from internal stores and regulating Ca2+ fluxes across the plasma membrane, ii) plasma membrane potential variation, iii) the activation of active oxygen species (AOS) production, and iv) defense gene expression, including phenylalanine ammonia lyase and stilbene synthase, which encode enzymes responsible for phytoalexin biosynthesis. Interestingly enough, mitogen-activated protein kinase (MAPK) activation is independent of this regulation pathway that closely connects Ca2+, NO, and AOS.

http://hdl.handle.net/11562/327547