title: PAMP (pathogen-associated molecular pattern)-induced changes in plasma membrane compartmentalization reveal novel components of plant immunity.
abstract: Plasma membrane compartmentalization spatiotemporally regulates cell-autonomous immune signaling in animal cells. To elucidate immediate early protein dynamics at the plant plasma membrane in response to the bacterial pathogen-associated molecular pattern (PAMP) flagellin (flg22) we employed quantitative mass spectrometric analysis on detergent-resistant membranes (DRMs) of Arabidopsis thaliana suspension cells. This approach revealed rapid and profound changes in DRM protein composition following PAMP treatment, prominently affecting proton ATPases and receptor-like kinases, including the flagellin receptor FLS2. We employed reverse genetics to address a potential contribution of a subset of these proteins in flg22-triggered cellular responses. Mutants of three candidates (DET3, AHA1, FER) exhibited a conspicuous defect in the PAMP-triggered accumulation of reactive oxygen species. In addition, these mutants showed altered mitogen-activated protein kinase (MAPK) activation, a defect in PAMP-triggered stomatal closure as well as altered bacterial infection phenotypes, which revealed three novel players in elicitor-dependent oxidative burst control and innate immunity. Our data provide evidence for dynamic elicitor-induced changes in the membrane compartmentalization of PAMP signaling components.
authors.affiliation: Department of Plant Microbe Interactions, Max Planck Institute for Plant Breeding Research, Carl-von-Linné-Weg 10, 50829 Cologne, Germany.
authors.forename: Nana F
authors.initials: NF
authors.lastname: Keinath
authors.forename: Sylwia
authors.initials: S
authors.lastname: Kierszniowska
authors.forename: Justine
authors.initials: J
authors.lastname: Lorek
authors.forename: Gildas
authors.initials: G
authors.lastname: Bourdais
authors.forename: Sharon A
authors.initials: SA
authors.lastname: Kessler
authors.forename: Hiroko
authors.initials: H
authors.lastname: Shimosato-Asano
authors.forename: Ueli
authors.initials: U
authors.lastname: Grossniklaus
authors.forename: Waltraud X
authors.initials: WX
authors.lastname: Schulze
authors.forename: Silke
authors.initials: S
authors.lastname: Robatzek
authors.forename: Ralph
authors.initials: R
authors.lastname: Panstruga
mesh_terms: D017360:Arabidopsis / Q000276:immunology* / Q000382:microbiology*; D029681:Arabidopsis Proteins; D002462:Cell Membrane / Q000378:metabolism*; D003902:Detergents / Q000494:pharmacology; D005408:Flagellin / Q000737:chemistry; D007107:Immune System; D007113:Immunity, Innate; D020935:MAP Kinase Signaling System; D013058:Mass Spectrometry / Q000379:methods; D021962:Membrane Microdomains / Q000737:chemistry; D010770:Phosphotransferases; D018515:Plant Leaves / Q000382:microbiology; D040901:Proteomics / Q000379:methods; D017382:Reactive Oxygen Species; D016897:Respiratory Burst; D025262:Vacuolar Proton-Translocating ATPases; D017346:Protein Serine-Threonine Kinases
chemical_list: D029681:Arabidopsis Proteins; D003902:Detergents; D005408:Flagellin; D010770:Phosphotransferases; D017382:Reactive Oxygen Species; D025262:Vacuolar Proton-Translocating ATPases; C522131:At3g51550 protein, Arabidopsis; D017346:Protein Serine-Threonine Kinases; C505814:Det3 protein, Arabidopsis