PAMP (Pathogen-associated Molecular Pattern)-induced Changes in Plasma Membrane Compartmentalization Reveal Novel Components of Plant Immunity

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 quantit...

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Published in:The Journal of biological chemistry 2010-12, Vol.285 (50), p.39140-39149
Main Authors: Keinath, Nana F., Kierszniowska, Sylwia, Lorek, Justine, Bourdais, Gildas, Kessler, Sharon A., Shimosato-Asano, Hiroko, Grossniklaus, Ueli, Schulze, Waltraud X., Robatzek, Silke, Panstruga, Ralph
Format: Article
Language:English
Subjects:
14N/15N-Metabolic Labeling
Arabidopsis - immunology
Arabidopsis - microbiology
Arabidopsis Proteins
Arabidopsis thaliana
Cell Membrane - metabolism
Detergent-resistant Membranes
Detergents - pharmacology
Flagellin - chemistry
flg22/FlS2
Immune System
Immunity, Innate
MAP Kinase Signaling System
Mass Spectrometry - methods
Membrane Microdomains - chemistry
Membrane Rafts
Pathogen-associated Molecular Pattern (PAMP)
Phosphotransferases
Plant
Plant Biology
Plant Leaves - microbiology
Plasma Membrane
Proteomics
Proteomics - methods
Quantitative Proteomics
Reactive Oxygen Species
Reactive Oxygen Species (ROS)
Respiratory Burst
Vacuolar Proton-Translocating ATPases
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Summary: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.
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.M110.160531