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PAMP (pathogen-associated molecular pattern)-induced changes in plasma membrane compartmentalization reveal novel components of plant immunity.

Type of publication Peer-reviewed
Publikationsform Original article (peer-reviewed)
Author Keinath Nana F, Kierszniowska Sylwia, Lorek Justine, Bourdais Gildas, Kessler Sharon A, Shimosato-Asano Hiroko, Grossniklaus Ueli, Schulze Waltraud X, Robatzek Silke, Panstruga Ralph,
Project The genetic and molecular basis of gametogenesis and maternal effects in arabidopsis
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Original article (peer-reviewed)

Journal The Journal of biological chemistry
Volume (Issue) 285(50)
Page(s) 39140 - 9
Title of proceedings The Journal of biological chemistry
DOI 10.1074/jbc.m110.160531

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.
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