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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| Format: | Article (Journal) |
| Language: | English |
| Published: |
September 15, 2010
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| In: |
The journal of biological chemistry
Year: 2010, Volume: 285, Issue: 50, Pages: 39140-39149 |
| ISSN: | 1083-351X |
| DOI: | 10.1074/jbc.M110.160531 |
| Online Access: | Verlag, kostenfrei, Volltext: http://dx.doi.org/10.1074/jbc.M110.160531 Verlag, kostenfrei, Volltext: http://www.jbc.org/content/285/50/39140 
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| Author Notes: | Nana F. Keinath, Sylwia Kierszniowska, Justine Lorek, Gildas Bourdais, Sharon A. Kessler, Hiroko Shimosato-Asano, Ueli Grossniklaus, Waltraud X. Schulze, Silke Robatzek, and Ralph Panstruga |
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| 245 | 1 | 0 | |a PAMP (Pathogen-associated molecular pattern)-induced changes in plasma membrane compartmentalization reveal novel components of plant immunity |c Nana F. Keinath, Sylwia Kierszniowska, Justine Lorek, Gildas Bourdais, Sharon A. Kessler, Hiroko Shimosato-Asano, Ueli Grossniklaus, Waltraud X. Schulze, Silke Robatzek, and Ralph Panstruga |
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| 520 | |a 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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| 650 | 4 | |a Detergent-resistant Membranes | |
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| 650 | 4 | |a Pathogen-associated Molecular Pattern (PAMP) | |
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| 650 | 4 | |a Proteomics | |
| 650 | 4 | |a Quantitative Proteomics | |
| 650 | 4 | |a Reactive Oxygen Species (ROS) | |
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