Please use this identifier to cite or link to this item: http://hdl.handle.net/2440/117088
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Type: Journal article
Title: Attenuation of pattern recognition receptor signaling is mediated by a MAP kinase kinase kinase
Author: Mithoe, S.C.
Ludwig, C.
Pel, M.J.
Cucinotta, M.
Casartelli, A.
Mbengue, M.
Sklenar, J.
Derbyshire, P.
Robatzek, S.
Pieterse, C.M.
Aebersold, R.
Menke, F.L.
Citation: EMBO reports, 2016; 17(3):441-454
Publisher: John Wiley & Sons
Issue Date: 2016
ISSN: 1469-221X
1469-3178
Statement of
Responsibility: 
Sharon C Mithoe, Christina Ludwig, Michiel JC Pel, Mara Cucinotta, Alberto Casartelli, Malick Mbengue, Jan Sklenar, Paul Derbyshire, Silke Robatzek, Corné MJ Pieterse, Ruedi Aebersold, Frank LH Menke
Abstract: Pattern recognition receptors (PRRs) play a key role in plant and animal innate immunity. PRR binding of their cognate ligand triggers a signaling network and activates an immune response. Activation of PRR signaling must be controlled prior to ligand binding to prevent spurious signaling and immune activation. Flagellin perception in Arabidopsis through FLAGELLIN‐SENSITIVE 2 (FLS2) induces the activation of mitogen‐activated protein kinases (MAPKs) and immunity. However, the precise molecular mechanism that connects activated FLS2 to downstream MAPK cascades remains unknown. Here, we report the identification of a differentially phosphorylated MAP kinase kinase kinase that also interacts with FLS2. Using targeted proteomics and functional analysis, we show that MKKK7 negatively regulates flagellin‐triggered signaling and basal immunity and this requires phosphorylation of MKKK7 on specific serine residues. MKKK7 attenuates MPK6 activity and defense gene expression. Moreover, MKKK7 suppresses the reactive oxygen species burst downstream of FLS2, suggesting that MKKK7‐mediated attenuation of FLS2 signaling occurs through direct modulation of the FLS2 complex.
Keywords: Immunology; microbiology; virology & hostpathogen interaction; plant biology
Rights: © 2016 John Wiley & Sons
RMID: 0030081349
DOI: 10.15252/embr.201540806
Appears in Collections:Biochemistry publications

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