Bifurcation of Arabidopsis NLR Immune Signaling via Ca2+-Dependent Protein Kinases

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Bifurcation of Arabidopsis NLR Immune Signaling via Ca2+-Dependent Protein Kinases

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Title: Bifurcation of Arabidopsis NLR Immune Signaling via Ca2+-Dependent Protein Kinases
Author: Gao, Xiquan; Chen, Xin; Lin, Wenwei; Chen, Sixue; Lu, Dongping; Niu, Yajie; Li, Lei; Cheng, Cheng; McCormack, Matthew Augustus; Sheen, Jenq-Yunn; Shan, Libo; He, Ping

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Citation: Gao, Xiquan, Xin Chen, Wenwei Lin, Sixue Chen, Dongping Lu, Yajie Niu, Lei Li, et al. 2013. Bifurcation of arabidopsis nlr immune signaling via ca2+-dependent protein kinases. PLoS Pathogens 9(1): e1003127.
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Abstract: Nucleotide-binding domain leucine-rich repeat (NLR) protein complexes sense infections and trigger robust immune responses in plants and humans. Activation of plant NLR resistance (R) proteins by pathogen effectors launches convergent immune responses, including programmed cell death (PCD), reactive oxygen species (ROS) production and transcriptional reprogramming with elusive mechanisms. Functional genomic and biochemical genetic screens identified six closely related Arabidopsis Ca2+-dependent protein kinases (CPKs) in mediating bifurcate immune responses activated by NLR proteins, RPS2 and RPM1. The dynamics of differential CPK1/2 activation by pathogen effectors controls the onset of cell death. Sustained CPK4/5/6/11 activation directly phosphorylates a specific subgroup of WRKY transcription factors, WRKY8/28/48, to synergistically regulate transcriptional reprogramming crucial for NLR-dependent restriction of pathogen growth, whereas CPK1/2/4/11 phosphorylate plasma membrane-resident NADPH oxidases for ROS production. Our studies delineate bifurcation of complex signaling mechanisms downstream of NLR immune sensors mediated by the myriad action of CPKs with distinct substrate specificity and subcellular dynamics.
Published Version: doi:10.1371/journal.ppat.1003127
Other Sources: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3561149/pdf/
Terms of Use: This article is made available under the terms and conditions applicable to Other Posted Material, as set forth at http://nrs.harvard.edu/urn-3:HUL.InstRepos:dash.current.terms-of-use#LAA
Citable link to this page: http://nrs.harvard.edu/urn-3:HUL.InstRepos:11235968
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