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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
2011-2-15
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pubmed:abstractText |
Plants have evolved sophisticated surveillance systems to recognize pathogen effectors delivered into host cells. RPM1 is an NB-LRR immune receptor that recognizes the Pseudomonas syringae effectors AvrB and AvrRpm1. Both effectors associate with and affect the phosphorylation of RIN4, an immune regulator. Although the kinase and the specific mechanisms involved are unclear, it has been hypothesized that RPM1 recognizes phosphorylated RIN4. Here, we identify RIPK as a RIN4-interacting receptor-like protein kinase that phosphorylates RIN4. In response to bacterial effectors, RIPK phosphorylates RIN4 at amino acid residues T21, S160, and T166. RIN4 phosphomimetic mutants display constitutive activation of RPM1-mediated defense responses and RIN4 phosphorylation is induced by AvrB and AvrRpm1 during P. syringae infection. RIPK knockout lines exhibit reduced RIN4 phosphorylation and blunted RPM1-mediated defense responses. Taken together, our results demonstrate that the RIPK kinase associates with and modifies an effector-targeted protein complex to initiate host immunity.
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pubmed:grant |
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pubmed:commentsCorrections |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Arabidopsis Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/AvrB protein, Pseudomonas syringae,
http://linkedlifedata.com/resource/pubmed/chemical/AvrRpm1 protein, Pseudomonas...,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/RIN4 protein, Arabidopsis,
http://linkedlifedata.com/resource/pubmed/chemical/RPM1 protein, Arabidopsis,
http://linkedlifedata.com/resource/pubmed/chemical/Threonine
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
1934-6069
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pubmed:author |
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pubmed:copyrightInfo |
Copyright © 2011 Elsevier Inc. All rights reserved.
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pubmed:issnType |
Electronic
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pubmed:day |
17
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pubmed:volume |
9
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
137-46
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pubmed:meshHeading |
pubmed-meshheading:21320696-Amino Acid Sequence,
pubmed-meshheading:21320696-Arabidopsis,
pubmed-meshheading:21320696-Arabidopsis Proteins,
pubmed-meshheading:21320696-Bacterial Proteins,
pubmed-meshheading:21320696-Carrier Proteins,
pubmed-meshheading:21320696-Cytoplasm,
pubmed-meshheading:21320696-Host-Pathogen Interactions,
pubmed-meshheading:21320696-Immunity, Innate,
pubmed-meshheading:21320696-Molecular Sequence Data,
pubmed-meshheading:21320696-Phosphorylation,
pubmed-meshheading:21320696-Plant Diseases,
pubmed-meshheading:21320696-Protein Binding,
pubmed-meshheading:21320696-Protein Kinases,
pubmed-meshheading:21320696-Protein Structure, Tertiary,
pubmed-meshheading:21320696-Pseudomonas syringae,
pubmed-meshheading:21320696-Sequence Alignment,
pubmed-meshheading:21320696-Threonine
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pubmed:year |
2011
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pubmed:articleTitle |
A receptor-like cytoplasmic kinase phosphorylates the host target RIN4, leading to the activation of a plant innate immune receptor.
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pubmed:affiliation |
Department of Plant Pathology, University of California, Davis, 95616, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, N.I.H., Extramural
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