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http://purl.uniprot.org/citations/32234500http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/32234500http://www.w3.org/2000/01/rdf-schema#comment"The Arabidopsis immune receptors RPS4 and RRS1 interact to co-confer responsiveness to bacterial effectors. The RRS1-R allele, with RPS4, responds to AvrRps4 and PopP2, whereas RRS1-S responds only to AvrRps4. Here, we show that the C terminus of RRS1-R but not RRS1-S is phosphorylated. Phosphorylation at Thr1214 in the WRKY domain maintains RRS1-R in its inactive state and also inhibits acetylation of RRS1-R by PopP2. PopP2 in turn catalyzes O-acetylation at the same site, thereby preventing its phosphorylation. Phosphorylation at other sites is required for PopP2 but not AvrRps4 responsiveness and facilitates the interaction of RRS1's C terminus with its TIR domain. Derepression of RRS1-R or RRS1-S involves effector-triggered proximity between their TIR domain and C termini. This effector-promoted interaction between these domains relieves inhibition of TIRRPS4 by TIRRRS1. Our data reveal effector-triggered and phosphorylation-regulated conformational changes within RRS1 that results in distinct modes of derepression of the complex by PopP2 and AvrRps4."xsd:string
http://purl.uniprot.org/citations/32234500http://purl.org/dc/terms/identifier"doi:10.1016/j.chom.2020.03.008"xsd:string
http://purl.uniprot.org/citations/32234500http://purl.uniprot.org/core/author"Huang J."xsd:string
http://purl.uniprot.org/citations/32234500http://purl.uniprot.org/core/author"Jones J.D.G."xsd:string
http://purl.uniprot.org/citations/32234500http://purl.uniprot.org/core/author"Guo H."xsd:string
http://purl.uniprot.org/citations/32234500http://purl.uniprot.org/core/author"Ma Y."xsd:string
http://purl.uniprot.org/citations/32234500http://purl.uniprot.org/core/author"Sklenar J."xsd:string
http://purl.uniprot.org/citations/32234500http://purl.uniprot.org/core/author"Ding P."xsd:string
http://purl.uniprot.org/citations/32234500http://purl.uniprot.org/core/author"Menke F.L.H."xsd:string
http://purl.uniprot.org/citations/32234500http://purl.uniprot.org/core/author"Ahn H.K."xsd:string
http://purl.uniprot.org/citations/32234500http://purl.uniprot.org/core/date"2020"xsd:gYear
http://purl.uniprot.org/citations/32234500http://purl.uniprot.org/core/name"Cell Host Microbe"xsd:string
http://purl.uniprot.org/citations/32234500http://purl.uniprot.org/core/pages"769-781.e6"xsd:string
http://purl.uniprot.org/citations/32234500http://purl.uniprot.org/core/title"Phosphorylation-Regulated Activation of the Arabidopsis RRS1-R/RPS4 Immune Receptor Complex Reveals Two Distinct Effector Recognition Mechanisms."xsd:string
http://purl.uniprot.org/citations/32234500http://purl.uniprot.org/core/volume"27"xsd:string
http://purl.uniprot.org/citations/32234500http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/32234500
http://purl.uniprot.org/citations/32234500http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/32234500
http://purl.uniprot.org/uniprot/#_E1B328-mappedCitation-32234500http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/32234500
http://purl.uniprot.org/uniprot/#_P0DKH5-mappedCitation-32234500http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/32234500
http://purl.uniprot.org/uniprot/#_Q9XGM3-mappedCitation-32234500http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/32234500
http://purl.uniprot.org/uniprot/Q9XGM3http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/32234500
http://purl.uniprot.org/uniprot/P0DKH5http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/32234500
http://purl.uniprot.org/uniprot/E1B328http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/32234500