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• W2136931477 endingPage "1959" @default.
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• W2136931477 abstract "Plant resistance proteins of the class of nucleotide-binding and leucine-rich repeat domain proteins (NB-LRRs) are immune sensors which recognize pathogen-derived molecules termed avirulence (AVR) proteins. We show that RGA4 and RGA5, two NB-LRRs from rice, interact functionally and physically to mediate resistance to the fungal pathogen Magnaporthe oryzae and accomplish different functions in AVR recognition. RGA4 triggers an AVR-independent cell death that is repressed in the presence of RGA5 in both rice protoplasts and Nicotiana benthamiana. Upon recognition of the pathogen effector AVR-Pia by direct binding to RGA5, repression is relieved and cell death occurs. RGA4 and RGA5 form homo- and hetero-complexes and interact through their coiled-coil domains. Localization studies in rice protoplast suggest that RGA4 and RGA5 localize to the cytosol. Upon recognition of AVR-Pia, neither RGA4 nor RGA5 is re-localized to the nucleus. These results establish a model for the interaction of hetero-pairs of NB-LRRs in plants: RGA4 mediates cell death activation, while RGA5 acts as a repressor of RGA4 and as an AVR receptor." @default.
• W2136931477 created "2016-06-24" @default.
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• W2136931477 date "2014-07-14" @default.
• W2136931477 modified "2023-10-07" @default.
• W2136931477 title "The <scp>NB</scp> ‐ <scp>LRR</scp> proteins <scp>RGA</scp> 4 and <scp>RGA</scp> 5 interact functionally and physically to confer disease resistance" @default.
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• W2136931477 doi "https://doi.org/10.15252/embj.201487923" @default.
• W2136931477 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4195788" @default.
• W2136931477 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/25024433" @default.
• W2136931477 hasPublicationYear "2014" @default.
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