The DOI matches its Crossref record; 73 of the 73 references it cites were found in a registry or an index.
The NB ‐ LRR proteins RGA 4 and RGA 5 interact functionally and physically to confer disease resistance
Open accessAbstract
Plant resistance proteins of the class of nucleotide‐binding and leucine‐rich repeat domain proteins ( NB ‐ LRR s) are immune sensors which recognize pathogen‐derived molecules termed avirulence ( AVR ) proteins. We show that RGA 4 and RGA 5, two NB ‐ LRR s from rice, interact functionally and physically to mediate resistance to the fungal pathogen Magnaporthe oryzae and accomplish different functions in AVR recognition. RGA 4 triggers an AVR ‐independent cell death that is repressed in the presence of RGA 5 in both rice protoplasts and Nicotiana benthamiana . Upon recognition of the pathogen effector AVR ‐Pia by direct binding to RGA 5, repression is relieved and cell death occurs. RGA 4 and RGA 5 form homo‐ and hetero‐complexes and interact through their coiled‐coil domains. Localization studies in rice protoplast suggest that RGA 4 and RGA 5 localize to the cytosol. Upon recognition of AVR ‐Pia, neither RGA 4 nor RGA 5 is re‐localized to the nucleus. These results establish a model for the interaction of hetero‐pairs of NB ‐ LRR s in plants: RGA 4 mediates cell death activation, while RGA 5 acts as a repressor of RGA 4 and as an AVR receptor.
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Self-citationA Gateway Cloning Vector Set for High-Throughput Functional Analysis of Genes in Planta
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Cited by
Sugihara, Y., Abe, Y., Takagi, H., Abe, A., Shimizu, M., Ito, K., Kanzaki, E., Oikawa, K., Kourelis, J., Langner, T., et al. (2023) · PLOS Biology · doi:10.1371/journal.pbio.3001945 · Cited by 59
Self-citationLi, L., & Weigel, D. (2021) · Annual Review of Phytopathology · doi:10.1146/annurev-phyto-020620-114826 · Cited by 48
Metadata
- Authors
- Césari, S., Kanzaki, H., Fujiwara, T., Bernoux, M., Chalvon, V., Kawano, Y., Shimamoto, K., Dodds, P., Terauchi, R., & Kroj, T.
- Venue
- The EMBO Journal
- Published
- 2014-07-14
- Volume
- 33
- Issue
- 17
- Pages
- 1941-1959
- ISSN
- 0261-4189 (ISSN-L)
- 1460-2075
- OpenAlex
- W2136931477
- Cited by
- 371
- References
- 73
- FWCI
- 27.03
- Type
- journal article
- Language
- en
- Open access
- green
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- Césari, S., Kanzaki, H., Fujiwara, T., Bernoux, M., Chalvon, V., Kawano, Y., Shimamoto, K., Dodds, P., Terauchi, R., & Kroj, T. (2014). The NB ‐ LRR proteins RGA 4 and RGA 5 interact functionally and physically to confer disease resistance. The EMBO Journal. https://doi.org/10.15252/embj.201487923
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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