The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.
A Receptor-like Cytoplasmic Kinase Phosphorylates the Host Target RIN4, Leading to the Activation of a Plant Innate Immune Receptor
Open accessAbstract
SUMMARY 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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Jones, J. D. G., & Dangl, J. L. (2006) · Nature · doi:10.1038/nature05286 · Cited by 13,177
Host-Microbe Interactions: Shaping the Evolution of the Plant Immune Response
Chisholm, S. T., Coaker, G., Day, B., & Staskawicz, B. J. (2006) · Cell · doi:10.1016/j.cell.2006.02.008 · Cited by 2,957
Self-citationNLRs at the intersection of cell death and immunity
Ting, J. P.-Y., Willingham, S. B., & Bergstralh, D. T. (2008) · Nature Reviews Immunology · doi:10.1038/nri2296 · Cited by 371 · cited 1×
“Plant NB-LRR immune receptors are structurally analogous to animal NLR (nucleotide-binding domain, leucine-rich repeat containing) receptors (Ting et al., 2008).”
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Cited by
Wan, J., Tanaka, K., Zhang, X.-C., Son, G. H., Brechenmacher, L., Nguyen, T. H. N., & Stacey, G. (2012) · Plant Physiology · doi:10.1104/pp.112.201699 · Cited by 305
Pathogen Effectors Target Arabidopsis EDS1 and Alter Its Interactions with Immune Regulators
Bhattacharjee, S., Halane, M. K., Kim, S. H., & Gassmann, W. (2011) · Science · doi:10.1126/science.1211592 · Cited by 305
Wang, G., Roux, B., Feng, F., Guy, E., Li, L., Li, N., Zhang, X., Lautier, M., Jardinaud, M.-F., Chabannes, M., et al. (2015) · Cell Host & Microbe · doi:10.1016/j.chom.2015.08.004 · Cited by 273
Metadata
- Authors
- Liu, J., Elmore, J. M., Lin, Z.-J. D., & Coaker, G.
- Venue
- Cell Host & Microbe
- Publisher
- Elsevier BV
- Published
- 2011-02
- Volume
- 9
- Issue
- 2
- Pages
- 137-146
- ISSN
- 1931-3128 (ISSN-L)
- OpenAlex
- W2023721784
- Cited by
- 334
- References
- 3
- FWCI
- 27.24
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Liu, J., Elmore, J. M., Lin, Z.-J. D., & Coaker, G. (2011). A Receptor-like Cytoplasmic Kinase Phosphorylates the Host Target RIN4, Leading to the Activation of a Plant Innate Immune Receptor. Cell Host & Microbe. https://doi.org/10.1016/j.chom.2011.01.010
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