TY - JOUR
T1 - Oligomerization of a plant helper NLR requires cell-surface and intracellular immune receptor activation
AU - Feehan, Joanna M.
AU - Wang, Junli
AU - Sun, Xinhua
AU - Choi, Jihyeon
AU - Ahn, Hee-Kyung
AU - Ngou, Bruno Pok Man
AU - Parker, Jane E.
AU - Jones, Jonathan D. G.
N1 - Data, Materials, and Software Availability: All study data are included in the article and/or SI Appendix.
Funding Information: Work in the Parker lab was supported by the Max-Planck Society, Deutsche Forschungsgemeinschaft grant SFB-1403–414786233 (J.E.P., X.S.) and an Alexander von Humboldt Foundation postdoctoral fellowship (J.W.). Work in the Jones lab was supported by European Research Council Advanced Investigator grant “ImmunityByPairDesign" (H.-K.A.), Biotechnology and Biological Sciences Research Council Doctoral Training Partnership program (B.P.M.N.), and by Gatsby Foundation support to TSL (J.M.F. and J.D.G.J.).
PY - 2023/3/14
Y1 - 2023/3/14
N2 - Plant disease resistance involves both detection of microbial molecular patterns by cell-surface pattern recognition receptors and detection of pathogen effectors by intracellular NLR immune receptors. NLRs are classified as sensor NLRs, involved in effector detection, or helper NLRs required for sensor NLR signaling. TIR-domain-containing sensor NLRs (TNLs) require helper NLRs NRG1 and ADR1 for resistance, and helper NLR activation of defense requires the lipase-domain proteins EDS1, SAG101, and PAD4. Previously, we found that NRG1 associates with EDS1 and SAG101 in a TNL activation-dependent manner [X. Sun et al., Nat. Commun. 12, 3335 (2021)]. We report here how the helper NLR NRG1 associates with itself and with EDS1 and SAG101 during TNL-initiated immunity. Full immunity requires coactivation and mutual potentiation of cell-surface and intracellular immune receptor-initiated signaling [B. P. M. Ngou, H.-K. Ahn, P. Ding, J. D. G. Jones, Nature 592, 110–115 (2021), M. Yuan et al., Nature 592, 105–109 (2021)]. We find that while activation of TNLs is sufficient to promote NRG1–EDS1–SAG101 interaction, the formation of an oligomeric NRG1–EDS1–SAG101 resistosome requires the additional coactivation of cell-surface receptor-initiated defense. These data suggest that NRG1–EDS1–SAG101 resistosome formation in vivo is part of the mechanism that links intracellular and cell-surface receptor signaling pathways.
AB - Plant disease resistance involves both detection of microbial molecular patterns by cell-surface pattern recognition receptors and detection of pathogen effectors by intracellular NLR immune receptors. NLRs are classified as sensor NLRs, involved in effector detection, or helper NLRs required for sensor NLR signaling. TIR-domain-containing sensor NLRs (TNLs) require helper NLRs NRG1 and ADR1 for resistance, and helper NLR activation of defense requires the lipase-domain proteins EDS1, SAG101, and PAD4. Previously, we found that NRG1 associates with EDS1 and SAG101 in a TNL activation-dependent manner [X. Sun et al., Nat. Commun. 12, 3335 (2021)]. We report here how the helper NLR NRG1 associates with itself and with EDS1 and SAG101 during TNL-initiated immunity. Full immunity requires coactivation and mutual potentiation of cell-surface and intracellular immune receptor-initiated signaling [B. P. M. Ngou, H.-K. Ahn, P. Ding, J. D. G. Jones, Nature 592, 110–115 (2021), M. Yuan et al., Nature 592, 105–109 (2021)]. We find that while activation of TNLs is sufficient to promote NRG1–EDS1–SAG101 interaction, the formation of an oligomeric NRG1–EDS1–SAG101 resistosome requires the additional coactivation of cell-surface receptor-initiated defense. These data suggest that NRG1–EDS1–SAG101 resistosome formation in vivo is part of the mechanism that links intracellular and cell-surface receptor signaling pathways.
KW - defense signaling
KW - NLR immune receptor proteins
KW - plant immunity
KW - TIR domain
UR - http://www.scopus.com/inward/record.url?scp=85150000008&partnerID=8YFLogxK
U2 - 10.1073/pnas.2210406120
DO - 10.1073/pnas.2210406120
M3 - Article
C2 - 36877846
AN - SCOPUS:85150000008
SN - 0027-8424
VL - 120
JO - Proceedings of the National Academy of Sciences of the United States of America
JF - Proceedings of the National Academy of Sciences of the United States of America
IS - 11
M1 - e2210406120
ER -