Wang, JunzhuChen, TianyuanHan, MengQian, LichaoLi, JinlinWu, MingHan, TingCao, JidongNagalakshmi, UgrappaRathjen, JohnHong, YiguoLiu, Yule2022-09-292022-09-29Wang J, Chen T, Han M, Qian L, Li J, Wu M, et al. (2020) Plant NLR immune receptor Tm- 22 activation requires NB-ARC domain-mediated self-association of CC domain. PLoS Pathog 16(4): e1008475. https://doi.org/10.1371/journal. ppat.10084751553-7366http://hdl.handle.net/1885/274187The nucleotide-binding, leucine-rich repeat-containing (NLR) class of immune receptors of plants and animals recognize pathogen-encoded proteins and trigger host defenses. Although animal NLRs form oligomers upon pathogen recognition to activate downstream signaling, the mechanisms of plant NLR activation remain largely elusive. Tm-22 is a plasma membrane (PM)-localized coiled coil (CC)-type NLR and confers resistance to Tobacco mosaic virus (TMV) by recognizing its viral movement protein (MP). In this study, we found that Tm-22 self-associates upon recognition of MP. The CC domain of Tm-22 is the signaling domain and its function requires PM localization and self-association. The nucleotide-binding (NB-ARC) domain is important for Tm-22 self-interaction and regulates activation of the CC domain through its nucleotide-binding and self-association. (d)ATP binding may alter the NB-ARC conformation to release its suppression of Tm-22 CC domain-mediated cell death. Our findings provide the first example of signaling domain for PM-localized NLR and insight into PM-localized NLR activation.This work was supported by the National Natural Science Foundation of China (31530059, 31920103013 and 31421001) and the National Transgenic Program of China (2019ZX08009-003; 2019ZX08005-001).application/pdfen-AU© 2020 Wang et al.https://creativecommons.org/licenses/by/4.0/2020-04-2710.1371/journal.ppat.10084752021-11-28Creative Commons Attribution License