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Updated: Aug 20, 2025

Identification of Post-translational Modifications of Plant Protein Complexes
Published on: February 22, 2014
Structure, biochemical function, and signaling mechanism of plant NLRs
Jizong Wang1, Wen Song2, Jijie Chai3
1State Key Laboratory of Protein and Plant Gene Research, School of Advanced Agricultural Sciences, Peking University, Beijing 100871, China; Peking University Institute of Advanced Agricultural Sciences, Shandong Laboratory of Advanced Agricultural Sciences at Weifang, Weifang, Shandong 261000, China.
Abstract:
To counter pathogen invasion, plants have evolved a large number of immune receptors, including membrane-resident pattern recognition receptors (PRRs) and intracellular nucleotide-binding and leucine-rich repeat receptors (NLRs). Our knowledge about PRR and NLR signaling mechanisms has expanded significantly over the past few years. Plant NLRs form multi-protein complexes called resistosomes in response to pathogen effectors, and the signaling mediated by NLR resistosomes converges on Ca2+-permeable channels. Ca2+-permeable channels important for PRR signaling have also been identified. These findings highlight a crucial role of Ca2+ in triggering plant immune signaling. In this review, we first discuss the structural and biochemical mechanisms of non-canonical NLR Ca2+ channels and then summarize our knowledge about immune-related Ca2+-permeable channels and their roles in PRR and NLR signaling. We also discuss the potential role of Ca2+ in the intricate interaction between PRR and NLR signaling.
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