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<p>Fungi, arthropods, and nematodes are chitin-containing organisms that cause severe damage to crop production. Plants can sense chitin to activate immunity against these invaders. In <i>Arabidopsis thaliana</i> (<i>Arabidopsis</i>), the lysin motif-containing receptor kinases (LysM-RKs) AtLYK5 and AtCERK1 are considered the primary chitin receptor and coreceptor for chitin binding and signaling, respectively. However, several studies indicate that AtCERK1 also possesses chitin-binding ability, raising a critical question: can AtCERK1 respond to chitin independently? To address this question, we generated an octuple mutant allele lacking all LysM receptors and hierarchically complemented the LysM-RKs involved in chitin perception. Our results revealed that while AtCERK1 alone could respond to chitin, it required an additional receptor to fully restore chitin-induced immune responses. Surprisingly, AtLYK4, the closest paralog of AtLYK5, forms a minimal chitin receptor complex with AtCERK1. Furthermore, we demonstrated that both N-glycosylation modifications of the extracellular domain of AtLYK4 and two key residues within its chitin-binding pocket were important for chitin recognition. Our findings not only revise the long-prevailing model of chitin perception but also define the core architecture of the chitin receptor complex in <i>Arabidopsis</i>. Additionally, we identify bipartite molecular determinants that regulate chitin-receptor interactions in plants.</p>

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AtLYK4 is the major chitin receptor in Arabidopsis with N-glycosylation and ligand-interacting residues orchestrating chitin perception

  • 期刊论文

  • 发表日期：

    2026年1月5日

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  • Feng-Zhu Wang,
  • Ying Bao,
  • Xinran Yao,
  • Ben-Qiang Gong,
  • Xiangyu Xiong,
  • Jia-Jun Wang,
  • Zhe Li,
  • Jian-Feng Li

摘要

Fungi, arthropods, and nematodes are chitin-containing organisms that cause severe damage to crop production. Plants can sense chitin to activate immunity against these invaders. In Arabidopsis thaliana (Arabidopsis), the lysin motif-containing receptor kinases (LysM-RKs) AtLYK5 and AtCERK1 are considered the primary chitin receptor and coreceptor for chitin binding and signaling, respectively. However, several studies indicate that AtCERK1 also possesses chitin-binding ability, raising a critical question: can AtCERK1 respond to chitin independently? To address this question, we generated an octuple mutant allele lacking all LysM receptors and hierarchically complemented the LysM-RKs involved in chitin perception. Our results revealed that while AtCERK1 alone could respond to chitin, it required an additional receptor to fully restore chitin-induced immune responses. Surprisingly, AtLYK4, the closest paralog of AtLYK5, forms a minimal chitin receptor complex with AtCERK1. Furthermore, we demonstrated that both N-glycosylation modifications of the extracellular domain of AtLYK4 and two key residues within its chitin-binding pocket were important for chitin recognition. Our findings not only revise the long-prevailing model of chitin perception but also define the core architecture of the chitin receptor complex in Arabidopsis. Additionally, we identify bipartite molecular determinants that regulate chitin-receptor interactions in plants.