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<p>Kinase fusion proteins (KFPs) are an emerging class of diverse intracellular plant immune receptors with critical roles in immunity in wheat (<i>Triticum aestivum</i>) and other members of the Triticeae. These proteins contain at least one kinase domain fused to one or more additional domains, possibly including another kinase domain. Many KFP kinase domains are predicted to possess an atypical structural motif, the extended β-finger, indicating that KFPs may operate through shared mechanisms in plant immunity despite their structural diversity. Recent research has demonstrated that KFP SR62<sup>TK</sup> from <i>Aegilops sharonensis</i> and RWT4 (allelic to PM24) from wheat serve as primary receptors that initiate immune signaling by recruiting a nucleotide-binding leucine-rich repeat (NLR) protein similar to sensor and helper NLR pairs. This study consolidates the current understanding of KFPs, emphasizing their structural and functional diversity, evolutionary significance and potential for engineering durable disease resistance in crops.</p>

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The emerging role of kinase fusion proteins in cereal immunity

  • 期刊论文

  • 发表日期：

    2026年3月3日

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  • Oliver R. Powell,
  • Francisco J. Guzmán-Vega,
  • Daniel S. Yu,
  • Yan L. Wang,
  • Ping Lu,
  • Stefan T. Arold,
  • Zhiyong Liu,
  • Mark J. Banfield,
  • Brande B. H. Wulff,
  • Renjie Chen

摘要

Kinase fusion proteins (KFPs) are an emerging class of diverse intracellular plant immune receptors with critical roles in immunity in wheat (Triticum aestivum) and other members of the Triticeae. These proteins contain at least one kinase domain fused to one or more additional domains, possibly including another kinase domain. Many KFP kinase domains are predicted to possess an atypical structural motif, the extended β-finger, indicating that KFPs may operate through shared mechanisms in plant immunity despite their structural diversity. Recent research has demonstrated that KFP SR62TK from Aegilops sharonensis and RWT4 (allelic to PM24) from wheat serve as primary receptors that initiate immune signaling by recruiting a nucleotide-binding leucine-rich repeat (NLR) protein similar to sensor and helper NLR pairs. This study consolidates the current understanding of KFPs, emphasizing their structural and functional diversity, evolutionary significance and potential for engineering durable disease resistance in crops.