Taking the lead: NLR immune receptor N-terminal domains execute plant immune responses

Nucleotide-binding domain and leucine-rich repeat (NLR) proteins are important intracellular immune receptors that activate robust plant immune responses upon detecting pathogens. Canonical NLRs consist of a conserved tripartite architecture that includes a central regulatory nucleotide-binding domain, C-terminal leucine-rich repeats, and variable N-terminal domains that directly participate in immune execution. In flowering plants, the vast majority of NLR N-terminal domains belong to the coiled-coil, Resistance to Powdery Mildew 8, or Toll/interleukin-1 receptor subfamilies, with recent structural and biochemical studies providing detailed mechanistic insights into their functions. In this insight review, we focus on the immune-related biochemistries of known plant NLR N-terminal domains and discuss the evolutionary diversity of atypical NLR domains in nonflowering plants. We further contrast these observations against the known diversity of NLR-related receptors from microbes to metazoans across the tree of life.

Automated summary

Nucleotide-binding domain and leucine-rich repeat (NLR) proteins are intracellular immune receptors in plants that activate immune responses against pathogens. They have a conserved tripartite structure, consisting of a regulatory nucleotide-binding domain, leucine-rich repeats, and variable N-terminal domains. Recent studies have provided insights into their functions, focusing on the biochemistry and evolutionary diversity of these domains.