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Plant NLRs are getting into higher-order architectures.

Nayun Kim1, Eunyoung Chae2, Ji-Joon Song1,3

  • 1Department of Biological Sciences, KI for BioInnovation, Korea Advanced Institute of Science and Technology (KAIST), Daejeon, 34141, Korea.

The Plant Journal : for Cell and Molecular Biology
|April 13, 2026
PubMed
Summary

Nucleotide-binding leucine-rich repeat (NLR) proteins form dynamic, higher-order structures essential for plant immunity. Understanding these assemblies reveals conserved and divergent mechanisms critical for plant defense signaling.

Keywords:
biomolecular condensateseffector‐triggered immunityfilamenthigh‐order structuresnucleotide‐binding leucine‐rich repeatresistosome

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Area of Science:

  • Plant immunology
  • Molecular and cellular biology

Background:

  • Nucleotide-binding leucine-rich repeat (NLR) proteins are key regulators of plant immunity.
  • NLRs detect pathogen effectors and trigger defense responses.
  • NLRs exhibit structural diversity due to co-evolution with pathogens.

Purpose of the Study:

  • To review recent advances in understanding the formation and function of higher-order NLR assemblies.
  • To highlight the dynamic nature of NLRs in immune signaling.
  • To discuss conserved and divergent mechanisms of NLR assembly.

Main Methods:

  • Literature review of recent structural and biochemical studies.
  • Analysis of dynamic assembly processes of NLR proteins.
  • Examination of NLR interactions within immune networks.

Main Results:

  • NLRs dynamically assemble into higher-order structures like complexes, filaments, and condensates.
  • These higher-order architectures are crucial for NLR activation and signaling.
  • Both conserved and divergent mechanisms govern NLR assembly.

Conclusions:

  • Higher-order structures are fundamental to NLR function in plant immunity.
  • Understanding NLR assembly mechanisms provides insights into plant defense strategies.
  • Further research into NLR dynamics will advance plant immune system knowledge.