Uncoiling CNLs: Structure/Function Approaches to Understanding CC Domain Function in Plant NLRs

@article{Bentham2018UncoilingCS,
  title={Uncoiling CNLs: Structure/Function Approaches to Understanding CC Domain Function in Plant NLRs},
  author={Adam R. Bentham and Rafał Zdrzałek and Juan Carlos De la Concepcion and Mark J. Banfield},
  journal={Plant and Cell Physiology},
  year={2018},
  volume={59},
  pages={2398 - 2408}
}
Abstract Plant nucleotide-binding leucine-rich repeat receptors (NLRs) are intracellular pathogen receptors whose N-terminal domains are integral to signal transduction after perception of a pathogen-derived effector protein. The two major plant NLR classes are defined by the presence of either a Toll/interleukin-1 receptor (TIR) or a coiled-coil (CC) domain at their N-terminus (TNLs and CNLs). Our knowledge of how CC domains function in plant CNLs lags behind that of how TIR domains function… 
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Genome-wide functional analyses of plant coiled–coil NLR-type pathogen receptors reveal essential roles of their N-terminal domain in oligomerization, networking, and immunity
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It is shown that upon pathogen perception, NLRs use their N-terminal domains to transactivate other receptors, suggesting that plant NLRs oligomerize upon activation, similar to the vertebrate NLRs; however, consistent with their large number in plants, the complexes are highly heterometric.
Advancement of research on plant NLRs evolution, biochemical activity, structural association, and engineering.
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A review of evolution of plant intracellular immune receptors, oligomeric complex formation, enzymatic action, engineering, and mechanisms of immune inspection for appropriate defense outcomes highlights structural basis of perception of the virulence factors by NLRs or NLR pairs to design novel classes of plant immune receptors.
Diversity, structure and function of the coiled-coil domains of plant NLR immune receptors.
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This review outlines the current understanding of NLR CC domains, including their diversity/classification and structure, their roles in cell death induction, disease resistance, and interaction with other proteins, and provides possible directions for future work.
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Deleterious allele-specific interactions between an NLR and a non-NLR gene cluster are reported, resulting in not one, but multiple hybrid necrosis cases in Arabidopsis thaliana.
An N-terminal motif in NLR immune receptors is functionally conserved across distantly related plant species
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In vitro Mu transposition is used to generate a random truncation library and identify the minimal functional region of NLRs and revealed that the NRC4 N-terminal 29 amino acids are sufficient to induce hypersensitive cell death.
Three conserved hydrophobic residues in the CC domain of Pit contribute to its plasma membrane localization and immune induction
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It is revealed that the rice NLR Pit self-associates through its CC domain, and the role of the three conserved hydrophobic residues in Pit is found to be involved in the plasma membrane localization.
Help wanted: helper NLRs and plant immune responses.
Plant pathogens convergently evolved to counteract redundant nodes of an NLR immune receptor network
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Plant pathogens have evolved to counteract central nodes of the NRC immune receptor network through different mechanisms, concluding that NRC diversification into functionally redundant nodes in a massively expanded NLR network.
NLR singletons, pairs, and networks: evolution, assembly, and regulation of the intracellular immunoreceptor circuitry of plants.
Animal NLRs continue to inform plant NLR structure and function.
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