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… 
View on Wolters Kluwer
europepmc.org
38 Citations
Highly Influential Citations
3
Background Citations
13
Results Citations
1

Figures from this paper

38 Citations

Citation Type

Citation Type

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
TLDR
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.
TLDR
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.
TLDR
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.
RPW8/HR Repeats Control NLR Activation in A. thaliana
TLDR
The number of RPW8/HR repeats and the short C-terminal tail correlate, in an allele-specific manner, with the severity of hybrid necrosis when these alleles are combined with RPP7 variants, and this findings are discussed in light of sequence similarity between RPW 8/HR and pore-forming toxins MLKL and HET-S from mammals and fungi.
RPW8/HR repeats control NLR activation in Arabidopsis thaliana
TLDR
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
TLDR
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
TLDR
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
TLDR
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.
Plant pathogens convergently evolved to counteract redundant nodes of an NLR immune receptor network
TLDR
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.
...
...

References

SHOWING 1-10 OF 89 REFERENCES
A novel conserved mechanism for plant NLR protein pairs: the “integrated decoy” hypothesis
TLDR
An “integrated decoy” model for the function of these receptor complexes is described, in which a plant protein targeted by an effector has been duplicated and fused to one member of the NLR pair, where it acts as a bait to trigger defense signaling by the second NLR upon effector binding.
The CC domain structure from the wheat stem rust resistance protein Sr33 challenges paradigms for dimerization in plant NLR proteins
TLDR
The solution structure of the N-terminal coiled-coil domain from the wheat stem rust resistance protein Sr33 is reported, suggesting that self-association of the minimal CC domain is necessary for signaling but is likely to involve a different structural basis than previously suggested by the MLA10 crystallographic dimer.
Animal NLRs provide structural insights into plant NLR function
TLDR
The similarities and differences between plant and animal NLRs are assessed, and the structural information on the animal NLR pair NAIP/NLRC4 is used to derive a plausible model for plant NLR activation.
Structure-Function Analysis of Barley NLR Immune Receptor MLA10 Reveals Its Cell Compartment Specific Activity in Cell Death and Disease Resistance
TLDR
Data showing an essential and sufficient nuclear MLA10 activity in disease resistance and cell death signaling in barley and Nicotiana benthamiana suggests a bifurcation of MLA10-triggered cell death and disease resistance signaling in a compartment-dependent manner.
Structural insights into plant NLR immune receptor function
TLDR
A clearer view is provided into exactly how NLR proteins function, including how the immune response is suppressed in the absence of pathogens and how it is appropriately activated.
How to build a pathogen detector: structural basis of NB-LRR function.
Structural and functional analysis of a plant resistance protein TIR domain reveals interfaces for self-association, signaling, and autoregulation.
Integration of decoy domains derived from protein targets of pathogen effectors into plant immune receptors is widespread
TLDR
This study suggests that integration of decoy domains in NLR immune receptors is widespread and frequent in plants and the integrated decoy model is therefore a powerful concept to identify new proteins involved in disease resistance.
The “sensor domains” of plant NLR proteins: more than decoys?
TLDR
It is proposed to refer to the extraneous domains of classic NLR proteins described by Cesari et al. (2014) as sensor domains (SD), a term that is agnostic to any potential biochemical activities of the integrated module.
Multiple Domain Associations within the Arabidopsis Immune Receptor RPP1 Regulate the Activation of Programmed Cell Death
TLDR
It is demonstrated that the nucleotide-binding (NB)-ARC1 region of RPP1 self-associates and plays a critical role in cell death activation, likely by facilitating TIR:TIR interactions.
...
...