The “sensor domains” of plant NLR proteins: more than decoys?

Wu, Chih‐Hang; Krasileva, Ksenia V.; Banfield, Mark J.; Terauchi, Ryohei; Kamoun, Sophien

doi:10.3389/fpls.2015.00134

Cited by 79 publications

(80 citation statements)

References 10 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Intriguingly, at least in the case of the Arabidopsis helper NLR ADR1, the integrity of the P-loop is not required for HR signalling (Bonardi et al, 2011), in contrast to the ATP-dependent NAIP/NLRC4 system. The plant NLR pairs that have been described to contain 'integrated decoy' or 'sensor' domains (Cesari et al, 2014a;Maqbool et al, 2015;Le Roux et al, 2015;Wu et al, 2015;Kroj et al, 2016;Sarris et al, 2016) may in fact be more difficult to reconcile with the NAIP/ NLRC4 model. For instance, RPS4 and RRS1 appear to interact in both pre-and post-activated states, with the protein partners playing key roles in regulation as well as activation.…”

Section: Conclusion Outlook and Future Directionsmentioning

confidence: 99%

Animal NLRs provide structural insights into plant NLR function

Bentham

Burdett

Anderson

et al. 2016

Ann Bot

View full text Add to dashboard Cite

Background The plant immune system employs intracellular NLRs (nucleotide binding [NB], leucine-rich repeat [LRR]/nucleotide-binding oligomerization domain [NOD]-like receptors) to detect effector proteins secreted into the plant cell by potential pathogens. Activated plant NLRs trigger a range of immune responses, collectively known as the hypersensitive response (HR), which culminates in death of the infected cell. Plant NLRs show structural and functional resemblance to animal NLRs involved in inflammatory and innate immune responses. Therefore, knowledge of the activation and regulation of animal NLRs can help us understand the mechanism of action of plant NLRs, and vice versa.Scope This review provides an overview of the innate immune pathways in plants and animals, focusing on the available structural and biochemical information available for both plant and animal NLRs. We highlight the gap in knowledge between the animal and plant systems, in particular the lack of structural information for plant NLRs, with crystal structures only available for the N-terminal domains of plant NLRs and an integrated decoy domain, in contrast to the more complete structures available for animal NLRs. We assess the similarities and differences between plant and animal NLRs, and use the structural information on the animal NLR pair NAIP/NLRC4 to derive a plausible model for plant NLR activation.Conclusions Signalling by cooperative assembly formation (SCAF) appears to operate in most innate immunity pathways, including plant and animal NLRs. Our proposed model of plant NLR activation includes three key steps: (1) initially, the NLR exists in an inactive auto-inhibited state; (2) a combination of binding by activating elicitor and ATP leads to a structural rearrangement of the NLR; and (3) signalling occurs through cooperative assembly of the resistosome. Further studies, structural and biochemical in particular, will be required to provide additional evidence for the different features of this model and shed light on the many existing variations, e.g. helper NLRs and NLRs containing integrated decoys.

show abstract

Section: Conclusion Outlook and Future Directionsmentioning

confidence: 99%

Animal NLRs provide structural insights into plant NLR function

Bentham

Burdett

Anderson

et al. 2016

Ann Bot

View full text Add to dashboard Cite

show abstract

“…An interesting and exciting solution to this evolutionary conundrum, coined ‘integrated domains’, has recently gained wide attention (Fig. ; Cesari et al ., ; Wu et al ., ; reviewed by Ellis, ; Krattinger & Keller, ). Several independent studies have reported that protein domains mimicking effector targets can be integrated into NLR immune receptors where they act as effector traps.…”

Section: Inside the Cell – The Role Of Intracellular Immune Receptorsmentioning

confidence: 99%

Molecular genetics and evolution of disease resistance in cereals

2016

View full text Add to dashboard Cite

Contents 320I.320II.321III.321IV.322V.324VI.328VII.329330References330 Summary Cereal crops produce a large part of the globally consumed food and feed. Because of the constant presence of devastating pathogens, the molecular characterization of disease resistance is a major research area and highly relevant for breeding. There has been recent and accelerating progress in the understanding of three distinct resistance mechanisms in cereals: resistance conferred by plasma membrane‐localized receptor proteins; race‐specific resistance conferred by intracellular immune receptors; and quantitative disease resistance. Intracellular immune receptors provide a particularly rich source for evolutionary studies, and have, for example, resulted in the recent discovery of a novel detection mechanism based on integrated decoy domains. Evolutionary studies have also revealed the origins of active resistance genes in both wild progenitors of today's cereals as well as in cultivated forms. In addition, independent evolution of orthologous genes in related cereals has resulted in resistance to different pathogen species. Quantitative resistance genes have been best characterized in wheat. The quantitative resistance genes identified so far in wheat encode transporter proteins or unusual kinase proteins. The recent discoveries in these three different resistance mechanisms have contributed to the basic molecular understanding of cereal immunity against pathogens and have suggested novel applications for resistance breeding.

show abstract

“…It is also possible that pathogen effectors directly target sensor NLRs to facilitate pathogen virulence in susceptible genotypes (Wu et al, 2015). The extra domain present on the sensor NLR could either be a decoy or a bona fide effector virulence target (Wu et al, 2015). Multiple head-to-head NLR pairs with one member possessing an additional domain have been identified, indicating that the integrated decoy hypothesis may be one broadly conserved mechanism for NLR activation (Césari et al, 2014a).…”

Section: Nlr Pairsmentioning

confidence: 99%

“…Effector binding then facilitates activation of the second signaling NLR with classical domain architecture, leading to ETI (Césari et al, 2014a). It is also possible that pathogen effectors directly target sensor NLRs to facilitate pathogen virulence in susceptible genotypes (Wu et al, 2015). The extra domain present on the sensor NLR could either be a decoy or a bona fide effector virulence target (Wu et al, 2015).…”

Section: Nlr Pairsmentioning

confidence: 99%