Towards the structure of the TIR-domain signalosome

Nimma, Surekha; Ve, Thomas; Williams, Simon J.; Kobe, Boštjan

doi:10.1016/j.sbi.2016.12.014

Cited by 67 publications

(74 citation statements)

References 65 publications

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“…The TIR domain was first determined after sequence alignments of the IL‐1R and the Drosophila protein Toll showing sequence similarities . Both molecules are involved in innate immunity not only in animals but also in plants and are even found in bacterial proteins (, reviewed in ). In mammals, TIR domains are conserved among TLRs, IL‐1Rs and the MyD88 family of adapter molecules (reviewed in ).…”

Section: Membrane‐proximal Signaling Events In the Tir Domain‐containmentioning

confidence: 99%

The family of the interleukin‐1 receptors

Boraschi

Italiani

Weil

et al. 2017

Immunological Reviews

264

225

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The extracellular forms of the IL-1 cytokines are active through binding to specific receptors on the surface of target cells. IL-1 ligands bind to the extracellular portion of their ligand-binding receptor chain. For signaling to take place, a non-binding accessory chain is recruited into a heterotrimeric complex. The intracellular approximation of the Toll-IL-1-receptor (TIR) domains of the 2 receptor chains is the event that initiates signaling. The family of IL-1 receptors (IL-1R) includes 10 structurally related members, and the distantly related soluble protein IL-18BP that acts as inhibitor of the cytokine IL-18. Over the years the receptors of the IL-1 family have been known with many different names, with significant confusion. Thus, we will use here a recently proposed unifying nomenclature. The family includes several ligand-binding chains (IL-1R1, IL-1R2, IL-1R4, IL-1R5, and IL-1R6), 2 types of accessory chains (IL-1R3, IL-1R7), molecules that act as inhibitors of signaling (IL-1R2, IL-1R8, IL-18BP), and 2 orphan receptors (IL-1R9, IL-1R10). In this review, we will examine how the receptors of the IL-1 family regulate the inflammatory and anti-inflammatory functions of the IL-1 cytokines and are, more at large, involved in modulating defensive and pathological innate immunity and inflammation. Regulation of the IL-1/IL-1R system in the brain will be also described, as an example of the peculiarities of organ-specific modulation of inflammation.

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Section: Membrane‐proximal Signaling Events In the Tir Domain‐containmentioning

confidence: 99%

The family of the interleukin‐1 receptors

Boraschi

Italiani

Weil

et al. 2017

Immunological Reviews

264

225

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“…N-terminal selfassociation is important for cell death induction and is thought to allow interaction with undefined signaling partners. Signaling could involve higher order NLR assembly but this has not been experimentally documented in plants (Nimma et al, 2017 effectors from diverse pathogens was created that conferred, in combination with RPS5, resistance to new pathogens (Kim et al, 2016). This strategy may be broadly applicable, as diverse pathogens are known to secrete proteases during host infection.…”

Section: How To Engineer Nlr-mediated Disease Resistance?mentioning

confidence: 99%

Section: How To Engineer Nlr-mediated Disease Resistance?mentioning

confidence: 99%

Multiple strategies for pathogen perception by plant immune receptors

2017

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Contents Summary17I.Introduction17II.Pathogen perception by NLRs: from direct recognition to integrated decoys18III.Multiple activation and signaling pathways for NLRs18IV.How to engineer NLR‐mediated disease resistance?21V.Conclusion23Acknowledgements23References23 Summary Plants have evolved a complex immune system to protect themselves against phytopathogens. A major class of plant immune receptors called nucleotide‐binding domain and leucine‐rich repeat‐containing proteins (NLRs) is ubiquitous in plants and is widely used for crop disease protection, making these proteins critical contributors to global food security. Until recently, NLRs were thought to be conserved in their modular architecture and functional features. Investigation of their biochemical, functional and structural properties has revealed fascinating mechanisms that enable these proteins to perceive a wide range of pathogens. Here, I review recent insights demonstrating that NLRs are more mechanistically and structurally diverse than previously thought. I also discuss how these findings provide exciting future prospects to improve plant disease resistance.

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“…The best hit corresponds to the TIR domain of the TNL SNC1 [69, 70], predicted with 100% confidence over 155 amino acid residues (8-163), encompassing the MIST1 predicted TIR domain; SNC1 is included amongst the structure-based phylogeny of proteins similar to hSARM1 TIR as described by [67]. The available data on TIR-TIR interactions is compatible with their association into high-order oligomers, stabilized in activated NLRs by self-association of other domains such as NB-ARC [71]. Interestingly, MIST1 also displays high structural homology with the CNL ZAR1 [72], predicted with 100% confidence over 700 amino acids (120-820) mostly outside MIST1 TIR domain, despite ZAR1 and MIST1 only sharing 18% sequence identity over the same region.…”

Section: Discussionmentioning

confidence: 99%

MiRNA and phasiRNAs-mediated regulation of TIR-NBS-LRR defense genes inArabidopsis thaliana

López-Márquez

Del-Espino

López-Pagán

et al. 2020

Preprint

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Plants encode large numbers of intracellular immune receptors known as resistance (R) proteins or nucleotide-binding (NB) leucine-rich repeat (LRR) receptors (NLRs), involved in perception of pathogen-derived effectors and activation of immunity.Here, we report a two-tiered regulatory network mediated by microRNA and secondary phased small RNAs (phasiRNA) that targets the silencing of dozens of NLR genes encoding yet uncharacterized members of the Toll/interleukin-1 (TIR)-NBS-LRR (TNLs) subfamily in Arabidopsis. We show that miR825-5p downregulates expression of Arabidopsis AT5G38850 gene (renamed as microRNA-silenced TNL 1 or MIST1) by targeting the sequence coding for a highly conserved functional amino acid motif (TIR2) within the TIR domain of the receptor. Further, we show that MIST1 functions as a regulatory hub, since miRNA825-5p triggers RDR6-mediated processing of MIST1 transcripts, to generate trans-acting phasiRNAs that in turn target, a wide network of TNL genes for gene silencing. Regulation through MIST1 affects disease resistance against the model bacterial pathogen Pseudomonas syringae, since altered levels of miRNA825-5p lead to changes in Arabidopsis ability to establish basal defenses against this pathogen. MiR825-5p is expressed in unchallenged adult leaves and its production is down regulated in response to PAMPs such as bacterial flagellin but also fungal chitin.

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Towards the structure of the TIR-domain signalosome

Cited by 67 publications

References 65 publications

The family of the interleukin‐1 receptors

The family of the interleukin‐1 receptors

Multiple strategies for pathogen perception by plant immune receptors

MiRNA and phasiRNAs-mediated regulation of TIR-NBS-LRR defense genes inArabidopsis thaliana

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