scholarly journals A Coevolved EDS1-SAG101-NRG1 Module Mediates Cell Death Signaling by TIR-Domain Immune Receptors

2019 ◽  
Vol 31 (10) ◽  
pp. 2430-2455 ◽  
Author(s):  
Dmitry Lapin ◽  
Viera Kovacova ◽  
Xinhua Sun ◽  
Joram A. Dongus ◽  
Deepak Bhandari ◽  
...  
Keyword(s):  
Cell Death ◽  
Tir Domain ◽  
Immune Receptors ◽  
Cell Death Signaling

scholarly journals A coevolved EDS1-SAG101-NRG1 module mediates cell death signaling by TIR-domain immune receptors

2019 ◽  
Author(s):  
Dmitry Lapin ◽  
Viera Kovacova ◽  
Xinhua Sun ◽  
Joram Dongus ◽  
Deepak D. Bhandari ◽  
...  
Keyword(s):  
Cell Death ◽  
Coiled Coil ◽  
Rate Variation ◽  
Distinctive Features ◽  
Tir Domain ◽  
Immune Receptors ◽  
Pathogen Effectors ◽  
Cell Death Signaling ◽  
Basal Defense

AbstractPlant intracellular nucleotide-binding/leucine-rich repeat (NLR) immune receptors are activated by pathogen effectors to trigger host defenses and cell death. Toll-Interleukin1-receptor (TIR)-domain NLRs (TNLs) converge on the Enhanced Disease Susceptibility1 (EDS1) family of lipase-like proteins for all resistance outputs. In Arabidopsis TNL immunity,AtEDS1 heterodimers with Phytoalexin Deficient4 (AtPAD4) transcriptionally boost basal defense pathways.AtEDS1 uses the same surface to interact with PAD4-related Senescence-Associated Gene101 (AtSAG101), but the role ofAtEDS1-AtSAG101 heterodimers was unclear. We show thatAtEDS1-AtSAG101 function together withAtNRG1 coiled-coil domain helper NLRs as a coevolved TNL cell death signaling module.AtEDS1-AtSAG101-AtNRG1 cell death activity is transferable to the solanaceous species,Nicotiana benthamiana, and cannot be substituted byAtEDS1-AtPAD4 withAtNRG1 orAtEDS1-AtSAG101 with endogenousNbNRG1. Analysis of EDS1-family evolutionary rate variation and heterodimer structure-guided phenotyping ofAtEDS1 variants orAtPAD4-AtSAG101 chimeras identify closely aligned α-helical coil surfaces in theAtEDS1-AtSAG101 partner C-terminal domains that are necessary for TNL cell death signaling. Our data suggest that TNL-triggered cell death and pathogen growth restriction are determined by distinctive features of EDS1-SAG101 and EDS1-PAD4 complexes and that these signaling machineries coevolved with further components within plant species or clades to regulate downstream pathways in TNL immunity.

scholarly journals Cytosolic activation of cell death and stem rust resistance by cereal MLA-family CC–NLR proteins

2016 ◽  
Vol 113 (36) ◽  
pp. 10204-10209 ◽  
Author(s):  
Stella Cesari ◽  
John Moore ◽  
Chunhong Chen ◽  
Daryl Webb ◽  
Sambasivam Periyannan ◽  
...  
Keyword(s):  
Cell Death ◽  
Disease Resistance ◽  
Stem Rust ◽  
Nuclear Export ◽  
Rust Resistance ◽  
Stem Rust Resistance ◽  
Full Length ◽  
Induce Cell Death ◽  
Immune Receptors ◽  
Cell Death Signaling

Plants possess intracellular immune receptors designated “nucleotide-binding domain and leucine-rich repeat” (NLR) proteins that translate pathogen-specific recognition into disease-resistance signaling. The wheat immune receptors Sr33 and Sr50 belong to the class of coiled-coil (CC) NLRs. They confer resistance against a broad spectrum of field isolates of Puccinia graminis f. sp. tritici, including the Ug99 lineage, and are homologs of the barley powdery mildew-resistance protein MLA10. Here, we show that, similarly to MLA10, the Sr33 and Sr50 CC domains are sufficient to induce cell death in Nicotiana benthamiana. Autoactive CC domains and full-length Sr33 and Sr50 proteins self-associate in planta. In contrast, truncated CC domains equivalent in size to an MLA10 fragment for which a crystal structure was previously determined fail to induce cell death and do not self-associate. Mutations in the truncated region also abolish self-association and cell-death signaling. Analysis of Sr33 and Sr50 CC domains fused to YFP and either nuclear localization or nuclear export signals in N. benthamiana showed that cell-death induction occurs in the cytosol. In stable transgenic wheat plants, full-length Sr33 proteins targeted to the cytosol provided rust resistance, whereas nuclear-targeted Sr33 was not functional. These data are consistent with CC-mediated induction of both cell-death signaling and stem rust resistance in the cytosolic compartment, whereas previous research had suggested that MLA10-mediated cell-death and disease resistance signaling occur independently, in the cytosol and nucleus, respectively.

scholarly journals Cross Kingdom Immunity: The Role of Immune Receptors and Downstream Signaling in Animal and Plant Cell Death

2021 ◽  
Vol 11 ◽  
Author(s):  
Thibault Roudaire ◽  
Marie-Claire Héloir ◽  
David Wendehenne ◽  
Aymeric Zadoroznyj ◽  
Laurence Dubrez ◽  
...  
Keyword(s):  
Cell Death ◽  
Plant Immunity ◽  
Crop Protection ◽  
Nucleotide Binding ◽  
Lectin Receptors ◽  
Surface Receptors ◽  
Immune Receptors ◽  
Regulated Cell Death ◽  
Cell Death Signaling ◽  
Molecular Patterns

Both plants and animals are endowed with sophisticated innate immune systems to combat microbial attack. In these multicellular eukaryotes, innate immunity implies the presence of cell surface receptors and intracellular receptors able to detect danger signal referred as damage-associated molecular patterns (DAMPs) and pathogen-associated molecular patterns (PAMPs). Membrane-associated pattern recognition receptors (PRRs), such as Toll-like receptors (TLRs), C-type lectin receptors (CLRs), receptor-like kinases (RLKs), and receptor-like proteins (RLPs) are employed by these organisms for sensing different invasion patterns before triggering antimicrobial defenses that can be associated with a form of regulated cell death. Intracellularly, animals nucleotide-binding and oligomerization domain (NOD)-like receptors or plants nucleotide-binding domain (NBD)-containing leucine rich repeats (NLRs) immune receptors likely detect effectors injected into the host cell by the pathogen to hijack the immune signaling cascade. Interestingly, during the co-evolution between the hosts and their invaders, key cross-kingdom cell death-signaling macromolecular NLR-complexes have been selected, such as the inflammasome in mammals and the recently discovered resistosome in plants. In both cases, a regulated cell death located at the site of infection constitutes a very effective mean for blocking the pathogen spread and protecting the whole organism from invasion. This review aims to describe the immune mechanisms in animals and plants, mainly focusing on cell death signaling pathways, in order to highlight recent advances that could be used on one side or the other to identify the missing signaling elements between the perception of the invasion pattern by immune receptors, the induction of defenses or the transmission of danger signals to other cells. Although knowledge of plant immunity is less advanced, these organisms have certain advantages allowing easier identification of signaling events, regulators and executors of cell death, which could then be exploited directly for crop protection purposes or by analogy for medical research.

scholarly journals Multiple functional self-association interfaces in plant TIR domains

2017 ◽  
Vol 114 (10) ◽  
pp. E2046-E2052 ◽  
Author(s):  
Xiaoxiao Zhang ◽  
Maud Bernoux ◽  
Adam R. Bentham ◽  
Toby E. Newman ◽  
Thomas Ve ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Cell Death ◽  
Interleukin 1 ◽  
Tir Domain ◽  
Disease Resistance Protein ◽  
Resistance Protein ◽  
Cell Death Signaling ◽  
Self Association ◽  
Tir Domains ◽  
Diverse Plant

The self-association of Toll/interleukin-1 receptor/resistance protein (TIR) domains has been implicated in signaling in plant and animal immunity receptors. Structure-based studies identified different TIR-domain dimerization interfaces required for signaling of the plant nucleotide-binding oligomerization domain-like receptors (NLRs) L6 from flax and disease resistance protein RPS4 fromArabidopsis. Here we show that the crystal structure of the TIR domain from theArabidopsisNLR suppressor of npr1-1, constitutive 1 (SNC1) contains both an L6-like interface involving helices αD and αE (DE interface) and an RPS4-like interface involving helices αA and αE (AE interface). Mutations in either the AE- or DE-interface region disrupt cell-death signaling activity of SNC1, L6, and RPS4 TIR domains and full-length L6 and RPS4. Self-association of L6 and RPS4 TIR domains is affected by mutations in either region, whereas only AE-interface mutations affect SNC1 TIR-domain self-association. We further show two similar interfaces in the crystal structure of the TIR domain from theArabidopsisNLR recognition ofPeronospora parasitica1 (RPP1). These data demonstrate that both the AE and DE self-association interfaces are simultaneously required for self-association and cell-death signaling in diverse plant NLRs.

scholarly journals TIR domains of plant immune receptors are 2',3'-cAMP/cGMP synthetases mediating cell death

2021 ◽  
Author(s):  
Dongli Yu ◽  
Wen Song ◽  
Eddie Yong Jun Tan ◽  
Li Liu ◽  
Yu Cao ◽  
...  
Keyword(s):  
Cell Death ◽  
Immune Responses ◽  
Interleukin 1 ◽  
Structural Data ◽  
Negative Regulator ◽  
Synthetase Activity ◽  
Leucine Rich Repeat ◽  
Tir Domain ◽  
Immune Receptors ◽  
Tir Domains

2′,3′-cAMP is a positional isomer of the well-established second messenger 3′,5′-cAMP, but little is known on the biology of this noncanonical cyclic nucleotide monophosphate (cNMP). Toll/interleukin-1 receptor (TIR) domains of nucleotide-binding leucine-rich repeat (NLR) immune receptors have NADase function necessary but insufficient to activate plant immune responses. Here we show that plant TIR proteins, besides being NADases, act as 2′,3′-cAMP/cGMP synthetases by hydrolyzing RNA/DNA. Structural data shows that a TIR domain adopts distinct oligomers with dual and exclusive enzymatic activity. Mutations specifically disrupting the synthetase activity abrogate TIR-mediated cell death in Nicotiana benthamiana, supporting an important role for these cNMPs in TIR signaling. Furthermore, the Arabidopsis negative regulator of TIR-NLR signaling, NUDT7 displays 2′,3′-cAMP/cGMP but not 3′,5′-cAMP/cGMP phosphodiesterase activity and suppresses cell death activity of TIRs in N. benthamiana. Our study identifies a novel family of 2′,3′-cAMP/cGMP synthetase and establishes a role for the noncanonical cNMPs in plant immune responses.

scholarly journals Cell Death Related Proteins Beyond Apoptosis in the CNS

2022 ◽  
Vol 9 ◽  
Author(s):  
Bazhena Bahatyrevich-Kharitonik ◽  
Rafael Medina-Guzman ◽  
Alicia Flores-Cortes ◽  
Marta García-Cruzado ◽  
Edel Kavanagh ◽  
...  
Keyword(s):  
Cell Death ◽  
Protein Function ◽  
Apoptotic Cell ◽  
Apoptotic Cell Death ◽  
Original Function ◽  
New Concepts ◽  
Cytoskeleton Reorganization ◽  
Caspase Substrates ◽  
Cell Death Signaling ◽  
Related Proteins

Cell death related (CDR) proteins are a diverse group of proteins whose original function was ascribed to apoptotic cell death signaling. Recently, descriptions of non-apoptotic functions for CDR proteins have increased. In this minireview, we comment on recent studies of CDR proteins outside the field of apoptosis in the CNS, encompassing areas such as the inflammasome and non-apoptotic cell death, cytoskeleton reorganization, synaptic plasticity, mitophagy, neurodegeneration and calcium signaling among others. Furthermore, we discuss the evolution of proteomic techniques used to predict caspase substrates that could potentially explain their non-apoptotic roles. Finally, we address new concepts in the field of non-apoptotic functions of CDR proteins that require further research such the effect of sexual dimorphism on non-apoptotic CDR protein function and the emergence of zymogen-specific caspase functions.

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