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Broader functions of TIR domains in Arabidopsis immunity

ABSTRACT: Broader functions of TIR domains in Arabidopsis immunity

PROVIDER: PRJNA933663 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR23406900_1.fastq.gz	Fastqsanger.gz
	SRR23406900_2.fastq.gz	Fastqsanger.gz
	SRR23406901_1.fastq.gz	Fastqsanger.gz
	SRR23406901_2.fastq.gz	Fastqsanger.gz
	SRR23406902_1.fastq.gz	Fastqsanger.gz

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Broader functions of TIR domains in Arabidopsis immunity [DV]

Project description:Broader functions of TIR domains in Arabidopsis immunity [DV]

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Broader functions of TIR domains in Arabidopsis immunity [NAM]

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Broader functions of TIR domains in Arabidopsis immunity [NAM]

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Broader functions of TIR domains in Arabidopsis immunity.

Project description:TIR domains are NAD-degrading enzymes that function during immune signaling in prokaryotes, plants, and animals. In plants, most TIR domains are incorporated into intracellular immune receptors termed TNLs. In Arabidopsis, TIR-derived small molecules bind and activate EDS1 heterodimers, which in turn activate RNLs, a class of cation channel-forming immune receptors. RNL activation drives cytoplasmic Ca2+ influx, transcriptional reprogramming, pathogen resistance, and host cell death. We screened for mutants that suppress an RNL activation mimic allele and identified a TNL, SADR1. Despite being required for the function of an autoactivated RNL, SADR1 is not required for defense signaling triggered by other tested TNLs. SADR1 is required for defense signaling initiated by some transmembrane pattern recognition receptors and contributes to the unbridled spread of cell death in lesion simulating disease 1. Together with RNLs, SADR1 regulates defense gene expression at infection site borders, likely in a non-cell autonomous manner. RNL mutants that cannot sustain this pattern of gene expression are unable to prevent disease spread beyond localized infection sites, suggesting that this pattern corresponds to a pathogen containment mechanism. SADR1 potentiates RNL-driven immune signaling not only through the activation of EDS1 but also partially independently of EDS1. We studied EDS1-independent TIR function using nicotinamide, an NADase inhibitor. Nicotinamide decreased defense induction from transmembrane pattern recognition receptors and decreased calcium influx, pathogen growth restriction, and host cell death following intracellular immune receptor activation. We demonstrate that TIR domains can potentiate calcium influx and defense and are thus broadly required for Arabidopsis immunity.

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Broader functions of TIR domains in Arabidopsis immunity

Project description:This SuperSeries is composed of the SubSeries listed below.

2023-04-21 | GSE225075 | GEO

Broader functions of TIR domains in Arabidopsis immunity [DV]

Project description:Characterization of ADR1-L2 D484V suppressor mutants

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Lysosomal integrity suppresses TIR-1/SARM1 aggregation to restrain toxic propagation of p38 innate immunity

Project description:Innate immunity in bacteria, plants and animals requires the specialized subset of TIR-domain proteins that are NAD+ hydrolases. Aggregation of these TIR proteins engages their enzymatic activity, but it is not known how this protein multimerization is regulated. Here, we discovered that TIR oligomerization is exquisitely controlled to prevent immune toxicity. We found that p38 propagates its own activation by promoting the feedforward expression and aggregation of the lone enzymatic TIR protein in the nematode C. elegans, TIR-1/SARM1. We performed a forward genetic screen to determine how the p38 positive feedforward loop is regulated. We discovered that the integrity of the specific lysosomal sub-compartment that expresses TIR-1/SARM1 is actively maintained to limit inappropriate aggregation of this protein and restrain toxic p38 immune activation. Thus, innate immune defenses in intestinal epithelial cells are regulated by specific control of TIR-1/SARM1 multimerization.

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CPK3 phosphorylates SNC1-TIR LC-MSMS

Project description:Toll/interleukin-1 receptor (TIR) domain proteins are immune signaling components and function as NAD+-cleaving enzymes to activate defense responses. Activation of TIRs represses growth and drives cell death in plants and promotes axon degeneration in animals, but how plant TIRs are repressed remains unclear. Here, we show that TIR NADase activity requires a conserved serine residue spatially close to the catalytic glutamate. The plant Ca2+-dependent protein kinases (CPKs), the mammalian Ca2+/calmodulin-dependent protein kinase II delta (CAMK2D) and TANK binding kinase 1 (TBK1) phosphorylate TIR domains at this conserved serine, which blocks TIR NADase activities and functions and thus maintains growth in plants and suppresses SARM1 TIR signaling in animals, respectively. Our findings define a fundamental molecular mechanism by which phosphorylation at a conserved serine residue blocks TIR signaling to balance growth and defense trade-offs.

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Interrogating the functions of PRDM9 domains in meiosis

Project description:Interrogating the functions of PRDM9 domains in meiosis

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