Abstract: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. 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 a… Show more
“…TIR-dependent NADase activity leads to production of the small signaling molecule(s) initiating the activation of ADR1s by the EDS1-PAD4 heterodimer and initiation of full PRR-triggered responses. The fact that chemical inhibition of TNL enzymatic activity leads to a reduction of some PRR-mediated immune outputs is supporting this hypothesis [ 30 ].…”
Section: Eds1-pad4-adr1s Form a Convergence Hub For Prr- And Nlr-medi...mentioning
“…TIR-dependent NADase activity leads to production of the small signaling molecule(s) initiating the activation of ADR1s by the EDS1-PAD4 heterodimer and initiation of full PRR-triggered responses. The fact that chemical inhibition of TNL enzymatic activity leads to a reduction of some PRR-mediated immune outputs is supporting this hypothesis [ 30 ].…”
Section: Eds1-pad4-adr1s Form a Convergence Hub For Prr- And Nlr-medi...mentioning
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