2024
DOI: 10.1016/j.isci.2024.108817
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Plant Toll/interleukin-1 receptor/resistance protein domains physically associate with enhanced disease susceptibility1 family proteins in immune signaling

Jian Chen,
Xiaoxiao Zhang,
Maud Bernoux
et al.
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Cited by 4 publications
(1 citation statement)
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“…Structural analysis of EDS1/PAD4 and EDS1-SAG101 heterodimers after TIR-NLR signaling activation showed that they each detect different small molecules produced by TIR enzymatic activity: 2ʹ-(5ʹʹ-phosphoribosyl)-5ʹ-adenosine mono- or di-phosphate (pRib-AMP/ADP) in the case of EDS1/PAD4 and ADP-ribosylated ATP or ADP-ribosylated ADP ribose (ADPr-ATP/di-ADPR) for EDS1/SAG101 ( Huang et al 2022 ; Jia et al 2022 ). Direct interaction of TIR domains with EDS1 complexes may facilitate efficient transfer of these short half-life metabolites ( Chen et al 2024 ). Binding of these TIR-derived molecules allosterically promotes interaction of EDS1/PAD4 and EDS1/SAG101 heterodimers with ADR1 or NRG1, respectively ( Sun et al 2021 ; Huang et al 2022 ; Jia et al 2022 ).…”
Section: The Eds1 Pathway Connects Tir-nlrs To Cc-nlr Outputsmentioning
confidence: 99%
“…Structural analysis of EDS1/PAD4 and EDS1-SAG101 heterodimers after TIR-NLR signaling activation showed that they each detect different small molecules produced by TIR enzymatic activity: 2ʹ-(5ʹʹ-phosphoribosyl)-5ʹ-adenosine mono- or di-phosphate (pRib-AMP/ADP) in the case of EDS1/PAD4 and ADP-ribosylated ATP or ADP-ribosylated ADP ribose (ADPr-ATP/di-ADPR) for EDS1/SAG101 ( Huang et al 2022 ; Jia et al 2022 ). Direct interaction of TIR domains with EDS1 complexes may facilitate efficient transfer of these short half-life metabolites ( Chen et al 2024 ). Binding of these TIR-derived molecules allosterically promotes interaction of EDS1/PAD4 and EDS1/SAG101 heterodimers with ADR1 or NRG1, respectively ( Sun et al 2021 ; Huang et al 2022 ; Jia et al 2022 ).…”
Section: The Eds1 Pathway Connects Tir-nlrs To Cc-nlr Outputsmentioning
confidence: 99%