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From Proteopedia
EDS1-PAD4 complexed with pRib-ADP
Structural highlights
FunctionEDS1C_ARATH Positive regulator of basal resistance and of effector-triggered immunity specifically mediated by TIR-NB-LRR (TNL) resistance proteins. Disruption by bacterial effector of EDS1-TIR-NB-LRR resistance protein interactions constitutes the first step in resistance activation (PubMed:22158819). Acts redundantly with salicylic acid to regulate resistance gene-mediated signaling (PubMed:19578402). Triggers early plant defenses and hypersensitive response independently of PAD4, and then recruits PAD4 to potentiate plant defenses through the accumulation of salicylic acid (PubMed:11574472). Nuclear localization is essential for basal and TNL-conditioned immunity and for reprogramming defense gene expression, while cytoplasmic EDS1 is required to induce a complete immune response (PubMed:20617163). Heterodimerization with PAD4 and/or SGA101 is necessary for TNL-mediated effector-triggered immunity (PubMed:24331460). Contributes to nonhost resistance against E.amylovora (PubMed:22316300). Loss of EDS1-PAD4 interaction compromises basal but not TNL-triggered resistance (PubMed:21434927). Necessary for systemic acquired resistance (SAR) signal generation and perception (PubMed:24755512). Has no direct lipase activity (PubMed:16040633). Putative lipase activity is dispensable for immune functions (PubMed:24331460).[1] [2] [3] [4] [5] [6] [7] [8] [9] Publication Abstract from PubMedPlant nucleotide-binding leucine-rich repeat-containing (NLR) receptors with an N-terminal Toll/interleukin-1 receptor (TIR) domain sense pathogen effectors to enable TIR-encoded nicotinamide adenine dinucleotide hydrolase (NADase) activity for immune signaling. TIR-NLR signaling requires the helper NLRs N requirement gene 1 (NRG1), Activated Disease Resistance 1 (ADR1), and Enhanced Disease Susceptibility 1 (EDS1), which forms a heterodimer with each of its paralogs Phytoalexin Deficient 4 (PAD4) and Senescence-Associated Gene 101 (SAG101). Here, we show that TIR-containing proteins catalyze the production of 2'-(5-phosphoribosyl)-5'-adenosine monophosphate (pRib-AMP) and diphosphate (pRib-ADP) in vitro and in planta. Biochemical and structural data demonstrate that EDS1-PAD4 is a receptor complex for pRib-AMP and pRib-ADP, which allosterically promote EDS1-PAD4 interaction with ADR1-L1 but not NRG1A. Our study identifies TIR-catalyzed pRib-AMP and pRib-ADP as a missing link in TIR signaling through EDS1-PAD4 and as likely second messengers for plant immunity. Identification and receptor mechanism of TIR-catalyzed small molecules in plant immunity.,Huang S, Jia A, Song W, Hessler G, Meng Y, Sun Y, Xu L, Laessle H, Jirschitzka J, Ma S, Xiao Y, Yu D, Hou J, Liu R, Sun H, Liu X, Han Z, Chang J, Parker JE, Chai J Science. 2022 Jul 29;377(6605):eabq3297. doi: 10.1126/science.abq3297. Epub 2022 , Jul 29. PMID:35857645[10] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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