EDS1 is an Arabidopsis EDS1-family lipase-like immune signaling hub required for TIR-NLR-dependent effector-triggered immunity and basal resistance. It forms distinct nucleocytoplasmic complexes with PAD4 or SAG101; current mechanistic work supports a ligand-responsive pseudoenzymatic adaptor/scaffold role that connects TIR-derived nucleotide signals to ADR1- or NRG1-family helper NLR outputs, salicylic-acid-associated defense amplification, and hypersensitive-response signaling. Direct lipase or lipid metabolic activity is not established.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0000304 response to singlet oxygen | IGI PMID:16790029 The role of EDS1 (enhanced disease susceptibility) during si... | KEEP AS NON CORE | Summary: EDS1 contributes to singlet-oxygen/redox stress signaling in Arabidopsis. Reason: This redox-stress phenotype is experimentally supported, but it is a contextual stress output of the EDS1 immune-redox node rather than the core molecular role. |
| GO:0001666 response to hypoxia | IMP PMID:18055613 Lysigenous aerenchyma formation in Arabidopsis is controlled... | KEEP AS NON CORE | Summary: EDS1 is genetically implicated in hypoxia-associated lysigenous aerenchyma and ROS regulation. Reason: This hypoxia/aerenchyma output is supported in the cited stress-developmental context, but it is downstream of EDS1/PAD4 immune-redox signaling rather than a core conserved EDS1 activity. |
| GO:0009626 plant-type hypersensitive response | IMP PMID:17997306 Nuclear accumulation of the Arabidopsis immune receptor RPS4... | ACCEPT | Summary: EDS1 is required for TIR-NLR-associated hypersensitive-response and cell-death outputs. Reason: Hypersensitive response is a major experimentally supported output of EDS1-dependent TIR-NLR immune signaling, especially through the EDS1-SAG101/NRG1 branch. |
| GO:0009627 systemic acquired resistance | IEP PMID:17419843 Pathogen-associated molecular pattern recognition rather tha... | ACCEPT | Summary: EDS1 promotes salicylic-acid-associated systemic acquired resistance and defense amplification. Reason: EDS1 acts upstream of SA accumulation/signaling and is necessary for systemic and basal defense reinforcement. |
| GO:0010310 regulation of hydrogen peroxide metabolic process | IMP PMID:18055613 Lysigenous aerenchyma formation in Arabidopsis is controlled... | KEEP AS NON CORE | Summary: EDS1 is genetically implicated in hypoxia-associated lysigenous aerenchyma and ROS regulation. Reason: This hypoxia/aerenchyma output is supported in the cited stress-developmental context, but it is downstream of EDS1/PAD4 immune-redox signaling rather than a core conserved EDS1 activity. |
| GO:0010618 aerenchyma formation | IMP PMID:18055613 Lysigenous aerenchyma formation in Arabidopsis is controlled... | KEEP AS NON CORE | Summary: EDS1 is genetically implicated in hypoxia-associated lysigenous aerenchyma and ROS regulation. Reason: This hypoxia/aerenchyma output is supported in the cited stress-developmental context, but it is downstream of EDS1/PAD4 immune-redox signaling rather than a core conserved EDS1 activity. |
| GO:0050829 defense response to Gram-negative bacterium | IMP PMID:29253890 Leaf shedding as an anti-bacterial defense in Arabidopsis ca... | ACCEPT | Summary: EDS1 contributes to defense against Gram-negative bacterial pathogens, including Pseudomonas defense contexts. Reason: Antibacterial defense is a central biological-process output of EDS1-dependent immune signaling. Supporting Evidence: PMID:29253890 eds1, sid2, pad4 sag101, and NahG transgenic plants all fail to abscise normally after infection with DC3000 |
| GO:0060866 leaf abscission | IMP PMID:29253890 Leaf shedding as an anti-bacterial defense in Arabidopsis ca... | KEEP AS NON CORE | Summary: EDS1 is required for pathogen-triggered cauline leaf abscission in the cited bacterial defense context. Reason: The leaf-abscission phenotype is a tissue-level antibacterial defense output mediated by SA/immune signaling, not a direct molecular role of EDS1. Supporting Evidence: PMID:29253890 pad4, eds1, and pad4 sag101 (SENESCENCE-ASSOCIATED GENE 101) mutants also had quantitatively impaired abscission |
| GO:0005515 protein binding | IPI PMID:11574472 Direct interaction between the Arabidopsis disease resistanc... | MARK AS OVER ANNOTATED | Summary: EDS1 physically associates with PAD4, SAG101, NLR/effectors, and other immune regulators, but generic protein binding does not describe the functional mechanism. Reason: The more informative curation is EDS1 disease-resistance complex membership and ligand-responsive signaling adaptor activity; protein binding alone is too generic for a core annotation. |
| GO:0005515 protein binding | IPI PMID:16040633 Arabidopsis SENESCENCE-ASSOCIATED GENE101 stabilizes and sig... | MARK AS OVER ANNOTATED | Summary: EDS1 physically associates with PAD4, SAG101, NLR/effectors, and other immune regulators, but generic protein binding does not describe the functional mechanism. Reason: The more informative curation is EDS1 disease-resistance complex membership and ligand-responsive signaling adaptor activity; protein binding alone is too generic for a core annotation. |
| GO:0005515 protein binding | IPI PMID:16040633 Arabidopsis SENESCENCE-ASSOCIATED GENE101 stabilizes and sig... | MARK AS OVER ANNOTATED | Summary: EDS1 physically associates with PAD4, SAG101, NLR/effectors, and other immune regulators, but generic protein binding does not describe the functional mechanism. Reason: The more informative curation is EDS1 disease-resistance complex membership and ligand-responsive signaling adaptor activity; protein binding alone is too generic for a core annotation. |
| GO:0005515 protein binding | IPI PMID:21434927 Different roles of Enhanced Disease Susceptibility1 (EDS1) b... | MARK AS OVER ANNOTATED | Summary: EDS1 physically associates with PAD4, SAG101, NLR/effectors, and other immune regulators, but generic protein binding does not describe the functional mechanism. Reason: The more informative curation is EDS1 disease-resistance complex membership and ligand-responsive signaling adaptor activity; protein binding alone is too generic for a core annotation. |
| GO:0005515 protein binding | IPI PMID:21434927 Different roles of Enhanced Disease Susceptibility1 (EDS1) b... | MARK AS OVER ANNOTATED | Summary: EDS1 physically associates with PAD4, SAG101, NLR/effectors, and other immune regulators, but generic protein binding does not describe the functional mechanism. Reason: The more informative curation is EDS1 disease-resistance complex membership and ligand-responsive signaling adaptor activity; protein binding alone is too generic for a core annotation. |
| GO:0005515 protein binding | IPI PMID:23275581 Natural variation in small molecule-induced TIR-NB-LRR signa... | MARK AS OVER ANNOTATED | Summary: EDS1 physically associates with PAD4, SAG101, NLR/effectors, and other immune regulators, but generic protein binding does not describe the functional mechanism. Reason: The more informative curation is EDS1 disease-resistance complex membership and ligand-responsive signaling adaptor activity; protein binding alone is too generic for a core annotation. |
| GO:0005515 protein binding | IPI PMID:28555890 The dual role of LESION SIMULATING DISEASE 1 as a condition-... | MARK AS OVER ANNOTATED | Summary: EDS1 physically associates with PAD4, SAG101, NLR/effectors, and other immune regulators, but generic protein binding does not describe the functional mechanism. Reason: The more informative curation is EDS1 disease-resistance complex membership and ligand-responsive signaling adaptor activity; protein binding alone is too generic for a core annotation. |
| GO:0005515 protein binding | IPI PMID:32612234 Extensive signal integration by the phytohormone protein net... | MARK AS OVER ANNOTATED | Summary: EDS1 physically associates with PAD4, SAG101, NLR/effectors, and other immune regulators, but generic protein binding does not describe the functional mechanism. Reason: The more informative curation is EDS1 disease-resistance complex membership and ligand-responsive signaling adaptor activity; protein binding alone is too generic for a core annotation. |
| GO:0005515 protein binding | IPI PMID:32612234 Extensive signal integration by the phytohormone protein net... | MARK AS OVER ANNOTATED | Summary: EDS1 physically associates with PAD4, SAG101, NLR/effectors, and other immune regulators, but generic protein binding does not describe the functional mechanism. Reason: The more informative curation is EDS1 disease-resistance complex membership and ligand-responsive signaling adaptor activity; protein binding alone is too generic for a core annotation. |
| GO:0005515 protein binding | IPI PMID:32612234 Extensive signal integration by the phytohormone protein net... | MARK AS OVER ANNOTATED | Summary: EDS1 physically associates with PAD4, SAG101, NLR/effectors, and other immune regulators, but generic protein binding does not describe the functional mechanism. Reason: The more informative curation is EDS1 disease-resistance complex membership and ligand-responsive signaling adaptor activity; protein binding alone is too generic for a core annotation. |
| GO:0005515 protein binding | IPI PMID:32612234 Extensive signal integration by the phytohormone protein net... | MARK AS OVER ANNOTATED | Summary: EDS1 physically associates with PAD4, SAG101, NLR/effectors, and other immune regulators, but generic protein binding does not describe the functional mechanism. Reason: The more informative curation is EDS1 disease-resistance complex membership and ligand-responsive signaling adaptor activity; protein binding alone is too generic for a core annotation. |
| GO:0005515 protein binding | IPI PMID:32612234 Extensive signal integration by the phytohormone protein net... | MARK AS OVER ANNOTATED | Summary: EDS1 physically associates with PAD4, SAG101, NLR/effectors, and other immune regulators, but generic protein binding does not describe the functional mechanism. Reason: The more informative curation is EDS1 disease-resistance complex membership and ligand-responsive signaling adaptor activity; protein binding alone is too generic for a core annotation. |
| GO:0005515 protein binding | IPI PMID:32612234 Extensive signal integration by the phytohormone protein net... | MARK AS OVER ANNOTATED | Summary: EDS1 physically associates with PAD4, SAG101, NLR/effectors, and other immune regulators, but generic protein binding does not describe the functional mechanism. Reason: The more informative curation is EDS1 disease-resistance complex membership and ligand-responsive signaling adaptor activity; protein binding alone is too generic for a core annotation. |
| GO:0016298 lipase activity | ISS PMID:10077677 EDS1, an essential component of R gene-mediated disease resi... | REMOVE | Summary: EDS1 is lipase-like by sequence/domain architecture, but no direct EDS1 lipase activity or physiological lipid substrate is established. Reason: The original lipase annotation was a sequence-based prediction; subsequent structural and functional evidence favors pseudoenzymatic immune signaling rather than a demonstrated hydrolase reaction. |
| GO:0042803 protein homodimerization activity | IDA PMID:11574472 Direct interaction between the Arabidopsis disease resistanc... | KEEP AS NON CORE | Summary: EDS1 homodimerization has been observed, particularly for cytosolic EDS1 pools. Reason: Self-association is experimentally supported but the best-supported functional immune modules are EDS1-PAD4 and EDS1-SAG101 complexes, so homodimerization should not be treated as the core function. |
| GO:0042803 protein homodimerization activity | IDA PMID:21434927 Different roles of Enhanced Disease Susceptibility1 (EDS1) b... | KEEP AS NON CORE | Summary: EDS1 homodimerization has been observed, particularly for cytosolic EDS1 pools. Reason: Self-association is experimentally supported but the best-supported functional immune modules are EDS1-PAD4 and EDS1-SAG101 complexes, so homodimerization should not be treated as the core function. |
| GO:0006629 lipid metabolic process | IEA GO_REF:0000002 | REMOVE | Summary: The InterPro lipid metabolic process transfer follows from the lipase-like fold but is not supported by EDS1 biology. Reason: EDS1 is an immune signaling pseudoenzyme/scaffold; no direct lipid metabolic process or lipid substrate is established. |
| GO:0006952 defense response | IEA GO_REF:0000002 | MARK AS OVER ANNOTATED | Summary: EDS1 is a central defense signaling protein, but the generic InterPro defense-response transfer is less informative than the specific TIR-NLR, SAR, and antibacterial defense annotations. Reason: The broad defense response term blurs the specific EDS1 immune signaling role captured by more precise experimental annotations. |
| GO:0009626 plant-type hypersensitive response | IMP PMID:16040633 Arabidopsis SENESCENCE-ASSOCIATED GENE101 stabilizes and sig... | ACCEPT | Summary: EDS1 is required for TIR-NLR-associated hypersensitive-response and cell-death outputs. Reason: Hypersensitive response is a major experimentally supported output of EDS1-dependent TIR-NLR immune signaling, especially through the EDS1-SAG101/NRG1 branch. Supporting Evidence: PMID:16040633 EDS1 is necessary for RESISTANCE ( R ) gene–triggered programmed cell death |
| GO:0009626 plant-type hypersensitive response | NAS PMID:16040633 Arabidopsis SENESCENCE-ASSOCIATED GENE101 stabilizes and sig... | ACCEPT | Summary: EDS1 is required for TIR-NLR-associated hypersensitive-response and cell-death outputs. Reason: Hypersensitive response is a major experimentally supported output of EDS1-dependent TIR-NLR immune signaling, especially through the EDS1-SAG101/NRG1 branch. Supporting Evidence: PMID:16040633 EDS1 is necessary for RESISTANCE ( R ) gene–triggered programmed cell death |
| GO:0009626 plant-type hypersensitive response | IMP PMID:19616764 Regulation of cell death and innate immunity by two receptor... | ACCEPT | Summary: EDS1 is required for TIR-NLR-associated hypersensitive-response and cell-death outputs. Reason: Hypersensitive response is a major experimentally supported output of EDS1-dependent TIR-NLR immune signaling, especially through the EDS1-SAG101/NRG1 branch. |
| GO:0009626 plant-type hypersensitive response | NAS PMID:22072959 SAG101 forms a ternary complex with EDS1 and PAD4 and is req... | ACCEPT | Summary: EDS1 is required for TIR-NLR-associated hypersensitive-response and cell-death outputs. Reason: Hypersensitive response is a major experimentally supported output of EDS1-dependent TIR-NLR immune signaling, especially through the EDS1-SAG101/NRG1 branch. Supporting Evidence: PMID:22072959 the combined activities of EDS1 and PAD4 proteins are required for HR formation and the restriction of pathogen growth |
| GO:0009862 systemic acquired resistance, salicylic acid mediated signaling pathway | IMP PMID:11574472 Direct interaction between the Arabidopsis disease resistanc... | ACCEPT | Summary: EDS1 promotes salicylic-acid-associated systemic acquired resistance and defense amplification. Reason: EDS1 acts upstream of SA accumulation/signaling and is necessary for systemic and basal defense reinforcement. Supporting Evidence: PMID:11574472 EDS1 and PAD4 are both required for accumulation of the plant defence-potentiating molecule, salicylic acid |
| GO:0009862 systemic acquired resistance, salicylic acid mediated signaling pathway | IMP PMID:16040633 Arabidopsis SENESCENCE-ASSOCIATED GENE101 stabilizes and sig... | ACCEPT | Summary: EDS1 promotes salicylic-acid-associated systemic acquired resistance and defense amplification. Reason: EDS1 acts upstream of SA accumulation/signaling and is necessary for systemic and basal defense reinforcement. Supporting Evidence: PMID:16040633 Arabidopsis EDS1 constitutes a central regulatory node in innate immunity, controlling the accumulation of salicylic acid and other defense molecules to drive basal resistance |
| GO:0009862 systemic acquired resistance, salicylic acid mediated signaling pathway | NAS PMID:22072959 SAG101 forms a ternary complex with EDS1 and PAD4 and is req... | ACCEPT | Summary: EDS1 promotes salicylic-acid-associated systemic acquired resistance and defense amplification. Reason: EDS1 acts upstream of SA accumulation/signaling and is necessary for systemic and basal defense reinforcement. Supporting Evidence: PMID:22072959 Besides EDS1 and SA, HRT-mediated resistance also requires PAD4 and EDS5 |
| GO:0005634 nucleus | IEA GO_REF:0000044 | ACCEPT | Summary: EDS1 functions in the nucleus as part of immune transcriptional reprogramming and EDS1-containing complexes. Reason: Nuclear EDS1 localization is experimentally supported and functionally important for basal and TIR-NLR-conditioned immunity. |
| GO:0005634 nucleus | IDA PMID:16040633 Arabidopsis SENESCENCE-ASSOCIATED GENE101 stabilizes and sig... | ACCEPT | Summary: EDS1 functions in the nucleus as part of immune transcriptional reprogramming and EDS1-containing complexes. Reason: Nuclear EDS1 localization is experimentally supported and functionally important for basal and TIR-NLR-conditioned immunity. Supporting Evidence: PMID:16040633 EDS1 and PAD4 localized to the cytosol and nucleus, whereas SAG101 was detected only in the nuclear compartment |
| GO:0005634 nucleus | IDA PMID:22072959 SAG101 forms a ternary complex with EDS1 and PAD4 and is req... | ACCEPT | Summary: EDS1 functions in the nucleus as part of immune transcriptional reprogramming and EDS1-containing complexes. Reason: Nuclear EDS1 localization is experimentally supported and functionally important for basal and TIR-NLR-conditioned immunity. Supporting Evidence: PMID:22072959 EDS1 and PAD4 are present in the nucleus and cytoplasm, whereas SAG101 preferentially localizes to the nucleus |
| GO:0005634 nucleus | NAS PMID:22072959 SAG101 forms a ternary complex with EDS1 and PAD4 and is req... | ACCEPT | Summary: EDS1 functions in the nucleus as part of immune transcriptional reprogramming and EDS1-containing complexes. Reason: Nuclear EDS1 localization is experimentally supported and functionally important for basal and TIR-NLR-conditioned immunity. Supporting Evidence: PMID:22072959 EDS1 and PAD4 are present in the nucleus and cytoplasm, whereas SAG101 preferentially localizes to the nucleus |
| GO:0005634 nucleus | EXP PMID:22158819 Pathogen effectors target Arabidopsis EDS1 and alter its int... | ACCEPT | Summary: EDS1 functions in the nucleus as part of immune transcriptional reprogramming and EDS1-containing complexes. Reason: Nuclear EDS1 localization is experimentally supported and functionally important for basal and TIR-NLR-conditioned immunity. |
| GO:0005634 nucleus | IDA PMID:33751092 EDS1-interacting J protein 1 is an essential negative regula... | ACCEPT | Summary: EDS1 functions in the nucleus as part of immune transcriptional reprogramming and EDS1-containing complexes. Reason: Nuclear EDS1 localization is experimentally supported and functionally important for basal and TIR-NLR-conditioned immunity. Supporting Evidence: PMID:33751092 allowing the nuclear accumulation of EDS1 for transcriptional resistance reinforcement |
| GO:0005737 cytoplasm | IEA GO_REF:0000044 | ACCEPT | Summary: EDS1 occupies cytoplasmic/cytosolic pools as part of nucleocytoplasmic immune signal relay. Reason: Cytoplasmic EDS1 is experimentally supported and contributes to complete EDS1-dependent immune outputs. |
| GO:0005737 cytoplasm | IDA PMID:16040633 Arabidopsis SENESCENCE-ASSOCIATED GENE101 stabilizes and sig... | ACCEPT | Summary: EDS1 occupies cytoplasmic/cytosolic pools as part of nucleocytoplasmic immune signal relay. Reason: Cytoplasmic EDS1 is experimentally supported and contributes to complete EDS1-dependent immune outputs. Supporting Evidence: PMID:16040633 EDS1 and PAD4 localized to the cytosol and nucleus, whereas SAG101 was detected only in the nuclear compartment |
| GO:0005737 cytoplasm | IDA PMID:22072959 SAG101 forms a ternary complex with EDS1 and PAD4 and is req... | ACCEPT | Summary: EDS1 occupies cytoplasmic/cytosolic pools as part of nucleocytoplasmic immune signal relay. Reason: Cytoplasmic EDS1 is experimentally supported and contributes to complete EDS1-dependent immune outputs. Supporting Evidence: PMID:22072959 EDS1 and PAD4 are present in the nucleus and cytoplasm, whereas SAG101 preferentially localizes to the nucleus |
| GO:0005737 cytoplasm | EXP PMID:22158818 Arabidopsis EDS1 connects pathogen effector recognition to c... | ACCEPT | Summary: EDS1 occupies cytoplasmic/cytosolic pools as part of nucleocytoplasmic immune signal relay. Reason: Cytoplasmic EDS1 is experimentally supported and contributes to complete EDS1-dependent immune outputs. |
| GO:0005737 cytoplasm | EXP PMID:22158819 Pathogen effectors target Arabidopsis EDS1 and alter its int... | ACCEPT | Summary: EDS1 occupies cytoplasmic/cytosolic pools as part of nucleocytoplasmic immune signal relay. Reason: Cytoplasmic EDS1 is experimentally supported and contributes to complete EDS1-dependent immune outputs. |
| GO:0005737 cytoplasm | IDA PMID:33751092 EDS1-interacting J protein 1 is an essential negative regula... | ACCEPT | Summary: EDS1 occupies cytoplasmic/cytosolic pools as part of nucleocytoplasmic immune signal relay. Reason: Cytoplasmic EDS1 is experimentally supported and contributes to complete EDS1-dependent immune outputs. Supporting Evidence: PMID:33751092 it interacted with EDS1, thereby restricting pathogen-triggered trafficking of EDS1 to the nucleus |
| GO:0005829 cytosol | IDA PMID:16040633 Arabidopsis SENESCENCE-ASSOCIATED GENE101 stabilizes and sig... | ACCEPT | Summary: EDS1 occupies cytoplasmic/cytosolic pools as part of nucleocytoplasmic immune signal relay. Reason: Cytoplasmic EDS1 is experimentally supported and contributes to complete EDS1-dependent immune outputs. Supporting Evidence: PMID:16040633 EDS1 and PAD4 localized to the cytosol and nucleus, whereas SAG101 was detected only in the nuclear compartment |
| GO:0009507 chloroplast | ISM GO_REF:0000122 | REMOVE | Summary: The cited EIJ1 study supports chloroplast localization of EIJ1 and cytoplasmic/nuclear regulation of EDS1, not a stable chloroplast pool of EDS1. Reason: Current UniProt and literature synthesis support nucleocytoplasmic EDS1; the chloroplast annotation appears to over-transfer the EIJ1 localization context to EDS1. |
| GO:0009507 chloroplast | IDA PMID:33751092 EDS1-interacting J protein 1 is an essential negative regula... | REMOVE | Summary: The cited EIJ1 study supports chloroplast localization of EIJ1 and cytoplasmic/nuclear regulation of EDS1, not a stable chloroplast pool of EDS1. Reason: Current UniProt and literature synthesis support nucleocytoplasmic EDS1; the chloroplast annotation appears to over-transfer the EIJ1 localization context to EDS1. |
| GO:0106093 EDS1 disease-resistance complex | IDA PMID:11574472 Direct interaction between the Arabidopsis disease resistanc... | ACCEPT | Summary: EDS1 is a component of EDS1 disease-resistance complexes with PAD4 and SAG101. Reason: EDS1-PAD4 and EDS1-SAG101 complex membership is central to EDS1 immune signaling and is directly supported by interaction and localization studies. Supporting Evidence: PMID:11574472 Co-immunoprecipitation experiments show that EDS1 and PAD4 proteins interact in healthy and pathogen-challenged plant cells |
| GO:0106093 EDS1 disease-resistance complex | IDA PMID:16040633 Arabidopsis SENESCENCE-ASSOCIATED GENE101 stabilizes and sig... | ACCEPT | Summary: EDS1 is a component of EDS1 disease-resistance complexes with PAD4 and SAG101. Reason: EDS1-PAD4 and EDS1-SAG101 complex membership is central to EDS1 immune signaling and is directly supported by interaction and localization studies. Supporting Evidence: PMID:16040633 an EDS1–SAG101 complex inside the nucleus that is molecularly and spatially distinct from EDS1–PAD4 associations in the nucleus and cytoplasm |
| GO:0106093 EDS1 disease-resistance complex | NAS PMID:22072959 SAG101 forms a ternary complex with EDS1 and PAD4 and is req... | ACCEPT | Summary: EDS1 is a component of EDS1 disease-resistance complexes with PAD4 and SAG101. Reason: EDS1-PAD4 and EDS1-SAG101 complex membership is central to EDS1 immune signaling and is directly supported by interaction and localization studies. Supporting Evidence: PMID:22072959 SAG101 forms a ternary complex with EDS1 and PAD4 and is required for resistance signaling against turnip crinkle virus |
| GO:0035591 signaling adaptor activity | IC file:ARATH/EDS1/EDS1-deep-research-falcon.md | NEW | Summary: EDS1 functions as a ligand-responsive immune signaling adaptor/pseudoenzyme rather than as a demonstrated lipase. Reason: Existing GOA rows capture EDS1 complex membership and defense outputs but not the current mechanistic molecular role of EDS1 heterodimers as ligand-responsive immune adaptor hubs. Supporting Evidence: file:ARATH/EDS1/EDS1-deep-research-falcon.md ligand-responsive immune signaling adaptor/pseudoenzyme that forms **EDS1–PAD4** and **EDS1–SAG101** heterodimers PMID:11574472 EDS1 and PAD4 proteins interact in healthy and pathogen-challenged plant cells. PMID:16040633 Dynamic interactions of EDS1 and its signaling partners in multiple cell compartments are important for plant defense signal relay. PMID:22072959 Co-IP of EDS1-90-MYC and PAD4-MYC with EDS1-80-FLAG. |
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Download this section (compressed HTML)Q: Should GO add a more specific EDS1-family immune adaptor activity term for ligand-responsive TIR-NLR signal relay to helper NLRs?
Q: Should chloroplast localization annotations for EDS1 be reviewed to separate EDS1 from the chloroplast-localized EIJ1 regulatory context?
Experiment: Reconstitute Arabidopsis EDS1-PAD4-ADR1 and EDS1-SAG101-NRG1 modules with defined TIR-derived nucleotide ligands to quantify EDS1-dependent helper-NLR recruitment and activation.
Experiment: Test purified EDS1 and EDS1-family complexes against candidate ester/lipid substrates alongside catalytic-site mutants to determine whether any physiologically relevant hydrolase activity exists.
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