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 | UNDECIDED | Summary: Sequence-model (AtSubP) prediction of chloroplast localization for EDS1. Reason: Sequence-model (AtSubP) chloroplast prediction for a well-characterized nucleocytoplasmic protein with no transit peptide; UniProt lists nucleus, cytoplasm and microsome from experimental data. On its own this prediction would be removed, but the same chloroplast claim also carries a TAIR IDA row (PMID:33751092) whose figures we cannot see, and that row is UNDECIDED. Rows sharing a term take one action, so this row is also UNDECIDED until someone with the full text settles whether EDS1 has a chloroplast pool (ARATH organelle audit tie-break, projects/ARATH/organelle-audit.md). |
| GO:0009507 chloroplast | IDA PMID:33751092 EDS1-interacting J protein 1 is an essential negative regula... | UNDECIDED | Summary: Chloroplast location for EDS1 curated from the EIJ1 study, in which EIJ1 is the chloroplast protein and EDS1 is described as nucleocytoplasmic. Reason: TAIR curated nucleus, cytoplasm and chloroplast from this paper. The cached text (which lacks the results section) shows chloroplast localization of EIJ1, which is released to the cytoplasm on infection and binds EDS1 there, and describes EDS1 as nucleocytoplasmic; it does not show a chloroplast pool of EDS1, but the curator saw the figures and we cannot. Without the relevant figures we can neither confirm nor reject the claim, so the row is UNDECIDED rather than removed or marked as over-annotated; the sibling ISM chloroplast row takes the same action. |
| 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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