EDS1

Existing Annotations Review

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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.

Core Functions

Ligand-responsive EDS1 immune signaling adaptor. EDS1 forms EDS1-PAD4 and EDS1-SAG101 immune complexes that translate TIR-NLR-derived nucleotide signals into helper-NLR-dependent salicylic-acid defense amplification, antibacterial defense, and hypersensitive-response outputs.

Molecular Function:

signaling adaptor activity

Directly Involved In:

systemic acquired resistance, salicylic acid mediated signaling pathway plant-type hypersensitive response

Cellular Locations:

nucleus cytoplasm

Supporting Evidence:

file:ARATH/EDS1/EDS1-deep-research-falcon.md
ligand-responsive immune signaling adaptor/pseudoenzyme that forms **EDS1–PAD4** and **EDS1–SAG101** heterodimers
file:ARATH/EDS1/EDS1-deep-research-falcon.md
EDS1 heterodimers act as ligand-responsive hubs
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.

References

GO_REF:0000002

Gene Ontology annotation through association of InterPro records with GO terms

GO_REF:0000044

Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt

GO_REF:0000122

AtSubP analysis

PMID:10077677

EDS1, an essential component of R gene-mediated disease resistance in Arabidopsis has homology to eukaryotic lipases.

EDS1 was cloned as a lipase-like gene required upstream of salicylic-acid-dependent PR1 expression and TIR-NLR-associated resistance.

PMID:11574472

Direct interaction between the Arabidopsis disease resistance signaling proteins, EDS1 and PAD4.

EDS1 interacts with PAD4, can homodimerize, acts early in defense, and recruits PAD4 for salicylic-acid-associated defense amplification.

PMID:16040633

Arabidopsis SENESCENCE-ASSOCIATED GENE101 stabilizes and signals within an ENHANCED DISEASE SUSCEPTIBILITY1 complex in plant innate immunity.

EDS1 forms molecularly and spatially distinct EDS1-SAG101 and EDS1-PAD4 complexes in nucleus and cytoplasm, and direct lipase activity was not demonstrated.

PMID:16790029

The role of EDS1 (enhanced disease susceptibility) during singlet oxygen-mediated stress responses of Arabidopsis.

EDS1 contributes to singlet oxygen-mediated stress responses.

PMID:17419843

Pathogen-associated molecular pattern recognition rather than development of tissue necrosis contributes to bacterial induction of systemic acquired resistance in Arabidopsis.

PMID:17997306

Nuclear accumulation of the Arabidopsis immune receptor RPS4 is necessary for triggering EDS1-dependent defense.

PMID:18055613

Lysigenous aerenchyma formation in Arabidopsis is controlled by LESION SIMULATING DISEASE1.

EDS1, PAD4, and LSD1 regulate hypoxia-associated aerenchyma formation and ROS-linked stress outputs.

PMID:19616764

Regulation of cell death and innate immunity by two receptor-like kinases in Arabidopsis.

PMID:21434927

Different roles of Enhanced Disease Susceptibility1 (EDS1) bound to and dissociated from Phytoalexin Deficient4 (PAD4) in Arabidopsis immunity.

Distinct EDS1 pools bound to PAD4 or SAG101 support basal resistance, salicylic-acid defense mobilization, and TIR-NLR immune signaling.

PMID:22072959

SAG101 forms a ternary complex with EDS1 and PAD4 and is required for resistance signaling against turnip crinkle virus.

EDS1 isoforms interact with PAD4 and SAG101 and can organize binary or ternary EDS1-family complexes with compartment-dependent localization.

PMID:22158818

Arabidopsis EDS1 connects pathogen effector recognition to cell compartment-specific immune responses.

EDS1 connects pathogen effector recognition to compartment-specific immune responses.

PMID:22158819

Pathogen effectors target Arabidopsis EDS1 and alter its interactions with immune regulators.

Pathogen effectors can target EDS1 and alter EDS1 interactions with immune regulators.

PMID:23275581

Natural variation in small molecule-induced TIR-NB-LRR signaling induces root growth arrest via EDS1- and PAD4-complexed R protein VICTR in Arabidopsis.

PMID:28555890

The dual role of LESION SIMULATING DISEASE 1 as a condition-dependent scaffold protein and transcription regulator.

PMID:29253890

Leaf shedding as an anti-bacterial defense in Arabidopsis cauline leaves.

EDS1 and other SA-defense components are required for pathogen-triggered cauline leaf abscission.

PMID:32612234

Extensive signal integration by the phytohormone protein network.

PMID:33751092

EDS1-interacting J protein 1 is an essential negative regulator of plant innate immunity in Arabidopsis.

EIJ1 regulates EDS1 nucleocytoplasmic distribution by interacting with EDS1 in the cytoplasm and limiting EDS1 nuclear trafficking.

file:ARATH/EDS1/EDS1-deep-research-falcon.md

Falcon deep research for Arabidopsis EDS1

EDS1 is a nucleocytoplasmic immune regulator that forms PAD4 or SAG101 complexes and functions as a ligand-responsive adaptor/pseudoenzyme in TIR-NLR signaling.
Current evidence supports EDS1 immune signal transduction via regulated complex formation rather than direct lipase/hydrolase activity.

file:ARATH/EDS1/EDS1-uniprot.txt

UniProt record for Arabidopsis EDS1

UniProt identifies EDS1/Q9SU72 as enhanced disease susceptibility 1 with nuclear, cytoplasmic, cytosolic, and EDS1 disease-resistance complex annotations.

file:interpro/panther/PTHR47090/PTHR47090-entries.csv

PANTHER PTHR47090 protein EDS1-related family entries

PTHR47090 places Arabidopsis Q9SU72/EDS1 in the protein EDS1-related family.

Suggested Experiments

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.

Deep Research

Falcon

(EDS1-deep-research-falcon.md)

this with annotations you find in gene/protein databases, but these can be outdated or inaccurate. Falcon Edison Scientific Literature 40 citations 2026-05-07T02:11:05.196768

The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.

You should prioritize authoritative reviews and primary scientific literature when conducting research. You can supplement
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.

We are specifically interested in the primary function of the gene - for enzymes, what reaction is catalyzed, and what is the substrate specificity? For transporters, what is the substrate? For structural proteins or adapters, what is the broader structural role? For signaling molecules, what is the role in the pathway.

We are interested in where in or outside the cell the gene product carries out its function.

We are also interested in the signaling or biochemical pathways in which the gene functions. We are less interested in broad pleiotropic effects, except where these elucidate the precise role.

Include evidence where possible. We are interested in both experimental evidence as well as inference from structure, evolution, or bioinformatic analysis. Precise studies should be prioritized over high-throughput, where available.

Research report: Arabidopsis thaliana ENHANCED DISEASE SUSCEPTIBILITY 1 (EDS1)

Target verification (mandatory disambiguation)

The target in this report is Arabidopsis thaliana EDS1 (ENHANCED DISEASE SUSCEPTIBILITY 1), a nucleocytoplasmic immune regulator that forms mutually exclusive complexes with PAD4 or SAG101 and is essential for TIR-NLR (TNL) immune signaling in Arabidopsis. This identity is consistent with canonical EDS1 literature descriptions and domain architecture (N-terminal lipase-like α/β-hydrolase fold + C-terminal EP domain). (wiermer2005plantimmunitythe pages 1-2, lapin2020originsandimmunity pages 1-2, wagner2013structuralbasisfor pages 1-2)

1) Key concepts and definitions (current understanding)

1.1 EDS1 as a central immune “node”

EDS1 is widely regarded as a central regulatory hub (“node”) in plant innate immunity that is genetically required for multiple TNL (TIR-domain NLR) receptor–mediated responses, and that integrates upstream receptor activation to downstream defense outputs. (wiermer2005plantimmunitythe pages 1-2, lapin2020originsandimmunity pages 1-2, wagner2013structuralbasisfor pages 1-2)

A unifying contemporary model is that EDS1 functions in two parallel, heterodimer-based signaling modules:
- EDS1–PAD4 → ADR1 helper NLRs: promotes defense signaling (including transcriptional reprogramming and salicylic-acid-associated responses). (yu2024activationofa pages 1-2, dangl2024acommonimmune pages 1-2, lapin2020originsandimmunity pages 11-12)
- EDS1–SAG101 → NRG1 helper NLRs: preferentially drives strong hypersensitive response (HR)–type cell death outputs in TNL immunity. (yu2024activationofa pages 1-2, dangl2024acommonimmune pages 1-2, lapin2020originsandimmunity pages 11-12)

This “branching” concept (EDS1–PAD4–ADR1 vs EDS1–SAG101–NRG1) is described in authoritative reviews and is reinforced by 2024 structural and mechanistic work. (lapin2020originsandimmunity pages 11-12, yu2024activationofa pages 1-2, dangl2024acommonimmune pages 1-2)

1.2 Domain architecture: lipase-like + EP domain

EDS1 belongs to a small plant-specific protein family with EDS1, PAD4, and SAG101. They share a characteristic architecture: an N-terminal lipase-like α/β-hydrolase fold domain and a C-terminal EP domain (all-helical). (lapin2020originsandimmunity pages 1-2, zonnchen2021differentialrequirementfor pages 1-3)

Crystal structures established that EDS1 heterodimers juxtapose these N-terminal lipase-like domains with their EP domains to create conserved signaling surfaces. (wagner2013structuralbasisfor pages 1-2, wagner2013structuralbasisfor pages 3-4)

1.3 Upstream receptor class: TIR-NLR (TNL) and TIR NADase activity

TNL receptors contain N-terminal TIR domains with enzymatic activity (NADase) that generates nucleotide-derived small molecules. These products serve as chemical messengers coupling receptor activation to EDS1-containing signaling assemblies. (lapin2020originsandimmunity pages 9-11, yu2024activationofa pages 1-2)

2) Recent developments and latest research (prioritizing 2023–2024)

2.1 2024 mechanistic breakthrough: ligand-activated EDS1–PAD4–ADR1 (EPA) heterotrimer

A major 2024 advance is the cryo-EM and functional characterization of an activated Arabidopsis EDS1–PAD4–ADR1 heterotrimer, termed EPA, bound to a ribosylated ligand (pRib-ADP). (yu2024activationofa pages 1-2, yu2024activationofa pages 2-4)

Key findings include:
- Direct small-molecule binding: the activated EPA complex was captured in complex with pRib-ADP, placing small-molecule recognition at the heart of EDS1 activation. (yu2024activationofa pages 2-4)
- Conformational activation: ligand binding induces an ~18° rotation of the PAD4 EP domain that opens an interaction cleft between EDS1 and PAD4, enabling helper NLR (ADR1) engagement. (yu2024activationofa pages 2-4)
- Quantified interaction surfaces: two main interaction interfaces (I-1, I-2) between EPA and ADR1 were defined with buried surface areas ~585.3 Å² and ~593 Å², respectively, and interface mutations reduce complex pull-down and effector-triggered cell death. (yu2024activationofa pages 2-4)
- Conserved ADR1 motif: a conserved ADR1 C-terminal motif (“FTVDWLDD”) contributes to one of the key docking interfaces and is functionally important for signaling. (yu2024activationofa pages 2-4)

Figure evidence from this work provides a visual summary of the EPA architecture and ligand binding site. (yu2024activationofa media ac32e15e, yu2024activationofa media a516d854, yu2024activationofa media b0c04168)

2.2 2024 expert synthesis: a conserved angiosperm immune response node

A 2024 Science Perspective emphasizes that EDS1 heterodimers act as ligand-responsive hubs that recruit different helper NLRs (ADR1 vs NRG1), and that helper NLRs can oligomerize into membrane-localized calcium channels that execute immune responses. (dangl2024acommonimmune pages 1-2)

2.3 2024 evidence for physical coupling of TIR domains to EDS1-family proteins

A 2024 study reports physical association of plant TIR domains with EDS1-family proteins (EDS1, PAD4, SAG101), supporting a model in which activated TIR signaling complexes could deliver or locally generate low-abundance ligands for EDS1 activation. (chen2024planttollinterleukin1receptorresistance pages 1-3)

3) Primary function of EDS1: enzyme vs signaling adaptor

3.1 EDS1 is lipase-like but not a proven hydrolase in immunity

Despite a canonical α/β-hydrolase fold and a conserved Ser-Asp-His “catalytic triad” (e.g., S123-D187-H317 in Arabidopsis EDS1), multiple lines of evidence indicate EDS1 is not acting as a classical lipase/hydrolase in immune signaling:
- No detectable hydrolase activity was reported for EDS1 in vitro in a foundational structural study. (wagner2013structuralbasisfor pages 9-10)
- Structural features in the EDS1–SAG101 complex include shielding/occlusion and disruption of oxyanion-hole geometry consistent with noncanonical or inactive hydrolase chemistry. (wagner2013structuralbasisfor pages 3-4)
- Genetic complementation data show that mutating predicted catalytic residues generally does not abrogate Arabidopsis EDS1 immune function, arguing against an essential catalytic reaction mechanism in Arabidopsis immunity. (wagner2013structuralbasisfor pages 3-4, zonnchen2021differentialrequirementfor pages 6-8)

Collectively, EDS1 is best described as a lipase-fold pseudoenzyme/scaffold whose primary function is immune signal transduction via regulated complex formation and ligand-driven conformational switching. (wagner2013structuralbasisfor pages 9-10, dangl2024acommonimmune pages 1-2, yu2024activationofa pages 2-4)

3.2 Catalytic triad: lineage/context dependence

Comparative mutagenesis suggests that catalytic-triad residues can be important in some heterologous Solanaceae contexts, but Arabidopsis EDS1–PAD4 signaling can be largely triad-independent in reported assays, highlighting species- and context-dependent constraints rather than universal enzymatic function. (zonnchen2021differentialrequirementfor pages 22-23, zonnchen2022eds1complexesare pages 10-10, zonnchen2021differentialrequirementfor pages 6-8)

3.3 What is the “substrate”?

For Arabidopsis EDS1, the most strongly supported “substrate-like” relationship is binding of nucleotide-derived small molecules (e.g., pRib-ADP/AMP and related TIR-NADase products) rather than hydrolysis of lipid/ester substrates. (yu2024activationofa pages 2-4, yu2024activationofa pages 1-2)

4) Pathways and mechanism: from TIR NADase to helper NLR execution

4.1 Signaling flow

Current evidence supports the following pathway logic:
1. Effector recognition by TNLs activates TIR enzymatic activity (NADase), generating nucleotide-derived products (including pRib-AMP/ADP and related metabolites). (yu2024activationofa pages 1-2)
2. These products (or processed derivatives) bind EDS1 heterodimer assemblies, inducing conformational changes that enable helper-NLR recruitment/activation. (dangl2024acommonimmune pages 1-2, yu2024activationofa pages 2-4)
3. EDS1–PAD4 preferentially recruits ADR1, forming ligand-activated EPA complexes; EDS1–SAG101 preferentially recruits NRG1 for cell-death–associated outputs. (dangl2024acommonimmune pages 1-2, yu2024activationofa pages 1-2)

A key mechanistic detail is the proposal that 2′cADPR may be a storage form that can be hydrolyzed to pRib-AMP, an active EPA ligand. (yu2024activationofa pages 1-2, yu2024activationofa pages 2-4)

4.2 Relationship to PTI/ETI and system differences

EDS1 family proteins are described as central for ETI and, in Arabidopsis, as contributing to broader immune signaling beyond TNL ETI (including reinforcement of defenses triggered by diverse receptors), though requirements can vary across species (e.g., N. benthamiana). (lapin2020originsandimmunity pages 1-2, zonnchen2022eds1complexesare pages 10-10)

5) Subcellular localization and where EDS1 functions

5.1 Nucleocytoplasmic localization

EDS1 is nucleocytoplasmic, and both EDS1–PAD4 and EDS1–SAG101 complexes can occupy nucleus and cytoplasm. (wagner2013structuralbasisfor pages 1-2, neubauer2020arabidopsisedr1protein pages 1-2)

5.2 Nuclear EDS1 is strongly linked to transcriptional defense outputs

Evidence supports that the nucleus is a principal site for EDS1–PAD4–dependent transcriptional defense reprogramming, and that nuclear EDS1 accumulation is functionally important for defense gene regulation in Arabidopsis immunity. (lapin2020originsandimmunity pages 11-12, wagner2013structuralbasisfor pages 1-2)

5.3 Cytoplasmic pools and cell-death outputs

Review-level synthesis suggests a cytoplasmic EDS1 pool contributes to TNL-triggered cell death, in parallel with nuclear functions. (lapin2020originsandimmunity pages 11-12)

Experimental mislocalization studies in a reconstituted Solanaceae system further support the importance of nuclear pools for ETI-associated outputs: forcing EDS1–SAG101 toward membranes or cytoplasm reduces cell death, while nuclear targeting can restore activity. (zonnchen2022eds1complexesare pages 9-9)

6) Applications and real-world implementations

6.1 Crop engineering implications: the EDS1 node as a compatibility requirement

Because EDS1 heterodimers connect TIR-derived small molecules to helper-NLR execution, the EDS1 node is a key consideration for transferring immune pathways between species; expert analysis highlights the node’s conservation and centrality across flowering plants. (dangl2024acommonimmune pages 1-2)

6.2 Actionable genetic levers around the EDS1 node

Mechanistic literature highlights several intervention points:
- Negative regulation by EDR1: EDR1 can associate with EDS1 and PAD4 and inhibit their association, implying that manipulating this regulator can alter the EDS1 node’s output. (neubauer2020arabidopsisedr1protein pages 1-2)
- Hyperactive defense via PAD4 S135F: single-residue changes in this node can strongly potentiate immunity (illustrating engineering potential but also risk of overactivation). (lapin2020originsandimmunity pages 8-9)

6.3 Reported translational examples (beyond Arabidopsis)

A structural synthesis compiling published examples notes that EDR1 knockout in wheat can increase powdery mildew resistance, and that modulating EDS1 expression influences grapevine powdery mildew resistance, indicating the EDS1 neighborhood is already being engaged in applied contexts via genetic manipulation. (voss2022crucialstepson pages 12-16)

7) Statistics and data highlights (from recent studies)

Ligand-activated EPA structure: PAD4 EP domain rotation ~18° upon ligand binding. (yu2024activationofa pages 2-4)
ADR1 docking interfaces: ~585.3 Å² (I-1) and ~593 Å² (I-2) buried surface areas; interface mutations reduce pull-down and cell death outputs. (yu2024activationofa pages 2-4)
Foundational biochemistry: no EDS1 hydrolase activity detected in vitro in a key structural paper. (wagner2013structuralbasisfor pages 9-10)

Evidence summary table

The following table consolidates key claims, evidence types, and bibliographic details (including URLs/DOIs and dates), emphasizing 2024 advances while anchoring them to foundational work.

Topic	Key claim	Evidence type	Main source	Year & publication date	URL/DOI	Notes/statistics
Identity / target verification	Arabidopsis thaliana EDS1 is the canonical ENHANCED DISEASE SUSCEPTIBILITY 1 immune regulator corresponding to locus At3g48090 and carrying an N-terminal lipase-like α/β-hydrolase domain plus a C-terminal EP domain.	Review + foundational primary; genetics/structure/domain analysis	Lapin, Annual Review of Phytopathology; Wagner, Cell Host & Microbe	2020 (Aug 2020); 2013 (Dec 2013)	https://doi.org/10.1146/annurev-phyto-010820-012840; https://doi.org/10.1016/j.chom.2013.11.006	Domain architecture aligns with UniProt Q9SU72 annotations; At3g48090 explicitly matches the Arabidopsis EDS1 locus in the literature-derived evidence set. (lapin2020originsandimmunity pages 1-2, wagner2013structuralbasisfor pages 1-2, panahi2026genomewideidentificationand pages 7-9)
EDS1-centered immune modules	EDS1 is a central hub in two Arabidopsis signaling modules: EDS1-PAD4 pairs with ADR1 helpers, whereas EDS1-SAG101 pairs with NRG1 helpers.	2024 primary + commentary; structure/function	Yu, Science; Dangl & Jones, Science	2024 (Dec 2024)	https://doi.org/10.1126/science.adr3150; https://doi.org/10.1126/science.adu4930	Defines parallel outputs: EDS1-PAD4-ADR1 (EPA) for defense signaling and EDS1-SAG101-NRG1 for strong cell-death outputs. (yu2024activationofa pages 1-2, dangl2024acommonimmune pages 1-2)
Small-molecule ligands downstream of TIR NADase	Effector-activated TIR domains generate nucleotide-derived messengers that directly engage EDS1 complexes. pRib-AMP/ADP activates the Arabidopsis EDS1-PAD4-ADR1 complex; related TIR products also activate EDS1-SAG101-NRG1.	2024 primary; cryo-EM/biochemistry/functional genetics	Yu, Science	2024 (Dec 2024)	https://doi.org/10.1126/science.adr3150	Ligands discussed include pRib-AMP, pRib-ADP, 2'cADPR, ADPr-ATP, and di-ADPR; 2'cADPR can be hydrolyzed to pRib-AMP, proposed as an active signaling form. (yu2024activationofa pages 2-4, yu2024activationofa pages 1-2)
EPA complex activation mechanism	In the pRib-ADP-bound EPA structure, ligand binding remodels EDS1-PAD4 to permit ADR1 docking and activation.	2024 primary; cryo-EM structure + mutagenesis	Yu, Science	2024 (Dec 2024)	https://doi.org/10.1126/science.adr3150	PAD4 EP domain rotates by ~18°; ADR1 interface I-1 buried surface ~585.3 Å^2; interface I-2 ~593 Å^2; ADR1 C-terminal motif “FTVDWLDD” is required; interface mutations reduce pull-down and effector-triggered cell death. (yu2024activationofa pages 2-4, yu2024activationofa media ac32e15e)
TIR-EDS1 physical coupling	TIR domains can physically associate with EDS1-family proteins, supporting direct handoff or local generation of low-abundance ligands for EDS1 activation.	2024 primary; interaction biology	Chen, iScience	2024 (Feb 2024)	https://doi.org/10.1016/j.isci.2024.108817	Supports a model in which activated TIRs contact EDS1, PAD4, and SAG101; consistent with ligand-mediated triggering of downstream EDS1 complexes but does not itself identify the final bound ligand in Arabidopsis. (chen2024planttollinterleukin1receptorresistance pages 1-3)
Foundational structural model	EDS1 forms mutually exclusive heterodimers with PAD4 or SAG101, and these complexes present signaling surfaces needed for immunity rather than acting like classical enzymes.	Foundational primary; crystal structure/genetics	Wagner, Cell Host & Microbe	2013 (Dec 2013)	https://doi.org/10.1016/j.chom.2013.11.006	Crystal structure of AtEDS1-AtSAG101 established juxtaposed N-terminal α/β-hydrolase-like and C-terminal EP domains; provided the early structural basis for exclusive heterodimer signaling. (wagner2013structuralbasisfor pages 1-2, wagner2013structuralbasisfor pages 9-10, wagner2013structuralbasisfor pages 3-4)
Enzymatic activity / pseudoenzyme question	Arabidopsis EDS1 is lipase-like but there is no convincing evidence that it acts as an active hydrolase in immunity; instead it behaves primarily as a signaling/scaffolding protein.	Primary + review; structure/biochemistry/genetics	Wagner, Cell Host & Microbe; Lapin, Annual Review of Phytopathology	2013 (Dec 2013); 2020 (Aug 2020)	https://doi.org/10.1016/j.chom.2013.11.006; https://doi.org/10.1146/annurev-phyto-010820-012840	No EDS1 hydrolase activity detected; catalytic triad S123-D187-H317 is conserved, but the oxyanion-hole region is disrupted/occluded; triad mutations in Arabidopsis generally do not abolish immune function. (wagner2013structuralbasisfor pages 9-10, wagner2013structuralbasisfor pages 3-4, zonnchen2021differentialrequirementfor pages 6-8)
Catalytic triad interpretation	Catalytic residues can matter in some Solanaceae assays, but Arabidopsis EDS1-PAD4 immune signaling does not require an intact catalytic triad in reported assays.	Comparative primary; mutagenesis/functional assays	Zönnchen, bioRxiv; Zönnchen, New Phytologist	2021 (Dec 2021); 2022 (Oct 2022)	https://doi.org/10.1101/2021.12.15.472806; https://doi.org/10.1111/nph.18511	Supports species/context dependence rather than a universal catalytic mechanism; strengthens the view that AtEDS1 is not a classical enzyme with a defined substrate. (zonnchen2021differentialrequirementfor pages 6-8, zonnchen2021differentialrequirementfor pages 22-23, zonnchen2022eds1complexesare pages 10-10)
Localization and functional compartmentation	EDS1 is nucleocytoplasmic; nuclear EDS1-PAD4 is closely tied to transcriptional defense and salicylic-acid-linked immunity, while cytoplasmic/nucleocytoplasmic EDS1-SAG101-NRG1 contributes to cell-death signaling.	Review + primary; localization/genetics	Lapin, Annual Review of Phytopathology; Neubauer, MPMI	2020 (Aug 2020); 2020 (Apr 2020)	https://doi.org/10.1146/annurev-phyto-010820-012840; https://doi.org/10.1094/mpmi-12-19-0339-r	Nuclear-targeted EDS1 can support transcriptional reprogramming; EDS1-PAD4 is linked to SA accumulation and defense-gene mobilization; EDS1-SAG101 is linked to HR-type cell death. (lapin2020originsandimmunity pages 11-12, neubauer2020arabidopsisedr1protein pages 1-2, wagner2013structuralbasisfor pages 1-2)
Experimental localization requirement	For TNL-triggered cell death in N. benthamiana, forcing EDS1-SAG101 into the nucleus preserves function, whereas driving it out of the nucleus or tethering it to membranes reduces activity.	Primary; localization engineering/cell-death assays	Zönnchen, New Phytologist	2022 (Oct 2022)	https://doi.org/10.1111/nph.18511	NES or myristoylation reduced XopQ/Roq1 cell death; NLS restored WT-like activity; supports the importance of nuclear EDS1 signaling and is consistent with Arabidopsis nuclear-function models. (zonnchen2022eds1complexesare pages 9-9, zonnchen2022eds1complexesare pages 11-11)
Broader immune outputs	EDS1-PAD4-ADR1 reinforces ROS-promoted defense transcription, salicylic acid accumulation, systemic immunity, and repression of jasmonate signaling, whereas EDS1-SAG101-NRG1 is more specialized for strong hypersensitive cell death.	Review	Lapin, Annual Review of Phytopathology	2020 (Aug 2020)	https://doi.org/10.1146/annurev-phyto-010820-012840	Useful functional distinction for annotation: EDS1’s primary role is immune signal transduction rather than metabolism. (lapin2020originsandimmunity pages 11-12, lapin2020originsandimmunity pages 9-11, lapin2020originsandimmunity pages 12-14)
Current applications / translation	The EDS1 node is being used conceptually for crop engineering: receptor transfer and pathway engineering must account for compatibility with downstream EDS1-PAD4-ADR1 or EDS1-SAG101-NRG1 modules.	Recent review/thesis-style engineering overview + authoritative commentary	Dangl & Jones, Science; Song, engineering review	2024 (Dec 2024); 2024 (Sep 2024)	https://doi.org/10.1126/science.adu4930; https://doi.org/10.15496/publikation-99005	Practical implication: moving a TIR receptor alone may fail unless the recipient species has a compatible EDS1-helper NLR node; this is especially relevant across dicot/monocot boundaries and for pathway reconstitution. (dangl2024acommonimmune pages 1-2, lapin2020originsandimmunity pages 8-9)
Engineering opportunities and limitations	Manipulating regulators of the EDS1 node can enhance resistance, but overactivation risks growth-defense penalties and autoimmune phenotypes.	Review / mechanistic synthesis	Lapin, Annual Review of Phytopathology; Voß, structural synthesis	2020 (Aug 2020); 2022	https://doi.org/10.1146/annurev-phyto-010820-012840	Examples include PAD4 S135F gain-of-function and loss of the negative regulator EDR1 increasing resistance; these illustrate translational potential but also the need for dosage/control. (lapin2020originsandimmunity pages 8-9, voss2022crucialstepson pages 12-16)

Table: This table summarizes the most relevant evidence for Arabidopsis thaliana EDS1 (UniProt Q9SU72 / At3g48090), emphasizing 2024 mechanistic advances while anchoring them to foundational structural and review literature. It highlights identity, signaling modules, ligand activation, localization, enzymatic interpretation, and translational relevance.

Concluding functional annotation (for ARATH EDS1 / UniProt Q9SU72)

Primary molecular function: ligand-responsive immune signaling adaptor/pseudoenzyme that forms EDS1–PAD4 and EDS1–SAG101 heterodimers; upon binding of TIR-NADase-derived nucleotide ligands (e.g., pRib-ADP/AMP), EDS1 heterodimers recruit/activate helper NLRs (ADR1 or NRG1) to execute immune outputs. (yu2024activationofa pages 1-2, yu2024activationofa pages 2-4, dangl2024acommonimmune pages 1-2)

Enzymatic activity: no validated lipase/hydrolase catalytic reaction or substrate specificity for Arabidopsis EDS1; catalytic-triad residues are largely dispensable for Arabidopsis immune function in multiple assays, consistent with pseudoenzymatic signaling roles. (wagner2013structuralbasisfor pages 9-10, wagner2013structuralbasisfor pages 3-4, zonnchen2021differentialrequirementfor pages 6-8)

Cellular location of function: nucleocytoplasmic; nuclear pools are strongly associated with transcriptional defense reprogramming and SA-linked immunity, while cytoplasmic/nucleocytoplasmic pools contribute to ETI-associated outputs including cell death, depending on module and species context. (lapin2020originsandimmunity pages 11-12, wagner2013structuralbasisfor pages 1-2, zonnchen2022eds1complexesare pages 9-9)

References

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(neubauer2020arabidopsisedr1protein pages 1-2): Matthew Neubauer, Irene Serrano, Natalie Rodibaugh, Deepak D. Bhandari, Jaqueline Bautor, Jane E. Parker, and Roger W. Innes. arabidopsis edr1 protein kinase regulates the association of eds1 and pad4 to inhibit cell death. Molecular Plant-Microbe Interactions®, 33:693-703, Apr 2020. URL: https://doi.org/10.1094/mpmi-12-19-0339-r, doi:10.1094/mpmi-12-19-0339-r. This article has 36 citations.
(zonnchen2022eds1complexesare pages 9-9): Josua Zönnchen, Johannes Gantner, Dmitry Lapin, Karen Barthel, Lennart Eschen‐Lippold, Jessica L. Erickson, Sergio Landeo Villanueva, Stefan Zantop, Carola Kretschmer, Matthieu H. A. J. Joosten, Jane E. Parker, Raphael Guerois, and Johannes Stuttmann. eds1 complexes are not required for prr responses and execute tnl‐eti from the nucleus in nicotiana benthamiana. New Phytologist, 236:2249-2264, Oct 2022. URL: https://doi.org/10.1111/nph.18511, doi:10.1111/nph.18511. This article has 38 citations and is from a highest quality peer-reviewed journal.
(lapin2020originsandimmunity pages 8-9): Dmitry Lapin, Deepak D. Bhandari, and Jane E. Parker. Origins and immunity networking functions of eds1 family proteins. Annual Review of Phytopathology, 58:253-276, Aug 2020. URL: https://doi.org/10.1146/annurev-phyto-010820-012840, doi:10.1146/annurev-phyto-010820-012840. This article has 198 citations and is from a domain leading peer-reviewed journal.
(voss2022crucialstepson pages 12-16): M Voß. Crucial steps on the way to a comprehensive structural understanding of the plant proteins eds1 and pad4 and their role in innate immunity. Unknown journal, 2022.
(panahi2026genomewideidentificationand pages 7-9): Bahman Panahi, Rasmieh Hamid, Zahra Ghorbanzadeh, and Feba Jacob. Genome-wide identification and functional characterisation of the eds1 gene family reveals evolutionary conservation and stress-responsive regulatory roles in barley. Scientific Reports, Mar 2026. URL: https://doi.org/10.1038/s41598-026-41481-8, doi:10.1038/s41598-026-41481-8. This article has 0 citations and is from a peer-reviewed journal.
(zonnchen2022eds1complexesare pages 11-11): Josua Zönnchen, Johannes Gantner, Dmitry Lapin, Karen Barthel, Lennart Eschen‐Lippold, Jessica L. Erickson, Sergio Landeo Villanueva, Stefan Zantop, Carola Kretschmer, Matthieu H. A. J. Joosten, Jane E. Parker, Raphael Guerois, and Johannes Stuttmann. eds1 complexes are not required for prr responses and execute tnl‐eti from the nucleus in nicotiana benthamiana. New Phytologist, 236:2249-2264, Oct 2022. URL: https://doi.org/10.1111/nph.18511, doi:10.1111/nph.18511. This article has 38 citations and is from a highest quality peer-reviewed journal.
(lapin2020originsandimmunity pages 12-14): Dmitry Lapin, Deepak D. Bhandari, and Jane E. Parker. Origins and immunity networking functions of eds1 family proteins. Annual Review of Phytopathology, 58:253-276, Aug 2020. URL: https://doi.org/10.1146/annurev-phyto-010820-012840, doi:10.1146/annurev-phyto-010820-012840. This article has 198 citations and is from a domain leading peer-reviewed journal.

Citations

yu2024activationofa pages 2-4
dangl2024acommonimmune pages 1-2
wagner2013structuralbasisfor pages 9-10
wagner2013structuralbasisfor pages 3-4
yu2024activationofa pages 1-2
lapin2020originsandimmunity pages 11-12
lapin2020originsandimmunity pages 8-9
voss2022crucialstepson pages 12-16
wiermer2005plantimmunitythe pages 1-2
lapin2020originsandimmunity pages 1-2
wagner2013structuralbasisfor pages 1-2
zonnchen2021differentialrequirementfor pages 1-3
lapin2020originsandimmunity pages 9-11
zonnchen2021differentialrequirementfor pages 6-8
zonnchen2021differentialrequirementfor pages 22-23
panahi2026genomewideidentificationand pages 7-9
lapin2020originsandimmunity pages 12-14
https://doi.org/10.1146/annurev-phyto-010820-012840;
https://doi.org/10.1016/j.chom.2013.11.006
https://doi.org/10.1126/science.adr3150;
https://doi.org/10.1126/science.adu4930
https://doi.org/10.1126/science.adr3150
https://doi.org/10.1016/j.isci.2024.108817
https://doi.org/10.1016/j.chom.2013.11.006;
https://doi.org/10.1146/annurev-phyto-010820-012840
https://doi.org/10.1101/2021.12.15.472806;
https://doi.org/10.1111/nph.18511
https://doi.org/10.1094/mpmi-12-19-0339-r
https://doi.org/10.1126/science.adu4930;
https://doi.org/10.15496/publikation-99005
https://doi.org/10.1016/j.pbi.2005.05.010,
https://doi.org/10.1146/annurev-phyto-010820-012840,
https://doi.org/10.1016/j.chom.2013.11.006,
https://doi.org/10.1126/science.adr3150,
https://doi.org/10.1126/science.adu4930,
https://doi.org/10.1101/2021.12.15.472806,
https://doi.org/10.1016/j.isci.2024.108817,
https://doi.org/10.1111/nph.18511,
https://doi.org/10.1094/mpmi-12-19-0339-r,
https://doi.org/10.1038/s41598-026-41481-8,

📄 View Raw YAML

id: Q9SU72
gene_symbol: EDS1
product_type: PROTEIN
status: COMPLETE
taxon:
  id: NCBITaxon:3702
  label: Arabidopsis thaliana
description: '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.'
alternative_products:
- name: '1'
  id: Q9SU72-1
- name: '2'
  id: Q9SU72-2
  sequence_note: VSP_057262
existing_annotations:
- term:
    id: GO:0000304
    label: response to singlet oxygen
  evidence_type: IGI
  original_reference_id: PMID:16790029
  review:
    summary: EDS1 contributes to singlet-oxygen/redox stress signaling in Arabidopsis.
    action: KEEP_AS_NON_CORE
    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.
- term:
    id: GO:0001666
    label: response to hypoxia
  evidence_type: IMP
  original_reference_id: PMID:18055613
  review:
    summary: EDS1 is genetically implicated in hypoxia-associated lysigenous aerenchyma and ROS regulation.
    action: KEEP_AS_NON_CORE
    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.
- term:
    id: GO:0009626
    label: plant-type hypersensitive response
  evidence_type: IMP
  original_reference_id: PMID:17997306
  review:
    summary: EDS1 is required for TIR-NLR-associated hypersensitive-response and cell-death outputs.
    action: ACCEPT
    reason: Hypersensitive response is a major experimentally supported output of EDS1-dependent TIR-NLR immune signaling, especially through the EDS1-SAG101/NRG1 branch.
- term:
    id: GO:0009627
    label: systemic acquired resistance
  evidence_type: IEP
  original_reference_id: PMID:17419843
  review:
    summary: EDS1 promotes salicylic-acid-associated systemic acquired resistance and defense amplification.
    action: ACCEPT
    reason: EDS1 acts upstream of SA accumulation/signaling and is necessary for systemic and basal defense reinforcement.
- term:
    id: GO:0010310
    label: regulation of hydrogen peroxide metabolic process
  evidence_type: IMP
  original_reference_id: PMID:18055613
  review:
    summary: EDS1 is genetically implicated in hypoxia-associated lysigenous aerenchyma and ROS regulation.
    action: KEEP_AS_NON_CORE
    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.
- term:
    id: GO:0010618
    label: aerenchyma formation
  evidence_type: IMP
  original_reference_id: PMID:18055613
  review:
    summary: EDS1 is genetically implicated in hypoxia-associated lysigenous aerenchyma and ROS regulation.
    action: KEEP_AS_NON_CORE
    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.
- term:
    id: GO:0050829
    label: defense response to Gram-negative bacterium
  evidence_type: IMP
  original_reference_id: PMID:29253890
  review:
    summary: EDS1 contributes to defense against Gram-negative bacterial pathogens, including Pseudomonas defense contexts.
    action: ACCEPT
    reason: Antibacterial defense is a central biological-process output of EDS1-dependent immune signaling.
- term:
    id: GO:0060866
    label: leaf abscission
  evidence_type: IMP
  original_reference_id: PMID:29253890
  review:
    summary: EDS1 is required for pathogen-triggered cauline leaf abscission in the cited bacterial defense context.
    action: KEEP_AS_NON_CORE
    reason: The leaf-abscission phenotype is a tissue-level antibacterial defense output mediated by SA/immune signaling, not a direct molecular role of EDS1.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:11574472
  supporting_entities:
  - UniProtKB:Q9S745
  review:
    summary: EDS1 physically associates with PAD4, SAG101, NLR/effectors, and other immune regulators, but generic protein binding does not describe the functional mechanism.
    action: MARK_AS_OVER_ANNOTATED
    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.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:16040633
  supporting_entities:
  - UniProtKB:Q4F883
  review:
    summary: EDS1 physically associates with PAD4, SAG101, NLR/effectors, and other immune regulators, but generic protein binding does not describe the functional mechanism.
    action: MARK_AS_OVER_ANNOTATED
    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.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:16040633
  supporting_entities:
  - UniProtKB:Q9S745
  review:
    summary: EDS1 physically associates with PAD4, SAG101, NLR/effectors, and other immune regulators, but generic protein binding does not describe the functional mechanism.
    action: MARK_AS_OVER_ANNOTATED
    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.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:21434927
  supporting_entities:
  - UniProtKB:Q4F883
  review:
    summary: EDS1 physically associates with PAD4, SAG101, NLR/effectors, and other immune regulators, but generic protein binding does not describe the functional mechanism.
    action: MARK_AS_OVER_ANNOTATED
    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.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:21434927
  supporting_entities:
  - UniProtKB:Q9S745
  review:
    summary: EDS1 physically associates with PAD4, SAG101, NLR/effectors, and other immune regulators, but generic protein binding does not describe the functional mechanism.
    action: MARK_AS_OVER_ANNOTATED
    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.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:23275581
  supporting_entities:
  - UniProtKB:F4KHI3
  review:
    summary: EDS1 physically associates with PAD4, SAG101, NLR/effectors, and other immune regulators, but generic protein binding does not describe the functional mechanism.
    action: MARK_AS_OVER_ANNOTATED
    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.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:28555890
  supporting_entities:
  - UniProtKB:Q9S745
  review:
    summary: EDS1 physically associates with PAD4, SAG101, NLR/effectors, and other immune regulators, but generic protein binding does not describe the functional mechanism.
    action: MARK_AS_OVER_ANNOTATED
    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.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:32612234
  supporting_entities:
  - UniProtKB:Q05466
  review:
    summary: EDS1 physically associates with PAD4, SAG101, NLR/effectors, and other immune regulators, but generic protein binding does not describe the functional mechanism.
    action: MARK_AS_OVER_ANNOTATED
    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.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:32612234
  supporting_entities:
  - UniProtKB:Q38845
  review:
    summary: EDS1 physically associates with PAD4, SAG101, NLR/effectors, and other immune regulators, but generic protein binding does not describe the functional mechanism.
    action: MARK_AS_OVER_ANNOTATED
    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.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:32612234
  supporting_entities:
  - UniProtKB:Q8RXD6
  review:
    summary: EDS1 physically associates with PAD4, SAG101, NLR/effectors, and other immune regulators, but generic protein binding does not describe the functional mechanism.
    action: MARK_AS_OVER_ANNOTATED
    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.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:32612234
  supporting_entities:
  - UniProtKB:Q94KL5
  review:
    summary: EDS1 physically associates with PAD4, SAG101, NLR/effectors, and other immune regulators, but generic protein binding does not describe the functional mechanism.
    action: MARK_AS_OVER_ANNOTATED
    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.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:32612234
  supporting_entities:
  - UniProtKB:Q9C9L2
  review:
    summary: EDS1 physically associates with PAD4, SAG101, NLR/effectors, and other immune regulators, but generic protein binding does not describe the functional mechanism.
    action: MARK_AS_OVER_ANNOTATED
    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.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:32612234
  supporting_entities:
  - UniProtKB:Q9S7W5
  review:
    summary: EDS1 physically associates with PAD4, SAG101, NLR/effectors, and other immune regulators, but generic protein binding does not describe the functional mechanism.
    action: MARK_AS_OVER_ANNOTATED
    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.
- term:
    id: GO:0016298
    label: lipase activity
  evidence_type: ISS
  original_reference_id: PMID:10077677
  review:
    summary: EDS1 is lipase-like by sequence/domain architecture, but no direct EDS1 lipase activity or physiological lipid substrate is established.
    action: REMOVE
    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.
- term:
    id: GO:0042803
    label: protein homodimerization activity
  evidence_type: IDA
  original_reference_id: PMID:11574472
  review:
    summary: EDS1 homodimerization has been observed, particularly for cytosolic EDS1 pools.
    action: KEEP_AS_NON_CORE
    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.
- term:
    id: GO:0042803
    label: protein homodimerization activity
  evidence_type: IDA
  original_reference_id: PMID:21434927
  review:
    summary: EDS1 homodimerization has been observed, particularly for cytosolic EDS1 pools.
    action: KEEP_AS_NON_CORE
    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.
- term:
    id: GO:0006629
    label: lipid metabolic process
  evidence_type: IEA
  original_reference_id: GO_REF:0000002
  review:
    summary: The InterPro lipid metabolic process transfer follows from the lipase-like fold but is not supported by EDS1 biology.
    action: REMOVE
    reason: EDS1 is an immune signaling pseudoenzyme/scaffold; no direct lipid metabolic process or lipid substrate is established.
- term:
    id: GO:0006952
    label: defense response
  evidence_type: IEA
  original_reference_id: GO_REF:0000002
  review:
    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.
    action: MARK_AS_OVER_ANNOTATED
    reason: The broad defense response term blurs the specific EDS1 immune signaling role captured by more precise experimental annotations.
- term:
    id: GO:0009626
    label: plant-type hypersensitive response
  evidence_type: IMP
  original_reference_id: PMID:16040633
  review:
    summary: EDS1 is required for TIR-NLR-associated hypersensitive-response and cell-death outputs.
    action: ACCEPT
    reason: Hypersensitive response is a major experimentally supported output of EDS1-dependent TIR-NLR immune signaling, especially through the EDS1-SAG101/NRG1 branch.
- term:
    id: GO:0009626
    label: plant-type hypersensitive response
  evidence_type: NAS
  original_reference_id: PMID:16040633
  review:
    summary: EDS1 is required for TIR-NLR-associated hypersensitive-response and cell-death outputs.
    action: ACCEPT
    reason: Hypersensitive response is a major experimentally supported output of EDS1-dependent TIR-NLR immune signaling, especially through the EDS1-SAG101/NRG1 branch.
- term:
    id: GO:0009626
    label: plant-type hypersensitive response
  evidence_type: IMP
  original_reference_id: PMID:19616764
  review:
    summary: EDS1 is required for TIR-NLR-associated hypersensitive-response and cell-death outputs.
    action: ACCEPT
    reason: Hypersensitive response is a major experimentally supported output of EDS1-dependent TIR-NLR immune signaling, especially through the EDS1-SAG101/NRG1 branch.
- term:
    id: GO:0009626
    label: plant-type hypersensitive response
  evidence_type: NAS
  original_reference_id: PMID:22072959
  review:
    summary: EDS1 is required for TIR-NLR-associated hypersensitive-response and cell-death outputs.
    action: ACCEPT
    reason: Hypersensitive response is a major experimentally supported output of EDS1-dependent TIR-NLR immune signaling, especially through the EDS1-SAG101/NRG1 branch.
- term:
    id: GO:0009862
    label: systemic acquired resistance, salicylic acid mediated signaling pathway
  evidence_type: IMP
  original_reference_id: PMID:11574472
  review:
    summary: EDS1 promotes salicylic-acid-associated systemic acquired resistance and defense amplification.
    action: ACCEPT
    reason: EDS1 acts upstream of SA accumulation/signaling and is necessary for systemic and basal defense reinforcement.
- term:
    id: GO:0009862
    label: systemic acquired resistance, salicylic acid mediated signaling pathway
  evidence_type: IMP
  original_reference_id: PMID:16040633
  review:
    summary: EDS1 promotes salicylic-acid-associated systemic acquired resistance and defense amplification.
    action: ACCEPT
    reason: EDS1 acts upstream of SA accumulation/signaling and is necessary for systemic and basal defense reinforcement.
- term:
    id: GO:0009862
    label: systemic acquired resistance, salicylic acid mediated signaling pathway
  evidence_type: NAS
  original_reference_id: PMID:22072959
  review:
    summary: EDS1 promotes salicylic-acid-associated systemic acquired resistance and defense amplification.
    action: ACCEPT
    reason: EDS1 acts upstream of SA accumulation/signaling and is necessary for systemic and basal defense reinforcement.
- term:
    id: GO:0005634
    label: nucleus
  evidence_type: IEA
  original_reference_id: GO_REF:0000044
  review:
    summary: EDS1 functions in the nucleus as part of immune transcriptional reprogramming and EDS1-containing complexes.
    action: ACCEPT
    reason: Nuclear EDS1 localization is experimentally supported and functionally important for basal and TIR-NLR-conditioned immunity.
- term:
    id: GO:0005634
    label: nucleus
  evidence_type: IDA
  original_reference_id: PMID:16040633
  review:
    summary: EDS1 functions in the nucleus as part of immune transcriptional reprogramming and EDS1-containing complexes.
    action: ACCEPT
    reason: Nuclear EDS1 localization is experimentally supported and functionally important for basal and TIR-NLR-conditioned immunity.
- term:
    id: GO:0005634
    label: nucleus
  evidence_type: IDA
  original_reference_id: PMID:22072959
  review:
    summary: EDS1 functions in the nucleus as part of immune transcriptional reprogramming and EDS1-containing complexes.
    action: ACCEPT
    reason: Nuclear EDS1 localization is experimentally supported and functionally important for basal and TIR-NLR-conditioned immunity.
- term:
    id: GO:0005634
    label: nucleus
  evidence_type: NAS
  original_reference_id: PMID:22072959
  review:
    summary: EDS1 functions in the nucleus as part of immune transcriptional reprogramming and EDS1-containing complexes.
    action: ACCEPT
    reason: Nuclear EDS1 localization is experimentally supported and functionally important for basal and TIR-NLR-conditioned immunity.
- term:
    id: GO:0005634
    label: nucleus
  evidence_type: EXP
  original_reference_id: PMID:22158819
  review:
    summary: EDS1 functions in the nucleus as part of immune transcriptional reprogramming and EDS1-containing complexes.
    action: ACCEPT
    reason: Nuclear EDS1 localization is experimentally supported and functionally important for basal and TIR-NLR-conditioned immunity.
- term:
    id: GO:0005634
    label: nucleus
  evidence_type: IDA
  original_reference_id: PMID:33751092
  review:
    summary: EDS1 functions in the nucleus as part of immune transcriptional reprogramming and EDS1-containing complexes.
    action: ACCEPT
    reason: Nuclear EDS1 localization is experimentally supported and functionally important for basal and TIR-NLR-conditioned immunity.
- term:
    id: GO:0005737
    label: cytoplasm
  evidence_type: IEA
  original_reference_id: GO_REF:0000044
  review:
    summary: EDS1 occupies cytoplasmic/cytosolic pools as part of nucleocytoplasmic immune signal relay.
    action: ACCEPT
    reason: Cytoplasmic EDS1 is experimentally supported and contributes to complete EDS1-dependent immune outputs.
- term:
    id: GO:0005737
    label: cytoplasm
  evidence_type: IDA
  original_reference_id: PMID:16040633
  review:
    summary: EDS1 occupies cytoplasmic/cytosolic pools as part of nucleocytoplasmic immune signal relay.
    action: ACCEPT
    reason: Cytoplasmic EDS1 is experimentally supported and contributes to complete EDS1-dependent immune outputs.
- term:
    id: GO:0005737
    label: cytoplasm
  evidence_type: IDA
  original_reference_id: PMID:22072959
  review:
    summary: EDS1 occupies cytoplasmic/cytosolic pools as part of nucleocytoplasmic immune signal relay.
    action: ACCEPT
    reason: Cytoplasmic EDS1 is experimentally supported and contributes to complete EDS1-dependent immune outputs.
- term:
    id: GO:0005737
    label: cytoplasm
  evidence_type: EXP
  original_reference_id: PMID:22158818
  review:
    summary: EDS1 occupies cytoplasmic/cytosolic pools as part of nucleocytoplasmic immune signal relay.
    action: ACCEPT
    reason: Cytoplasmic EDS1 is experimentally supported and contributes to complete EDS1-dependent immune outputs.
- term:
    id: GO:0005737
    label: cytoplasm
  evidence_type: EXP
  original_reference_id: PMID:22158819
  review:
    summary: EDS1 occupies cytoplasmic/cytosolic pools as part of nucleocytoplasmic immune signal relay.
    action: ACCEPT
    reason: Cytoplasmic EDS1 is experimentally supported and contributes to complete EDS1-dependent immune outputs.
- term:
    id: GO:0005737
    label: cytoplasm
  evidence_type: IDA
  original_reference_id: PMID:33751092
  review:
    summary: EDS1 occupies cytoplasmic/cytosolic pools as part of nucleocytoplasmic immune signal relay.
    action: ACCEPT
    reason: Cytoplasmic EDS1 is experimentally supported and contributes to complete EDS1-dependent immune outputs.
- term:
    id: GO:0005829
    label: cytosol
  evidence_type: IDA
  original_reference_id: PMID:16040633
  review:
    summary: EDS1 occupies cytoplasmic/cytosolic pools as part of nucleocytoplasmic immune signal relay.
    action: ACCEPT
    reason: Cytoplasmic EDS1 is experimentally supported and contributes to complete EDS1-dependent immune outputs.
- term:
    id: GO:0009507
    label: chloroplast
  evidence_type: ISM
  original_reference_id: GO_REF:0000122
  review:
    summary: The cited EIJ1 study supports chloroplast localization of EIJ1 and cytoplasmic/nuclear regulation of EDS1, not a stable chloroplast pool of EDS1.
    action: REMOVE
    reason: Current UniProt and literature synthesis support nucleocytoplasmic EDS1; the chloroplast annotation appears to over-transfer the EIJ1 localization context to EDS1.
- term:
    id: GO:0009507
    label: chloroplast
  evidence_type: IDA
  original_reference_id: PMID:33751092
  review:
    summary: The cited EIJ1 study supports chloroplast localization of EIJ1 and cytoplasmic/nuclear regulation of EDS1, not a stable chloroplast pool of EDS1.
    action: REMOVE
    reason: Current UniProt and literature synthesis support nucleocytoplasmic EDS1; the chloroplast annotation appears to over-transfer the EIJ1 localization context to EDS1.
- term:
    id: GO:0106093
    label: EDS1 disease-resistance complex
  evidence_type: IDA
  original_reference_id: PMID:11574472
  review:
    summary: EDS1 is a component of EDS1 disease-resistance complexes with PAD4 and SAG101.
    action: ACCEPT
    reason: EDS1-PAD4 and EDS1-SAG101 complex membership is central to EDS1 immune signaling and is directly supported by interaction and localization studies.
- term:
    id: GO:0106093
    label: EDS1 disease-resistance complex
  evidence_type: IDA
  original_reference_id: PMID:16040633
  review:
    summary: EDS1 is a component of EDS1 disease-resistance complexes with PAD4 and SAG101.
    action: ACCEPT
    reason: EDS1-PAD4 and EDS1-SAG101 complex membership is central to EDS1 immune signaling and is directly supported by interaction and localization studies.
- term:
    id: GO:0106093
    label: EDS1 disease-resistance complex
  evidence_type: NAS
  original_reference_id: PMID:22072959
  review:
    summary: EDS1 is a component of EDS1 disease-resistance complexes with PAD4 and SAG101.
    action: ACCEPT
    reason: EDS1-PAD4 and EDS1-SAG101 complex membership is central to EDS1 immune signaling and is directly supported by interaction and localization studies.
- term:
    id: GO:0035591
    label: signaling adaptor activity
  evidence_type: IC
  original_reference_id: file:ARATH/EDS1/EDS1-deep-research-falcon.md
  review:
    summary: EDS1 functions as a ligand-responsive immune signaling adaptor/pseudoenzyme rather than as a demonstrated lipase.
    action: NEW
    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.
    additional_reference_ids:
    - PMID:11574472
    - PMID:16040633
    - PMID:22072959
    supported_by:
    - reference_id: file:ARATH/EDS1/EDS1-deep-research-falcon.md
      supporting_text: ligand-responsive immune signaling adaptor/pseudoenzyme that forms **EDS1–PAD4** and **EDS1–SAG101** heterodimers
    - reference_id: PMID:11574472
      supporting_text: EDS1 and PAD4 proteins interact in healthy and pathogen-challenged plant cells.
    - reference_id: PMID:16040633
      supporting_text: Dynamic interactions of EDS1 and its signaling partners in multiple cell compartments
        are important for plant defense signal relay.
    - reference_id: PMID:22072959
      supporting_text: Co-IP of EDS1-90-MYC and PAD4-MYC with EDS1-80-FLAG.
references:
- id: GO_REF:0000002
  title: Gene Ontology annotation through association of InterPro records with GO terms
  findings: []
- id: GO_REF:0000044
  title: Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
  findings: []
- id: GO_REF:0000122
  title: AtSubP analysis
  findings: []
- id: PMID:10077677
  title: EDS1, an essential component of R gene-mediated disease resistance in Arabidopsis has homology to eukaryotic lipases.
  findings:
  - statement: EDS1 was cloned as a lipase-like gene required upstream of salicylic-acid-dependent PR1 expression and TIR-NLR-associated resistance.
- id: PMID:11574472
  title: Direct interaction between the Arabidopsis disease resistance signaling proteins, EDS1 and PAD4.
  findings:
  - statement: EDS1 interacts with PAD4, can homodimerize, acts early in defense, and recruits PAD4 for salicylic-acid-associated defense amplification.
- id: PMID:16040633
  title: Arabidopsis SENESCENCE-ASSOCIATED GENE101 stabilizes and signals within an ENHANCED DISEASE SUSCEPTIBILITY1 complex in plant innate immunity.
  findings:
  - statement: EDS1 forms molecularly and spatially distinct EDS1-SAG101 and EDS1-PAD4 complexes in nucleus and cytoplasm, and direct lipase activity was not demonstrated.
- id: PMID:16790029
  title: The role of EDS1 (enhanced disease susceptibility) during singlet oxygen-mediated stress responses of Arabidopsis.
  findings:
  - statement: EDS1 contributes to singlet oxygen-mediated stress responses.
- id: PMID:17419843
  title: Pathogen-associated molecular pattern recognition rather than development of tissue necrosis contributes to bacterial induction of systemic acquired resistance in Arabidopsis.
  findings: []
- id: PMID:17997306
  title: Nuclear accumulation of the Arabidopsis immune receptor RPS4 is necessary for triggering EDS1-dependent defense.
  findings: []
- id: PMID:18055613
  title: Lysigenous aerenchyma formation in Arabidopsis is controlled by LESION SIMULATING DISEASE1.
  findings:
  - statement: EDS1, PAD4, and LSD1 regulate hypoxia-associated aerenchyma formation and ROS-linked stress outputs.
- id: PMID:19616764
  title: Regulation of cell death and innate immunity by two receptor-like kinases in Arabidopsis.
  findings: []
- id: PMID:21434927
  title: Different roles of Enhanced Disease Susceptibility1 (EDS1) bound to and dissociated from Phytoalexin Deficient4 (PAD4) in Arabidopsis immunity.
  findings:
  - statement: Distinct EDS1 pools bound to PAD4 or SAG101 support basal resistance, salicylic-acid defense mobilization, and TIR-NLR immune signaling.
- id: PMID:22072959
  title: SAG101 forms a ternary complex with EDS1 and PAD4 and is required for resistance signaling against turnip crinkle virus.
  findings:
  - statement: EDS1 isoforms interact with PAD4 and SAG101 and can organize binary or ternary EDS1-family complexes with compartment-dependent localization.
- id: PMID:22158818
  title: Arabidopsis EDS1 connects pathogen effector recognition to cell compartment-specific immune responses.
  findings:
  - statement: EDS1 connects pathogen effector recognition to compartment-specific immune responses.
- id: PMID:22158819
  title: Pathogen effectors target Arabidopsis EDS1 and alter its interactions with immune regulators.
  findings:
  - statement: Pathogen effectors can target EDS1 and alter EDS1 interactions with immune regulators.
- id: PMID:23275581
  title: Natural variation in small molecule-induced TIR-NB-LRR signaling induces root growth arrest via EDS1- and PAD4-complexed R protein VICTR in Arabidopsis.
  findings: []
- id: PMID:28555890
  title: The dual role of LESION SIMULATING DISEASE 1 as a condition-dependent scaffold protein and transcription regulator.
  findings: []
- id: PMID:29253890
  title: Leaf shedding as an anti-bacterial defense in Arabidopsis cauline leaves.
  findings:
  - statement: EDS1 and other SA-defense components are required for pathogen-triggered cauline leaf abscission.
- id: PMID:32612234
  title: Extensive signal integration by the phytohormone protein network.
  findings: []
- id: PMID:33751092
  title: EDS1-interacting J protein 1 is an essential negative regulator of plant innate immunity in Arabidopsis.
  findings:
  - statement: EIJ1 regulates EDS1 nucleocytoplasmic distribution by interacting with EDS1 in the cytoplasm and limiting EDS1 nuclear trafficking.
- id: file:ARATH/EDS1/EDS1-deep-research-falcon.md
  title: Falcon deep research for Arabidopsis EDS1
  findings:
  - statement: EDS1 is a nucleocytoplasmic immune regulator that forms PAD4 or SAG101 complexes and functions as a ligand-responsive adaptor/pseudoenzyme in TIR-NLR signaling.
  - statement: Current evidence supports EDS1 immune signal transduction via regulated complex formation rather than direct lipase/hydrolase activity.
- id: file:ARATH/EDS1/EDS1-uniprot.txt
  title: UniProt record for Arabidopsis EDS1
  findings:
  - statement: UniProt identifies EDS1/Q9SU72 as enhanced disease susceptibility 1 with nuclear, cytoplasmic, cytosolic, and EDS1 disease-resistance complex annotations.
- id: file:interpro/panther/PTHR47090/PTHR47090-entries.csv
  title: PANTHER PTHR47090 protein EDS1-related family entries
  findings:
  - statement: PTHR47090 places Arabidopsis Q9SU72/EDS1 in the protein EDS1-related family.
core_functions:
- description: Ligand-responsive EDS1 immune signaling adaptor. EDS1 forms EDS1-PAD4 and EDS1-SAG101 immune complexes that translate TIR-NLR-derived nucleotide signals into helper-NLR-dependent salicylic-acid defense amplification, antibacterial defense, and hypersensitive-response outputs.
  molecular_function:
    id: GO:0035591
    label: signaling adaptor activity
  directly_involved_in:
  - id: GO:0009862
    label: systemic acquired resistance, salicylic acid mediated signaling pathway
  - id: GO:0009626
    label: plant-type hypersensitive response
  locations:
  - id: GO:0005634
    label: nucleus
  - id: GO:0005737
    label: cytoplasm
  supported_by:
  - reference_id: file:ARATH/EDS1/EDS1-deep-research-falcon.md
    supporting_text: ligand-responsive immune signaling adaptor/pseudoenzyme that forms **EDS1–PAD4** and **EDS1–SAG101** heterodimers
  - reference_id: file:ARATH/EDS1/EDS1-deep-research-falcon.md
    supporting_text: EDS1 heterodimers act as ligand-responsive hubs
  - reference_id: PMID:11574472
    supporting_text: EDS1 and PAD4 proteins interact in healthy and pathogen-challenged plant cells.
  - reference_id: PMID:16040633
    supporting_text: Dynamic interactions of EDS1 and its signaling partners in multiple cell compartments
      are important for plant defense signal relay.
proposed_new_terms: []
suggested_questions:
- question: Should GO add a more specific EDS1-family immune adaptor activity term for ligand-responsive TIR-NLR signal relay to helper NLRs?
- question: Should chloroplast localization annotations for EDS1 be reviewed to separate EDS1 from the chloroplast-localized EIJ1 regulatory context?
suggested_experiments:
- description: 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.
- description: 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.

Gene Description

Existing Annotations Review

Core Functions

Ligand-responsive EDS1 immune signaling adaptor. EDS1 forms EDS1-PAD4 and EDS1-SAG101 immune complexes that translate TIR-NLR-derived nucleotide signals into helper-NLR-dependent salicylic-acid defense amplification, antibacterial defense, and hypersensitive-response outputs.

References

Suggested Questions for Experts

Suggested Experiments

Deep Research

Falcon

Research report: Arabidopsis thaliana ENHANCED DISEASE SUSCEPTIBILITY 1 (EDS1)

Target verification (mandatory disambiguation)

1) Key concepts and definitions (current understanding)

1.1 EDS1 as a central immune “node”

1.2 Domain architecture: lipase-like + EP domain

1.3 Upstream receptor class: TIR-NLR (TNL) and TIR NADase activity

2) Recent developments and latest research (prioritizing 2023–2024)

2.1 2024 mechanistic breakthrough: ligand-activated EDS1–PAD4–ADR1 (EPA) heterotrimer

2.2 2024 expert synthesis: a conserved angiosperm immune response node

2.3 2024 evidence for physical coupling of TIR domains to EDS1-family proteins

3) Primary function of EDS1: enzyme vs signaling adaptor

3.1 EDS1 is lipase-like but not a proven hydrolase in immunity

3.2 Catalytic triad: lineage/context dependence

3.3 What is the “substrate”?

4) Pathways and mechanism: from TIR NADase to helper NLR execution

4.1 Signaling flow

4.2 Relationship to PTI/ETI and system differences

5) Subcellular localization and where EDS1 functions

5.1 Nucleocytoplasmic localization

5.2 Nuclear EDS1 is strongly linked to transcriptional defense outputs

5.3 Cytoplasmic pools and cell-death outputs

6) Applications and real-world implementations

6.1 Crop engineering implications: the EDS1 node as a compatibility requirement

6.2 Actionable genetic levers around the EDS1 node

6.3 Reported translational examples (beyond Arabidopsis)

7) Statistics and data highlights (from recent studies)

Evidence summary table

Concluding functional annotation (for ARATH EDS1 / UniProt Q9SU72)

Citations

📄 View Raw YAML