RPM1 is an Arabidopsis coiled-coil NB-LRR/CNL immune receptor that confers resistance to Pseudomonas syringae strains delivering AvrB or AvrRpm1. RPM1 acts at the cytoplasmic face of the plasma membrane, where it guards the RIN4 immune hub and is activated by effector-induced RIN4 modification, especially Thr166 phosphorylation. Its core role is nucleotide-dependent immune receptor signaling that triggers effector-triggered antibacterial defense and hypersensitive response; generic protein binding and broad defense-response rows should be interpreted through this RPM1-RIN4 plasma-membrane guard mechanism.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0006952 defense response | TAS PMID:7638602 Structure of the Arabidopsis RPM1 gene enabling dual specifi... | MODIFY | Summary: RPM1 mediates effector-triggered defense against Pseudomonas strains expressing AvrB or AvrRpm1, but the existing defense response term is broad. Reason: Defense response to bacterium better captures the experimentally supported RPM1 output than generic defense response. Proposed replacements: defense response to bacterium |
| GO:0009626 plant-type hypersensitive response | IDA PMID:8768370 Expression of the Pseudomonas syringae avirulence protein Av... | ACCEPT | Summary: RPM1 activation by AvrB/AvrRpm1-triggered RIN4 modification elicits hypersensitive-response cell death. Reason: Hypersensitive response is a canonical output of RPM1-mediated effector-triggered immunity and is supported by AvrB/RPM1 experiments. |
| GO:0000166 nucleotide binding | ISS PMID:7638602 Structure of the Arabidopsis RPM1 gene enabling dual specifi... | MODIFY | Summary: RPM1 has an NB-ARC nucleotide-binding module, but generic nucleotide binding is less precise than the ADP/ATP switch used by NLRs. Reason: Use ADP binding or ATP binding for the NB-ARC molecular switch rather than a broad nucleotide-binding term. Proposed replacements: ADP binding ATP binding |
| GO:0005515 protein binding | IPI PMID:11955429 RIN4 interacts with Pseudomonas syringae type III effector m... | MARK AS OVER ANNOTATED | Summary: RPM1-associated interactions with RIN4, RIN-family proteins, CRT1, and other immune regulators are biologically meaningful, but generic protein binding obscures the receptor mechanism. Reason: The informative curation is RPM1 immune receptor activity at a RIN4-centered plasma-membrane complex; protein binding alone is too generic for the core function. |
| GO:0005515 protein binding | IPI PMID:15722472 RIN13 is a positive regulator of the plant disease resistanc... | MARK AS OVER ANNOTATED | Summary: RPM1-associated interactions with RIN4, RIN-family proteins, CRT1, and other immune regulators are biologically meaningful, but generic protein binding obscures the receptor mechanism. Reason: The informative curation is RPM1 immune receptor activity at a RIN4-centered plasma-membrane complex; protein binding alone is too generic for the core function. |
| GO:0005515 protein binding | IPI PMID:16212605 A duplicated pair of Arabidopsis RING-finger E3 ligases cont... | MARK AS OVER ANNOTATED | Summary: RPM1-associated interactions with RIN4, RIN-family proteins, CRT1, and other immune regulators are biologically meaningful, but generic protein binding obscures the receptor mechanism. Reason: The informative curation is RPM1 immune receptor activity at a RIN4-centered plasma-membrane complex; protein binding alone is too generic for the core function. |
| GO:0005515 protein binding | IPI PMID:20332379 Endosome-associated CRT1 functions early in resistance gene-... | MARK AS OVER ANNOTATED | Summary: RPM1-associated interactions with RIN4, RIN-family proteins, CRT1, and other immune regulators are biologically meaningful, but generic protein binding obscures the receptor mechanism. Reason: The informative curation is RPM1 immune receptor activity at a RIN4-centered plasma-membrane complex; protein binding alone is too generic for the core function. |
| GO:0005515 protein binding | IPI PMID:38358510 The RIN4-like/NOI proteins NOI10 and NOI11 modulate the resp... | MARK AS OVER ANNOTATED | Summary: RPM1-associated interactions with RIN4, RIN-family proteins, CRT1, and other immune regulators are biologically meaningful, but generic protein binding obscures the receptor mechanism. Reason: The informative curation is RPM1 immune receptor activity at a RIN4-centered plasma-membrane complex; protein binding alone is too generic for the core function. |
| GO:0043531 ADP binding | IEA GO_REF:0000002 | KEEP AS NON CORE | Summary: RPM1 contains an NB-ARC module expected to bind ADP/ATP as part of NLR molecular switching. Reason: ADP binding is mechanistically relevant, but RPM1's core gene-level role is immune receptor signaling rather than nucleotide binding alone. |
| GO:0006952 defense response | IEA GO_REF:0000002 | MODIFY | Summary: RPM1 mediates effector-triggered defense against Pseudomonas strains expressing AvrB or AvrRpm1, but the existing defense response term is broad. Reason: Defense response to bacterium better captures the experimentally supported RPM1 output than generic defense response. Proposed replacements: defense response to bacterium |
| GO:0009626 plant-type hypersensitive response | IEA GO_REF:0000117 | ACCEPT | Summary: RPM1 activation by AvrB/AvrRpm1-triggered RIN4 modification elicits hypersensitive-response cell death. Reason: Hypersensitive response is a canonical output of RPM1-mediated effector-triggered immunity and is supported by AvrB/RPM1 experiments. |
| GO:0005886 plasma membrane | IEA GO_REF:0000044 | ACCEPT | Summary: RPM1 is a peripheral protein enriched at the plasma membrane. Reason: Plasma membrane localization is central to RPM1 function because RPM1 guards RIN4 at the cytoplasmic face of the plasma membrane. |
| GO:0005886 plasma membrane | IEA GO_REF:0000117 | ACCEPT | Summary: RPM1 is a peripheral protein enriched at the plasma membrane. Reason: Plasma membrane localization is central to RPM1 function because RPM1 guards RIN4 at the cytoplasmic face of the plasma membrane. |
| GO:0005886 plasma membrane | IDA PMID:9861059 The Arabidopsis thaliana RPM1 disease resistance gene produc... | ACCEPT | Summary: RPM1 is a peripheral protein enriched at the plasma membrane. Reason: Plasma membrane localization is central to RPM1 function because RPM1 guards RIN4 at the cytoplasmic face of the plasma membrane. |
| GO:0012505 endomembrane system | IEA GO_REF:0000044 | MODIFY | Summary: The cited localization evidence points to plasma-membrane/microsomal association and is better captured by a plasma-membrane cytoplasmic-face term than by broad endomembrane system. Reason: RPM1 is specifically a peripheral/extrinsic protein at the cytoplasmic side of the plasma membrane; endomembrane system is less precise. Proposed replacements: extrinsic component of cytoplasmic side of plasma membrane |
| GO:0012505 endomembrane system | EXP PMID:9861059 The Arabidopsis thaliana RPM1 disease resistance gene produc... | MODIFY | Summary: The cited localization evidence points to plasma-membrane/microsomal association and is better captured by a plasma-membrane cytoplasmic-face term than by broad endomembrane system. Reason: RPM1 is specifically a peripheral/extrinsic protein at the cytoplasmic side of the plasma membrane; endomembrane system is less precise. Proposed replacements: extrinsic component of cytoplasmic side of plasma membrane |
| GO:0031234 extrinsic component of cytoplasmic side of plasma membrane | IDA PMID:9861059 The Arabidopsis thaliana RPM1 disease resistance gene produc... | ACCEPT | Summary: RPM1 resides on the cytoplasmic face of the plasma membrane as a peripheral membrane-associated immune receptor. Reason: This is the most precise existing localization annotation for the site of RPM1-RIN4 guard signaling. |
| GO:0140375 immune receptor activity | IC file:ARATH/RPM1/RPM1-deep-research-falcon.md | NEW | Summary: RPM1 functions as a CNL immune receptor that monitors effector-induced RIN4 modification. Reason: GOA captures defense outputs and nucleotide binding but omits the core molecular role of RPM1 as an immune receptor. Supporting Evidence: file:ARATH/RPM1/RPM1-deep-research-falcon.md RPM1 is a canonical example of **indirect effector recognition** PMID:7638602 The Arabidopsis thaliana RPM1 gene enables dual specificity to pathogens expressing either of two unrelated Pseudomonas syringae avr genes. PMID:8768370 both stable and transient expression of avrB in Arabidopsis resulted in RPM1-dependent necrosis |
| GO:0002218 activation of innate immune response | IC file:ARATH/RPM1/RPM1-deep-research-falcon.md | NEW | Summary: RPM1 activates intracellular effector-triggered immune signaling after effector-induced RIN4 modification. Reason: This broader innate-immune activation term avoids incorrectly treating RPM1 guarded effector recognition as PAMP pattern-recognition receptor signaling. Supporting Evidence: file:ARATH/RPM1/RPM1-deep-research-falcon.md mediating effector-triggered immunity (ETI) to *Pseudomonas syringae* effectors **AvrRpm1** and **AvrB** PMID:7638602 The Arabidopsis thaliana RPM1 gene enables dual specificity to pathogens expressing either of two unrelated Pseudomonas syringae avr genes. PMID:8768370 both stable and transient expression of avrB in Arabidopsis resulted in RPM1-dependent necrosis |
| GO:0042742 defense response to bacterium | IC file:ARATH/RPM1/RPM1-deep-research-falcon.md | NEW | Summary: RPM1 confers resistance to Pseudomonas syringae strains expressing AvrB or AvrRpm1. Reason: This is the precise antibacterial defense output missing from current RPM1 GOA rows. Supporting Evidence: file:ARATH/RPM1/RPM1-deep-research-falcon.md RPM1 mediates race-specific resistance to *P. syringae* strains delivering **AvrB** or **AvrRpm1** PMID:7638602 The Arabidopsis thaliana RPM1 gene enables dual specificity to pathogens expressing either of two unrelated Pseudomonas syringae avr genes. PMID:8768370 Both stable and transient expression of avrB in Arabidopsis resulted in RPM1-dependent necrosis. |
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Download this section (compressed HTML)Q: Should RPM1 and related CNLs receive immune receptor activity annotations rather than only generic nucleotide/protein binding annotations?
Q: Should broad endomembrane-system annotations for RPM1 be replaced upstream with the cytoplasmic-face plasma membrane term?
Experiment: Reconstitute RPM1 with RIN4 phosphorylation or ADP-ribosylation states in plasma-membrane fractions to quantify receptor activation and nucleotide exchange.
Experiment: Measure RPM1 ADP/ATP binding and hydrolysis states before and after RIN4 phosphomimic activation to connect NB-ARC switching with guardee modification sensing.
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