RPS2 is an Arabidopsis plasma-membrane-associated coiled-coil NB-LRR/CNL immune receptor that confers resistance to Pseudomonas syringae strains delivering AvrRpt2. Its core role is immune receptor signaling by guarding the RIN4 hub: AvrRpt2-mediated RIN4 cleavage/elimination relieves RPS2 inhibition and triggers effector-triggered immunity, hypersensitive response, and antibacterial defense. The NB-ARC domain supports nucleotide-dependent receptor switching, while generic protein-binding annotations should be interpreted through the RPS2-RIN4/NDR1 immune complex rather than as standalone molecular functions.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
|
GO:0006952
defense response
|
TAS
PMID:11333251 The leucine-rich repeat domain can determine effective inter... |
MODIFY |
Summary: RPS2 mediates antibacterial effector-triggered immunity, but the existing defense response term is broad.
Reason: RPS2 biology is specifically AvrRpt2/Pseudomonas-triggered antibacterial immune receptor signaling; defense response to bacterium is the more precise process term.
Proposed replacements:
defense response to bacterium
|
|
GO:0006952
defense response
|
TAS
PMID:8091210 RPS2 of Arabidopsis thaliana: a leucine-rich repeat class of... |
MODIFY |
Summary: RPS2 mediates antibacterial effector-triggered immunity, but the existing defense response term is broad.
Reason: RPS2 biology is specifically AvrRpt2/Pseudomonas-triggered antibacterial immune receptor signaling; defense response to bacterium is the more precise process term.
Proposed replacements:
defense response to bacterium
|
|
GO:0009626
plant-type hypersensitive response
|
IMP
PMID:11204781 Mutational analysis of the Arabidopsis RPS2 disease resistan... |
ACCEPT |
Summary: RPS2 activation by AvrRpt2/RIN4 perturbation triggers hypersensitive-response outputs.
Reason: Hypersensitive response is a canonical experimentally supported output of RPS2-mediated effector-triggered immunity.
|
|
GO:0016045
detection of bacterium
|
IMP
PMID:11333251 The leucine-rich repeat domain can determine effective inter... |
MODIFY |
Summary: RPS2 detects AvrRpt2-triggered perturbation of the host RIN4 complex rather than detecting bacteria directly.
Reason: The term should reflect activation of innate immunity by guarded effector-triggered RIN4 perturbation rather than generic detection of bacterium or PAMP pattern-recognition receptor signaling.
Proposed replacements:
activation of innate immune response
|
|
GO:0042742
defense response to bacterium
|
IMP
PMID:22331412 Structure-function analysis of the coiled-coil and leucine-r... |
REMOVE |
Summary: The process is appropriate for RPS2, but this cited paper is RPS5-focused and does not provide RPS2-specific support for the row.
Reason: Retain RPS2 antibacterial defense through the independently supported PMID:8091210 row; remove this evidence line because the cited reference is not RPS2-centered.
|
|
GO:0042742
defense response to bacterium
|
IMP
PMID:8091210 RPS2 of Arabidopsis thaliana: a leucine-rich repeat class of... |
ACCEPT |
Summary: RPS2 confers defense against Pseudomonas syringae strains expressing AvrRpt2.
Reason: Antibacterial defense is the primary biological-process output of RPS2-mediated effector-triggered immunity.
|
|
GO:0005515
protein binding
|
IPI
DOI:10.1016/j.pmpp.2005.02.006 |
MARK AS OVER ANNOTATED |
Summary: RPS2 interacts with immune regulators such as RIN4 and NLR-control proteins, but generic protein binding obscures the receptor mechanism.
Reason: The informative molecular role is immune receptor activity and RIN4-guard signaling; protein binding alone is too generic for RPS2 functional curation.
|
|
GO:0005515
protein binding
|
IPI
PMID:12581526 Initiation of RPS2-specified disease resistance in Arabidops... |
MARK AS OVER ANNOTATED |
Summary: RPS2 interacts with immune regulators such as RIN4 and NLR-control proteins, but generic protein binding obscures the receptor mechanism.
Reason: The informative molecular role is immune receptor activity and RIN4-guard signaling; protein binding alone is too generic for RPS2 functional curation.
|
|
GO:0005515
protein binding
|
IPI
PMID:19682297 An F-box gene, CPR30, functions as a negative regulator of t... |
REMOVE |
Summary: The cached CPR30/F-box paper supports CPR30 interactions with ASK proteins and defense regulation, but not direct RPS2 binding.
Reason: This IPI row lacks accessible RPS2-specific interaction support in the cited source; retain RPS2 interaction context through the RIN4-supported PMID:12581526 row instead.
Supporting Evidence:
PMID:19682297
CPR30 could interact with multiple Arabidopsis-SKP1-like (ASK) proteins in vivo
|
|
GO:0005515
protein binding
|
IPI
PMID:26867179 Plant TRAF Proteins Regulate NLR Immune Receptor Turnover. |
MARK AS OVER ANNOTATED |
Summary: RPS2 interacts with immune regulators such as RIN4 and NLR-control proteins, but generic protein binding obscures the receptor mechanism.
Reason: The informative molecular role is immune receptor activity and RIN4-guard signaling; protein binding alone is too generic for RPS2 functional curation.
|
|
GO:0043531
ADP binding
|
IEA
GO_REF:0000002 |
KEEP AS NON CORE |
Summary: RPS2 contains an NB-ARC nucleotide-binding module expected to function as an ADP/ATP-regulated molecular switch.
Reason: ADP binding is plausible and mechanistically relevant for the NLR switch, but the core gene-level role is immune receptor signaling rather than nucleotide binding alone.
|
|
GO:0002220
innate immune response activating cell surface receptor signaling pathway
|
EXP
PMID:22331412 Structure-function analysis of the coiled-coil and leucine-r... |
REMOVE |
Summary: RPS2 is an intracellular CNL receptor, not a cell-surface receptor signaling component, and the cited RPS5 paper does not support this RPS2-specific row.
Reason: Replace the concept in curation with cytoplasmic pattern recognition receptor signaling based on RPS2-specific evidence; this GOA row is both pathway-mismatched and citation-mismatched.
|
|
GO:0005737
cytoplasm
|
IEA
GO_REF:0000044 |
ACCEPT |
Summary: RPS2 was originally characterized as acting inside plant cells and has cytoplasmic/intracellular localization support.
Reason: Cytoplasmic localization is compatible with RPS2 as an intracellular immune receptor, although later work refines this to a plasma-membrane-associated RIN4 complex.
|
|
GO:0005737
cytoplasm
|
EXP
PMID:8986840 Molecular recognition of pathogen attack occurs inside of pl... |
ACCEPT |
Summary: RPS2 was originally characterized as acting inside plant cells and has cytoplasmic/intracellular localization support.
Reason: Cytoplasmic localization is compatible with RPS2 as an intracellular immune receptor, although later work refines this to a plasma-membrane-associated RIN4 complex.
Supporting Evidence:
PMID:8986840
Mutational analysis of RPS2 protein and in vitro translation/translocation studies indicated that RPS2 protein is localized in the plant cytoplasm.
|
|
GO:0005886
plasma membrane
|
IEA
GO_REF:0000044 |
ACCEPT |
Summary: RPS2 is plasma-membrane associated and remains membrane-associated during activation.
Reason: Plasma membrane localization is central to the RIN4-guard mechanism because RIN4 and AvrRpt2 act in a membrane-associated immune complex.
|
|
GO:0005886
plasma membrane
|
IDA
PMID:12581526 Initiation of RPS2-specified disease resistance in Arabidops... |
ACCEPT |
Summary: RPS2 is plasma-membrane associated and remains membrane-associated during activation.
Reason: Plasma membrane localization is central to the RIN4-guard mechanism because RIN4 and AvrRpt2 act in a membrane-associated immune complex.
|
|
GO:0005886
plasma membrane
|
EXP
PMID:22331412 Structure-function analysis of the coiled-coil and leucine-r... |
REMOVE |
Summary: RPS2 plasma-membrane association is well supported, but this RPS5-focused citation does not provide RPS2-specific support for the row.
Reason: Retain plasma membrane localization through the RPS2-specific PMID:12581526/UniProt-supported rows; remove this citation-mismatched PHI-base row.
|
|
GO:0140375
immune receptor activity
|
IC
file:ARATH/RPS2/RPS2-deep-research-falcon.md |
NEW |
Summary: RPS2 functions as an intracellular CNL immune receptor that senses AvrRpt2-mediated RIN4 perturbation.
Reason: GOA captures downstream defense outputs and ADP binding but omits the core molecular role of RPS2 as an immune receptor.
Supporting Evidence:
file:ARATH/RPS2/RPS2-deep-research-falcon.md
RPS2’s primary role is as a **disease resistance NLR**
PMID:12581526
RPS2 physically interacts with Arabidopsis RIN4
|
|
GO:0002218
activation of innate immune response
|
IC
file:ARATH/RPS2/RPS2-deep-research-falcon.md |
NEW |
Summary: RPS2 activates intracellular effector-triggered immune signaling after AvrRpt2-mediated RIN4 cleavage/elimination.
Reason: This broad innate-immune activation term captures guarded effector-triggered RIN4 perturbation without misclassifying RPS2 as a ligand/PAMP-binding cytoplasmic PRR.
Supporting Evidence:
file:ARATH/RPS2/RPS2-deep-research-falcon.md
membrane-associated CNL sensor
PMID:12581526
RPS2 initiates signaling based upon perception of RIN4 disappearance
|
Q: Should RPS2 and related CNLs receive immune receptor activity annotations rather than only ADP binding and generic protein binding?
Q: Should PHI-base/GOA rows citing RPS5 literature for RPS2 be corrected upstream?
Experiment: Reconstitute RPS2, RIN4, and AvrRpt2-controlled RIN4 cleavage states in plant membrane fractions to quantify receptor activation and nucleotide exchange.
Experiment: Test RPS2 NB-ARC nucleotide binding and hydrolysis states in purified or membrane-reconstituted complexes to connect ADP/ATP switching to RIN4-guard activation.
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.
The symbol RPS2 is ambiguous across biology (often “ribosomal protein S2”), but the literature retrieved here consistently uses RPS2 as an Arabidopsis NB-LRR/NLR disease-resistance protein that recognizes Pseudomonas syringae effector AvrRpt2 through perturbation of the host protein RIN4, matching the UniProt Q42484 description and domain architecture (NB-ARC + LRR; CNL class). No retrieved sources treat RPS2 as a ribosomal protein in this immune context. (axtell2003initiationofrps2specified pages 1-1, day2005molecularbasisfor pages 1-2, day2006ndr1interactionwith pages 1-2)
Plant immunity is often described as two interacting layers: pattern-triggered immunity (PTI) initiated by cell-surface pattern-recognition receptors (PRRs) and effector-triggered immunity (ETI) initiated by intracellular immune receptors (NLRs). Modern views emphasize PTI–ETI cooperation/synergy, where ETI and PTI share downstream signaling and can mutually potentiate defense outputs. (yu2024pti‐etisynergisticsignal pages 3-5, nabi2024patterntriggeredimmunityand pages 6-7)
NLRs (historically “NB-LRR” proteins) generally have (i) an N-terminal signaling domain (commonly CC in CNLs or TIR in TNLs), (ii) a central NB-ARC nucleotide-binding module that functions as an ADP/ATP-regulated molecular switch, and (iii) C-terminal LRRs that contribute to recognition and autoregulation. Activation involves conformational switching and, in many systems, oligomerization (“resistosome” concepts), with helper NLRs (e.g., ADR1/NRG1 families) contributing to downstream signal transduction including Ca2+-associated outputs in broader NLR biology. (nabi2024patterntriggeredimmunityand pages 6-7, yu2024pti‐etisynergisticsignal pages 3-5)
Direct receptor–effector binding is not always required. In the guard model, an NLR monitors (“guards”) a host protein (a guardee) that is targeted by pathogen effectors. Perturbation of the guardee then triggers NLR activation. In the Arabidopsis RPS2 system, RIN4 is a canonical guardee/hub targeted by multiple effectors; AvrRpt2-mediated cleavage/elimination of RIN4 is sensed to activate RPS2-dependent ETI. (axtell2003initiationofrps2specified pages 1-3, nabi2024patterntriggeredimmunityand pages 6-7)
RPS2’s primary role is as a disease resistance NLR that confers resistance to Pseudomonas syringae strains delivering AvrRpt2 into host cells via the type III secretion system, inducing ETI-associated defense outputs including hypersensitive response (HR)-like cell death and restriction of pathogen growth. (axtell2003initiationofrps2specified pages 1-1, day2006ndr1interactionwith pages 1-2)
A central experimental conclusion is that initiation of RPS2-specified resistance is coupled to AvrRpt2-directed elimination of RIN4, supporting an indirect recognition/guard mechanism. Importantly, AvrRpt2-mediated RIN4 elimination can occur even in mutant backgrounds that disrupt downstream signaling, indicating that RIN4 perturbation is upstream of RPS2 activation. (axtell2003initiationofrps2specified pages 1-3, axtell2003initiationofrps2specified pages 3-4)
RIN4 can negatively regulate RPS2 activity: in transient expression systems, co-expression of RIN4 suppresses RPS2-triggered HR, while AvrRpt2 restores HR concomitant with its action on RIN4. Mapping experiments identify RIN4 residues important for association and negative regulation of RPS2, emphasizing that the RPS2–RIN4 interaction is a key control point. (day2005molecularbasisfor pages 1-2, day2005molecularbasisfor pages 7-8)
Biochemical fractionation and extraction experiments with functional RPS2-HA indicate RPS2 is membrane-associated and behaves like an integral membrane protein. Treatments that remove peripheral proteins (e.g., high salt, carbonate at pH 11, urea) do not release RPS2-HA, while detergent does. A key conclusion from this work is that RPS2 remains membrane-bound during activation and pathogenesis, indicating activation does not require wholesale relocalization away from the membrane. (axtell2003initiationofrps2specified pages 3-4, axtell2003initiationofrps2specified pages 4-5)
RIN4 is a plasma-membrane-tethered protein (lipidation/acylation motifs), and AvrRpt2 also localizes to membranes. RPS2 physically associates with RIN4 in planta. These observations support a model in which the key recognition event (RIN4 cleavage/elimination) and early signaling occur within a membrane-associated complex. (axtell2003initiationofrps2specified pages 4-5, alam2021rin4homologsfrom pages 13-14)
NDR1 is a key signaling component required for resistance mediated by several CC-NLRs including RPS2. NDR1 associates with RIN4 in planta; mapping indicates the cytoplasmic N-terminus of NDR1 is required for RIN4 interaction, and NDR1 variants that disrupt this association fail to restore AvrRpt2/RPS2-dependent HR in complementation contexts. (day2006ndr1interactionwith pages 1-2, day2006ndr1interactionwith pages 4-5)
Together, the primary studies support an RPS2-centered signaling module where (i) RIN4 suppresses RPS2 in a pre-activation complex, (ii) AvrRpt2 cleavage/elimination of RIN4 removes this suppression and triggers ETI, and (iii) NDR1–RIN4 interaction contributes to correct activation of downstream resistance pathways. (day2005molecularbasisfor pages 1-2, day2006ndr1interactionwith pages 4-5)
A 2024 review synthesizes modern NLR concepts (NB-ARC nucleotide switch; resistosome ideas; helper NLRs; convergence of PTI/ETI outputs) and explicitly places RIN4 as a canonical guardee whose targeting (including by AvrRpt2) activates RPS2. This reinforces that RPS2 is a model system for indirect effector recognition and for thinking about PTI–ETI integration. (nabi2024patterntriggeredimmunityand pages 6-7)
A 2024 study reports that phosphorylation of RIN4 at T166 can disrupt RIN4 plasma-membrane localization by weakening interaction with Exo70B1, repressing defense activation and phenocopying exo70b1-associated PTI suppression in a phosphomimic line. Although not centered on RPS2 directly, this provides a mechanistic advance on how RIN4’s post-translational modification and trafficking/localization can tune immune signaling—highly relevant to a system where RIN4 status controls RPS2 activation. (zhao2024subcellularspatialregulation pages 1-2)
A 2024 Plant Communications study reanalyzes Arabidopsis time-course transcriptomes after low-dose AvrRpt2-triggered ETI, reporting pervasive double-peak expression patterns that can be decomposed into two coordinated single peaks, consistent with responses from two distinct cell populations. The authors also identify a conserved gene set showing similar kinetics during PTI, supporting overlapping downstream transcriptional networks for PTI and ETI. (liu2024decompositionofdynamic pages 1-2)
These are not field prevalence statistics (not applicable for a single Arabidopsis gene), but experimental quantitative anchors used in RPS2 functional studies.
Although RPS2 itself is primarily a model-gene system, the mechanistic principles derived from RPS2/RIN4/AvrRpt2 inform translational crop immunity strategies:
RPS2 (UniProt Q42484) is best interpreted as a membrane-associated CNL sensor that detects AvrRpt2 activity indirectly by monitoring the integrity/state of a plasma-membrane RIN4 complex. The most consistent mechanistic picture from classic primary work is: (i) RIN4 maintains RPS2 in an off state; (ii) AvrRpt2’s protease activity eliminates/cleaves RIN4; (iii) the resulting perturbation triggers RPS2-dependent ETI outputs; and (iv) NDR1, via physical association with RIN4 and its topology at the plasma membrane, contributes essentially to correct signal initiation/transduction. This architecture makes RPS2 a canonical example of “guarding” and illustrates why modern PTI–ETI convergence models place guarded hubs (like RIN4) at the interface of multiple immune inputs and post-translational/spatial regulation. (axtell2003initiationofrps2specified pages 1-3, day2005molecularbasisfor pages 1-2, day2006ndr1interactionwith pages 4-5, nabi2024patterntriggeredimmunityand pages 6-7, zhao2024subcellularspatialregulation pages 1-2)
| Topic | Key evidence/claim | Evidence type | Key experimental parameters or statistics (if available) | Primary sources with year, DOI URL |
|---|---|---|---|---|
| Identity | The target is the Arabidopsis thaliana immune receptor RPS2 (At4g26090; UniProt Q42484), an NB-LRR/NLR disease-resistance protein activated by Pseudomonas syringae effector AvrRpt2 via perturbation of RIN4, not ribosomal protein S2. | Genetics, biochemistry, review | RPS2-HA transgene complements rps2-101C; literature consistently places RPS2 in AvrRpt2-triggered ETI. | Axtell & Staskawicz 2003, Cell, https://doi.org/10.1016/S0092-8674(03)00036-9; Day et al. 2005, Plant Cell, https://doi.org/10.1105/tpc.104.030163; Day et al. 2006, Plant Cell, https://doi.org/10.1105/tpc.106.044693 (axtell2003initiationofrps2specified pages 1-1, day2005molecularbasisfor pages 1-2, day2006ndr1interactionwith pages 1-2) |
| Function | RPS2 is a CNL/NB-LRR intracellular immune receptor whose primary function is to trigger effector-triggered immunity (ETI) against AvrRpt2-expressing P. syringae, leading to defense outputs such as HR/cell death and disease resistance. | Genetics, cell biology, review | In transient assays, RPS2-dependent HR is detectable by ~22 h after infiltration; disease symptoms/resistance scored at 4–5 dpi in Arabidopsis pathoassays. | Day et al. 2005, Plant Cell, https://doi.org/10.1105/tpc.104.030163; Axtell & Staskawicz 2003, Cell, https://doi.org/10.1016/S0092-8674(03)00036-9; Nabi et al. 2024, Physiol Mol Biol Plants, https://doi.org/10.1007/s12298-024-01452-7 (day2005molecularbasisfor pages 1-2, axtell2003initiationofrps2specified pages 1-1, nabi2024patterntriggeredimmunityand pages 6-7, axtell2003initiationofrps2specified pages 3-4) |
| Recognition mechanism | RPS2 recognizes AvrRpt2 indirectly by sensing AvrRpt2-mediated cleavage/elimination of RIN4 (guard model), rather than direct AvrRpt2 binding. | Genetics, biochemistry, review | AvrRpt2-mediated RIN4 elimination occurs even in rps2, ndr1, and Atrar1 backgrounds, placing RIN4 removal upstream of RPS2 signaling. | Axtell & Staskawicz 2003, Cell, https://doi.org/10.1016/S0092-8674(03)00036-9; Nabi et al. 2024, Physiol Mol Biol Plants, https://doi.org/10.1007/s12298-024-01452-7 (axtell2003initiationofrps2specified pages 1-1, axtell2003initiationofrps2specified pages 1-3, nabi2024patterntriggeredimmunityand pages 6-7) |
| Complexes/partners | RPS2 forms a pre-activation complex with RIN4; NDR1 associates with RIN4 and is required for full AvrRpt2/RPS2 signaling. RIN4 is a negative regulator of RPS2. | Biochemistry, genetics, cell biology | RPS2–RIN4 co-immunoprecipitation shown in planta; NDR1–RIN4 interaction depends on NDR1 N-terminus; co-IP samples collected at 24 h and 40 h after inoculation; NDR1Δ4 fails to complement ndr1-1 for AvrRpt2/RPS2 HR. | Day et al. 2005, Plant Cell, https://doi.org/10.1105/tpc.104.030163; Day et al. 2006, Plant Cell, https://doi.org/10.1105/tpc.106.044693 (day2005molecularbasisfor pages 1-2, day2006ndr1interactionwith pages 1-2, day2006ndr1interactionwith pages 4-5) |
| Localization | RPS2 is plasma membrane-associated and behaves like an integral membrane protein; it remains membrane-bound during activation/pathogenesis. RIN4 is PM-tethered by C-terminal lipidation, and AvrRpt2 is also membrane-associated. | Cell biology, biochemistry | Extraction with 1.5 M NaCl, 100 mM Na2CO3 pH 11, or 2 M urea does not release RPS2-HA, whereas 1% SDS does; RPS2 remains PM-localized at 40–48 hpi in microscopy assays. | Axtell & Staskawicz 2003, Cell, https://doi.org/10.1016/S0092-8674(03)00036-9; Alam et al. 2021, Plant Cell Reports, https://doi.org/10.1007/s00299-021-02771-9 (axtell2003initiationofrps2specified pages 4-5, axtell2003initiationofrps2specified pages 3-4, alam2021rin4homologsfrom pages 13-14) |
| Regulation / PTMs | RIN4 negatively regulates RPS2; AvrRpt2, a cysteine protease, cleaves/eliminates RIN4 to relieve suppression. RIN4 membrane tethering is required for suppression, and distinct cleavage fragments have different regulatory activities. | Biochemistry, genetics, cell biology | Estradiol-inducible Arabidopsis assays used 20 mM ED; AvrRpt2 delivered after 24 h incubation; bacterial inoculation at 10^4 CFU/mL in one assay set; >250 RIN4 mutants screened; specific C-terminal deletions and cleavage-site mutants alter RPS2 regulation. | Day et al. 2005, Plant Cell, https://doi.org/10.1105/tpc.104.030163; Alam et al. 2021, Plant Cell Reports, https://doi.org/10.1007/s00299-021-02771-9 (day2005molecularbasisfor pages 7-8, day2005molecularbasisfor pages 10-11, alam2021rin4homologsfrom pages 13-14) |
| Recent 2024 developments | 2024 work/refined reviews emphasize: (i) PTI–ETI synergy and updated NLR activation frameworks (NB-ARC switch, resistosome/helper NLR concepts); (ii) RIN4 spatial/PTM control, including T166 phosphorylation disrupting PM localization via Exo70B1; (iii) AvrRpt2-triggered ETI transcriptomics revealing conserved and spatially distinct response components. | Review, primary transcriptomics, cell biology | RIN4 phosphomimic T166D suppresses PTI similarly to exo70b1; AvrRpt2 ETI transcriptomics support two responding cell populations and PTI-like overlap. | Nabi et al. 2024, Physiol Mol Biol Plants, https://doi.org/10.1007/s12298-024-01452-7; Yu et al. 2024, Plant Biotechnol J, https://doi.org/10.1111/pbi.14332; Zhao & Day 2024, Front Plant Sci, https://doi.org/10.3389/fpls.2024.1473944; Liu et al. 2024, Plant Communications, https://doi.org/10.1016/j.xplc.2024.100882 (nabi2024patterntriggeredimmunityand pages 6-7, yu2024pti‐etisynergisticsignal pages 3-5, zhao2024subcellularspatialregulation pages 1-2, liu2024decompositionofdynamic pages 1-2) |
| Applications | RPS2 is a model system for NLR biology and informs crop resistance engineering. Broader NLR applications include ETI/effector discovery pipelines, R-gene introgression/stacking, RenSeq/AgRenSeq, promoter engineering, and even use of ETI-eliciting effectors as biocontrol in crops. | Primary applied study, review | Tomato study screened 402 expressed effector alleles from a 529-allele resource and found ETI-eliciting effectors can protect plants when delivered by non-virulent strains before or together with virulent strains. | Lonjon et al. 2024, Nat Commun, https://doi.org/10.1038/s41467-024-49425-4; Ijaz et al. 2024, Biology, https://doi.org/10.3390/biology13060421; Lee & Yeom 2015, Brief Funct Genomics, https://doi.org/10.1093/bfgp/elv012 (lonjon2024theeffectortriggeredimmunity pages 1-2, ijaz2024molecularbasisof pages 19-20, ijaz2024molecularbasisof pages 10-11, lee2015plantnblrrproteins pages 4-5) |
Table: This table summarizes verified identity, function, mechanism, localization, regulation, recent developments, and applications for Arabidopsis RPS2 using only supported evidence from the retrieved context. It is useful as a compact evidence map for functional annotation and literature-backed reporting.
References
(axtell2003initiationofrps2specified pages 1-1): Michael J. Axtell and Brian J. Staskawicz. Initiation of rps2-specified disease resistance in arabidopsis is coupled to the avrrpt2-directed elimination of rin4. Cell, 112:369-377, Feb 2003. URL: https://doi.org/10.1016/s0092-8674(03)00036-9, doi:10.1016/s0092-8674(03)00036-9. This article has 1081 citations and is from a highest quality peer-reviewed journal.
(day2005molecularbasisfor pages 1-2): Brad Day, Douglas Dahlbeck, Jeffrey Huang, Stephen T. Chisholm, Donghui Li, and Brian J. Staskawicz. Molecular basis for the rin4 negative regulation of rps2 disease resistancew⃞. The Plant Cell Online, 17:1292-1305, Apr 2005. URL: https://doi.org/10.1105/tpc.104.030163, doi:10.1105/tpc.104.030163. This article has 220 citations.
(day2006ndr1interactionwith pages 1-2): Brad Day, Douglas Dahlbeck, and Brian J. Staskawicz. Ndr1 interaction with rin4 mediates the differential activation of multiple disease resistance pathways in arabidopsis. The Plant Cell Online, 18:2782-2791, Sep 2006. URL: https://doi.org/10.1105/tpc.106.044693, doi:10.1105/tpc.106.044693. This article has 203 citations.
(yu2024pti‐etisynergisticsignal pages 3-5): Xiao‐Qian Yu, Hao‐Qiang Niu, Chao Liu, Hou‐Ling Wang, Weilun Yin, and Xinli Xia. Pti‐eti synergistic signal mechanisms in plant immunity. Plant Biotechnology Journal, 22:2113-2128, Mar 2024. URL: https://doi.org/10.1111/pbi.14332, doi:10.1111/pbi.14332. This article has 217 citations and is from a highest quality peer-reviewed journal.
(nabi2024patterntriggeredimmunityand pages 6-7): Zarka Nabi, Subaya Manzoor, Sajad Un Nabi, Tanveer Ahmad Wani, Humira Gulzar, Mehreena Farooq, Vivak M. Arya, Faheem Shehzad Baloch, Carmen Vlădulescu, Simona Mariana Popescu, and Sheikh Mansoor. Pattern-triggered immunity and effector-triggered immunity: crosstalk and cooperation of prr and nlr-mediated plant defense pathways during host-pathogen interactions. Physiology and molecular biology of plants : an international journal of functional plant biology, 30 4:587-604, Apr 2024. URL: https://doi.org/10.1007/s12298-024-01452-7, doi:10.1007/s12298-024-01452-7. This article has 67 citations.
(axtell2003initiationofrps2specified pages 1-3): Michael J. Axtell and Brian J. Staskawicz. Initiation of rps2-specified disease resistance in arabidopsis is coupled to the avrrpt2-directed elimination of rin4. Cell, 112:369-377, Feb 2003. URL: https://doi.org/10.1016/s0092-8674(03)00036-9, doi:10.1016/s0092-8674(03)00036-9. This article has 1081 citations and is from a highest quality peer-reviewed journal.
(axtell2003initiationofrps2specified pages 3-4): Michael J. Axtell and Brian J. Staskawicz. Initiation of rps2-specified disease resistance in arabidopsis is coupled to the avrrpt2-directed elimination of rin4. Cell, 112:369-377, Feb 2003. URL: https://doi.org/10.1016/s0092-8674(03)00036-9, doi:10.1016/s0092-8674(03)00036-9. This article has 1081 citations and is from a highest quality peer-reviewed journal.
(day2005molecularbasisfor pages 7-8): Brad Day, Douglas Dahlbeck, Jeffrey Huang, Stephen T. Chisholm, Donghui Li, and Brian J. Staskawicz. Molecular basis for the rin4 negative regulation of rps2 disease resistancew⃞. The Plant Cell Online, 17:1292-1305, Apr 2005. URL: https://doi.org/10.1105/tpc.104.030163, doi:10.1105/tpc.104.030163. This article has 220 citations.
(axtell2003initiationofrps2specified pages 4-5): Michael J. Axtell and Brian J. Staskawicz. Initiation of rps2-specified disease resistance in arabidopsis is coupled to the avrrpt2-directed elimination of rin4. Cell, 112:369-377, Feb 2003. URL: https://doi.org/10.1016/s0092-8674(03)00036-9, doi:10.1016/s0092-8674(03)00036-9. This article has 1081 citations and is from a highest quality peer-reviewed journal.
(alam2021rin4homologsfrom pages 13-14): Maheen Alam, Jibran Tahir, Anam Siddiqui, Mazin Magzoub, Syed Shahzad-ul-Hussan, David Mackey, and A. J. Afzal. Rin4 homologs from important crop species differentially regulate the arabidopsis nb-lrr immune receptor, rps2. Plant Cell Reports, 40:2341-2356, Sep 2021. URL: https://doi.org/10.1007/s00299-021-02771-9, doi:10.1007/s00299-021-02771-9. This article has 15 citations and is from a peer-reviewed journal.
(day2006ndr1interactionwith pages 4-5): Brad Day, Douglas Dahlbeck, and Brian J. Staskawicz. Ndr1 interaction with rin4 mediates the differential activation of multiple disease resistance pathways in arabidopsis. The Plant Cell Online, 18:2782-2791, Sep 2006. URL: https://doi.org/10.1105/tpc.106.044693, doi:10.1105/tpc.106.044693. This article has 203 citations.
(zhao2024subcellularspatialregulation pages 1-2): Yi Zhao and Brad Day. Subcellular spatial regulation of immunity-induced phosphorylation of rin4 links pamp-triggered immunity to exo70b1. Frontiers in Plant Science, Dec 2024. URL: https://doi.org/10.3389/fpls.2024.1473944, doi:10.3389/fpls.2024.1473944. This article has 1 citations.
(liu2024decompositionofdynamic pages 1-2): Xiaotong Liu, Daisuke Igarashi, Rachel A. Hillmer, Thomas Stoddard, You Lu, Kenichi Tsuda, Chad L. Myers, and Fumiaki Katagiri. Decomposition of dynamic transcriptomic responses during effector-triggered immunity reveals conserved responses in two distinct plant cell populations. Plant Communications, 5:100882, Aug 2024. URL: https://doi.org/10.1016/j.xplc.2024.100882, doi:10.1016/j.xplc.2024.100882. This article has 7 citations and is from a peer-reviewed journal.
(lonjon2024theeffectortriggeredimmunity pages 1-2): Fabien Lonjon, Yan Lai, Nasrin Askari, Niharikaa Aiyar, Cedoljub Bundalovic-Torma, Bradley Laflamme, Pauline W. Wang, Darrell Desveaux, and David S. Guttman. The effector-triggered immunity landscape of tomato against pseudomonas syringae. Nature Communications, Jun 2024. URL: https://doi.org/10.1038/s41467-024-49425-4, doi:10.1038/s41467-024-49425-4. This article has 25 citations and is from a highest quality peer-reviewed journal.
(ijaz2024molecularbasisof pages 10-11): Usman Ijaz, Chenchen Zhao, Sergey Shabala, and Meixue Zhou. Molecular basis of plant–pathogen interactions in the agricultural context. Biology, 13:421, Jun 2024. URL: https://doi.org/10.3390/biology13060421, doi:10.3390/biology13060421. This article has 13 citations.
(ijaz2024molecularbasisof pages 19-20): Usman Ijaz, Chenchen Zhao, Sergey Shabala, and Meixue Zhou. Molecular basis of plant–pathogen interactions in the agricultural context. Biology, 13:421, Jun 2024. URL: https://doi.org/10.3390/biology13060421, doi:10.3390/biology13060421. This article has 13 citations.
(day2005molecularbasisfor pages 10-11): Brad Day, Douglas Dahlbeck, Jeffrey Huang, Stephen T. Chisholm, Donghui Li, and Brian J. Staskawicz. Molecular basis for the rin4 negative regulation of rps2 disease resistancew⃞. The Plant Cell Online, 17:1292-1305, Apr 2005. URL: https://doi.org/10.1105/tpc.104.030163, doi:10.1105/tpc.104.030163. This article has 220 citations.
(lee2015plantnblrrproteins pages 4-5): Hyun-Ah Lee and Seon-In Yeom. Plant nb-lrr proteins: tightly regulated sensors in a complex manner. Briefings in functional genomics, 14 4:233-42, Jul 2015. URL: https://doi.org/10.1093/bfgp/elv012, doi:10.1093/bfgp/elv012. This article has 134 citations and is from a peer-reviewed journal.
id: Q42484
gene_symbol: RPS2
product_type: PROTEIN
status: COMPLETE
taxon:
id: NCBITaxon:3702
label: Arabidopsis thaliana
description: 'RPS2 is an Arabidopsis plasma-membrane-associated coiled-coil NB-LRR/CNL immune receptor that confers resistance to Pseudomonas syringae strains delivering AvrRpt2. Its core role is immune receptor signaling by guarding the RIN4 hub: AvrRpt2-mediated RIN4 cleavage/elimination relieves RPS2 inhibition and triggers effector-triggered immunity, hypersensitive response, and antibacterial defense. The NB-ARC domain supports nucleotide-dependent receptor switching, while generic protein-binding annotations should be interpreted through the RPS2-RIN4/NDR1 immune complex rather than as standalone molecular functions.'
existing_annotations:
- term:
id: GO:0006952
label: defense response
evidence_type: TAS
original_reference_id: PMID:11333251
review:
summary: RPS2 mediates antibacterial effector-triggered immunity, but the existing defense response term is broad.
action: MODIFY
reason: RPS2 biology is specifically AvrRpt2/Pseudomonas-triggered antibacterial immune receptor signaling; defense response to bacterium is the more precise process term.
proposed_replacement_terms:
- id: GO:0042742
label: defense response to bacterium
- term:
id: GO:0006952
label: defense response
evidence_type: TAS
original_reference_id: PMID:8091210
review:
summary: RPS2 mediates antibacterial effector-triggered immunity, but the existing defense response term is broad.
action: MODIFY
reason: RPS2 biology is specifically AvrRpt2/Pseudomonas-triggered antibacterial immune receptor signaling; defense response to bacterium is the more precise process term.
proposed_replacement_terms:
- id: GO:0042742
label: defense response to bacterium
- term:
id: GO:0009626
label: plant-type hypersensitive response
evidence_type: IMP
original_reference_id: PMID:11204781
review:
summary: RPS2 activation by AvrRpt2/RIN4 perturbation triggers hypersensitive-response outputs.
action: ACCEPT
reason: Hypersensitive response is a canonical experimentally supported output of RPS2-mediated effector-triggered immunity.
- term:
id: GO:0016045
label: detection of bacterium
evidence_type: IMP
original_reference_id: PMID:11333251
review:
summary: RPS2 detects AvrRpt2-triggered perturbation of the host RIN4 complex rather than detecting bacteria directly.
action: MODIFY
reason: The term should reflect activation of innate immunity by guarded effector-triggered RIN4 perturbation rather than generic detection of bacterium or PAMP pattern-recognition receptor signaling.
proposed_replacement_terms:
- id: GO:0002218
label: activation of innate immune response
- term:
id: GO:0042742
label: defense response to bacterium
evidence_type: IMP
original_reference_id: PMID:22331412
review:
summary: The process is appropriate for RPS2, but this cited paper is RPS5-focused and does not provide RPS2-specific support for the row.
action: REMOVE
reason: Retain RPS2 antibacterial defense through the independently supported PMID:8091210 row; remove this evidence line because the cited reference is not RPS2-centered.
- term:
id: GO:0042742
label: defense response to bacterium
evidence_type: IMP
original_reference_id: PMID:8091210
review:
summary: RPS2 confers defense against Pseudomonas syringae strains expressing AvrRpt2.
action: ACCEPT
reason: Antibacterial defense is the primary biological-process output of RPS2-mediated effector-triggered immunity.
- term:
id: GO:0005515
label: protein binding
evidence_type: IPI
original_reference_id: DOI:10.1016/j.pmpp.2005.02.006
review:
summary: RPS2 interacts with immune regulators such as RIN4 and NLR-control proteins, but generic protein binding obscures the receptor mechanism.
action: MARK_AS_OVER_ANNOTATED
reason: The informative molecular role is immune receptor activity and RIN4-guard signaling; protein binding alone is too generic for RPS2 functional curation.
- term:
id: GO:0005515
label: protein binding
evidence_type: IPI
original_reference_id: PMID:12581526
review:
summary: RPS2 interacts with immune regulators such as RIN4 and NLR-control proteins, but generic protein binding obscures the receptor mechanism.
action: MARK_AS_OVER_ANNOTATED
reason: The informative molecular role is immune receptor activity and RIN4-guard signaling; protein binding alone is too generic for RPS2 functional curation.
- term:
id: GO:0005515
label: protein binding
evidence_type: IPI
original_reference_id: PMID:19682297
review:
summary: The cached CPR30/F-box paper supports CPR30 interactions with ASK proteins and defense regulation, but not direct RPS2 binding.
action: REMOVE
reason: This IPI row lacks accessible RPS2-specific interaction support in the cited source; retain RPS2 interaction context through the RIN4-supported PMID:12581526 row instead.
supported_by:
- reference_id: PMID:19682297
supporting_text: CPR30 could interact with multiple Arabidopsis-SKP1-like (ASK) proteins in vivo
- term:
id: GO:0005515
label: protein binding
evidence_type: IPI
original_reference_id: PMID:26867179
review:
summary: RPS2 interacts with immune regulators such as RIN4 and NLR-control proteins, but generic protein binding obscures the receptor mechanism.
action: MARK_AS_OVER_ANNOTATED
reason: The informative molecular role is immune receptor activity and RIN4-guard signaling; protein binding alone is too generic for RPS2 functional curation.
- term:
id: GO:0043531
label: ADP binding
evidence_type: IEA
original_reference_id: GO_REF:0000002
review:
summary: RPS2 contains an NB-ARC nucleotide-binding module expected to function as an ADP/ATP-regulated molecular switch.
action: KEEP_AS_NON_CORE
reason: ADP binding is plausible and mechanistically relevant for the NLR switch, but the core gene-level role is immune receptor signaling rather than nucleotide binding alone.
- term:
id: GO:0002220
label: innate immune response activating cell surface receptor signaling pathway
evidence_type: EXP
original_reference_id: PMID:22331412
review:
summary: RPS2 is an intracellular CNL receptor, not a cell-surface receptor signaling component, and the cited RPS5 paper does not support this RPS2-specific row.
action: REMOVE
reason: Replace the concept in curation with cytoplasmic pattern recognition receptor signaling based on RPS2-specific evidence; this GOA row is both pathway-mismatched and citation-mismatched.
- term:
id: GO:0005737
label: cytoplasm
evidence_type: IEA
original_reference_id: GO_REF:0000044
review:
summary: RPS2 was originally characterized as acting inside plant cells and has cytoplasmic/intracellular localization support.
action: ACCEPT
reason: Cytoplasmic localization is compatible with RPS2 as an intracellular immune receptor, although later work refines this to a plasma-membrane-associated RIN4 complex.
- term:
id: GO:0005737
label: cytoplasm
evidence_type: EXP
original_reference_id: PMID:8986840
review:
summary: RPS2 was originally characterized as acting inside plant cells and has cytoplasmic/intracellular localization support.
action: ACCEPT
reason: Cytoplasmic localization is compatible with RPS2 as an intracellular immune receptor, although later work refines this to a plasma-membrane-associated RIN4 complex.
supported_by:
- reference_id: PMID:8986840
supporting_text: Mutational analysis of RPS2 protein and in vitro translation/translocation studies indicated that RPS2 protein is localized in the plant cytoplasm.
- term:
id: GO:0005886
label: plasma membrane
evidence_type: IEA
original_reference_id: GO_REF:0000044
review:
summary: RPS2 is plasma-membrane associated and remains membrane-associated during activation.
action: ACCEPT
reason: Plasma membrane localization is central to the RIN4-guard mechanism because RIN4 and AvrRpt2 act in a membrane-associated immune complex.
- term:
id: GO:0005886
label: plasma membrane
evidence_type: IDA
original_reference_id: PMID:12581526
review:
summary: RPS2 is plasma-membrane associated and remains membrane-associated during activation.
action: ACCEPT
reason: Plasma membrane localization is central to the RIN4-guard mechanism because RIN4 and AvrRpt2 act in a membrane-associated immune complex.
- term:
id: GO:0005886
label: plasma membrane
evidence_type: EXP
original_reference_id: PMID:22331412
review:
summary: RPS2 plasma-membrane association is well supported, but this RPS5-focused citation does not provide RPS2-specific support for the row.
action: REMOVE
reason: Retain plasma membrane localization through the RPS2-specific PMID:12581526/UniProt-supported rows; remove this citation-mismatched PHI-base row.
- term:
id: GO:0140375
label: immune receptor activity
evidence_type: IC
original_reference_id: file:ARATH/RPS2/RPS2-deep-research-falcon.md
review:
summary: RPS2 functions as an intracellular CNL immune receptor that senses AvrRpt2-mediated RIN4 perturbation.
action: NEW
reason: GOA captures downstream defense outputs and ADP binding but omits the core molecular role of RPS2 as an immune receptor.
additional_reference_ids:
- PMID:12581526
supported_by:
- reference_id: file:ARATH/RPS2/RPS2-deep-research-falcon.md
supporting_text: RPS2’s primary role is as a **disease resistance NLR**
- reference_id: PMID:12581526
supporting_text: RPS2 physically interacts with Arabidopsis RIN4
- term:
id: GO:0002218
label: activation of innate immune response
evidence_type: IC
original_reference_id: file:ARATH/RPS2/RPS2-deep-research-falcon.md
review:
summary: RPS2 activates intracellular effector-triggered immune signaling after AvrRpt2-mediated RIN4 cleavage/elimination.
action: NEW
reason: This broad innate-immune activation term captures guarded effector-triggered RIN4 perturbation without misclassifying RPS2 as a ligand/PAMP-binding cytoplasmic PRR.
additional_reference_ids:
- PMID:12581526
supported_by:
- reference_id: file:ARATH/RPS2/RPS2-deep-research-falcon.md
supporting_text: membrane-associated CNL sensor
- reference_id: PMID:12581526
supporting_text: RPS2 initiates signaling based upon perception of RIN4 disappearance
references:
- id: GO_REF:0000002
title: Gene Ontology annotation through association of InterPro records with GO terms
findings:
- statement: InterPro2GO mapping electronically transfers GO terms (ADP/nucleotide binding, defense response) onto RPS2 from its NB-ARC/LRR InterPro signatures; useful as breadth, not as RPS2-specific evidence.
- 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:
- statement: UniProt SubcellularLocation-to-GO mapping yields plasma membrane and cytoplasm localization terms for RPS2, consistent with its RIN4-guard role at the cytoplasmic face of the plasma membrane.
- id: PMID:11204781
title: Mutational analysis of the Arabidopsis RPS2 disease resistance gene and the corresponding pseudomonas syringae avrRpt2 avirulence gene.
findings:
- statement: RPS2 encodes an NBS-LRR resistance protein that specifically recognizes Pseudomonas syringae strains expressing avrRpt2 and initiates a hypersensitive cell death response.
supporting_text: >-
The Arabidopsis RPS2 gene encodes a protein representative of the nucleotide-binding site-leucine-rich repeat (NBS-LRR) class of plant resistance proteins. RPS2 specifically recognizes Pseudomonas syringae pv. tomato strains expressing the avrRpt2 gene and initiates defense responses to bacteria carrying avrRpt2, including a hypersensitive cell death response (HR).
- statement: Point mutations in conserved NBS and LRR motifs disrupt RPS2 resistance function, identifying these motifs as essential for the receptor's avrRpt2-triggered response.
supporting_text: >-
Ten novel rps2 alleles were characterized with mutations in the NBS and the LRR. Several of these alleles code for point mutations in motifs that are conserved among NBS-LRR resistance genes, including the third LRR, which suggests the importance of these motifs for resistance gene function.
- id: PMID:11333251
title: The leucine-rich repeat domain can determine effective interaction between RPS2 and other host factors in arabidopsis RPS2-mediated disease resistance.
findings:
- statement: RPS2 LRR polymorphisms determine effective interaction with host factors required for avrRpt2-mediated resistance.
- id: PMID:12581526
title: Initiation of RPS2-specified disease resistance in Arabidopsis is coupled to the AvrRpt2-directed elimination of RIN4.
findings:
- statement: RPS2 physically associates with RIN4 and initiates signaling when AvrRpt2 causes RIN4 elimination.
- id: PMID:19682297
title: An F-box gene, CPR30, functions as a negative regulator of the defense response in Arabidopsis.
findings:
- statement: The cached source supports CPR30 defense regulation and CPR30-ASK protein interactions, but not direct RPS2 binding.
- id: PMID:22331412
title: Structure-function analysis of the coiled-coil and leucine-rich repeat domains of the RPS5 disease resistance protein.
findings:
- statement: This citation is RPS5-centered and should not be used as direct RPS2-specific support.
- id: PMID:26867179
title: Plant TRAF Proteins Regulate NLR Immune Receptor Turnover.
findings:
- statement: TRAF proteins regulate NLR immune receptor turnover, including RPS2-associated protein interactions.
- id: PMID:8091210
title: 'RPS2 of Arabidopsis thaliana: a leucine-rich repeat class of plant disease resistance genes.'
findings:
- statement: RPS2 encodes an LRR/NBS disease-resistance protein conferring resistance to Pseudomonas syringae strains expressing avrRpt2.
- id: PMID:8986840
title: Molecular recognition of pathogen attack occurs inside of plant cells in plant disease resistance specified by the Arabidopsis genes RPS2 and RPM1.
findings:
- statement: RPS2/RPM1 recognition occurs inside plant cells, supporting intracellular localization of the recognition event.
- id: DOI:10.1016/j.pmpp.2005.02.006
title: Identification and functional analysis of Arabidopsis proteins that interact with resistance gene product RPS2 in yeast.
findings:
- statement: This source reports candidate RPS2-interacting proteins but the generic protein binding term remains too broad for core functional curation.
- id: file:ARATH/RPS2/RPS2-deep-research-falcon.md
title: Falcon deep research for Arabidopsis RPS2
findings:
- statement: RPS2 is a membrane-associated CNL immune receptor that detects AvrRpt2 activity indirectly through RIN4 cleavage/elimination.
- statement: RPS2 remains associated with a plasma-membrane RIN4 complex and triggers ETI, hypersensitive response, and restriction of Pseudomonas growth.
- id: file:ARATH/RPS2/RPS2-uniprot.txt
title: UniProt record for Arabidopsis RPS2
findings:
- statement: UniProt identifies RPS2/Q42484 as a disease resistance NB-LRR protein with cytoplasmic and cell membrane localization annotations.
- id: file:interpro/panther/PTHR33463/PTHR33463-entries.csv
title: PANTHER PTHR33463 plant disease resistance NBS-LRR family entries
findings:
- statement: PTHR33463 places Arabidopsis Q42484/RPS2 in an NB-ARC domain-containing disease-resistance protein family.
core_functions:
- description: Plasma-membrane-associated CNL immune receptor guarding RIN4. RPS2 detects AvrRpt2-mediated RIN4 cleavage/elimination at a membrane-associated immune hub and activates effector-triggered antibacterial defense and hypersensitive-response signaling.
molecular_function:
id: GO:0140375
label: immune receptor activity
directly_involved_in:
- id: GO:0002218
label: activation of innate immune response
- id: GO:0042742
label: defense response to bacterium
locations:
- id: GO:0005886
label: plasma membrane
- id: GO:0005737
label: cytoplasm
supported_by:
- reference_id: file:ARATH/RPS2/RPS2-deep-research-falcon.md
supporting_text: RPS2’s primary role is as a **disease resistance NLR**
- reference_id: PMID:12581526
supporting_text: RPS2 physically interacts with Arabidopsis RIN4
- reference_id: file:ARATH/RPS2/RPS2-deep-research-falcon.md
supporting_text: membrane-associated CNL sensor
proposed_new_terms: []
suggested_questions:
- question: Should RPS2 and related CNLs receive immune receptor activity annotations rather than only ADP binding and generic protein binding?
- question: Should PHI-base/GOA rows citing RPS5 literature for RPS2 be corrected upstream?
suggested_experiments:
- description: Reconstitute RPS2, RIN4, and AvrRpt2-controlled RIN4 cleavage states in plant membrane fractions to quantify receptor activation and nucleotide exchange.
- description: Test RPS2 NB-ARC nucleotide binding and hydrolysis states in purified or membrane-reconstituted complexes to connect ADP/ATP switching to RIN4-guard activation.