RPS2

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

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

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.

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

Summary: Antibacterial defense is the primary biological-process output of RPS2; the cited RPS5 structure-function paper experimentally used RPS2 domains.

Reason: Defense response to bacterium is unambiguously correct for RPS2, and PMID:22331412 is not a citation mismatch - its abstract describes chimera experiments substituting the RPS2 CC and LRR domains into RPS5. The cached record is abstract-only, so the RPS2-specific data the curator used cannot be inspected here; an experimental annotation for a clearly correct core function should be deferred to, not removed.

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.

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.

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.

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.

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.

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.

Summary: RPS2 is an intracellular CC-NBS-LRR receptor; the immune-activation claim is sound but the cell-surface receptor pathway term is the wrong receptor class.

Reason: The essence of the annotation (RPS2 activates innate immune signaling upon effector recognition) is correct, and PMID:22331412 did assay RPS2 domains in RPS5 chimeras, so this is not a citation mismatch. However, RPS2 perceives AvrRpt2-triggered RIN4 perturbation intracellularly rather than at the cell surface, and it acts as a guard rather than as a ligand/PAMP-binding pattern-recognition receptor, so a receptor-class-neutral innate-immune-activation term is the accurate replacement for the cell-surface receptor pathway term. This matches the replacement proposed for the GO:0016045 row, which rejects PRR framing for RPS2 on the same grounds.

Proposed replacements: activation of innate immune response

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.

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.

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.

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.

Summary: RPS2 plasma-membrane association is well supported, and the cited RPS5 structure-function paper experimentally used RPS2 domains.

Reason: Plasma membrane localization is correct for RPS2 (independently supported by PMID:12581526 and UniProt), and PMID:22331412 is not a citation mismatch - its abstract describes chimera experiments substituting RPS2 CC and LRR domains into RPS5. The cached record is abstract-only, so the RPS2-specific localization data the curator used cannot be inspected here; an experimental annotation for a clearly correct localization should be deferred to, not removed.

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.

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.