FERONIA (FER) is a plasma-membrane receptor-like protein kinase of the CrRLK1L (Catharanthus roseus RLK1-like) subfamily and a master cell-surface sensor in Arabidopsis. It has an extracellular tandem malectin-like domain that, together with GPI-anchored co-receptors of the LORELEI/LLG family, perceives secreted RALF (rapid alkalinization factor) peptide ligands, and an intracellular serine/threonine protein kinase domain (EC 2.7.11.1) that autophosphorylates and phosphorylates downstream substrates. RALF binding activates FER, which acts as an upstream regulator of RAC/ROP GTPase signaling through ROPGEFs, driving NADPH-oxidase-dependent reactive oxygen species production; FER thereby couples cell-wall integrity sensing to control of polarized cell growth (root hairs, trichomes, general cell elongation) and to inhibition of cell expansion via phosphorylation-dependent down-regulation of the plasma-membrane H+-ATPase and apoplastic alkalinization. In the female gametophyte FER accumulates asymmetrically at the synergid filiform apparatus and is essential for pollen tube reception, sperm release, and the polytubey block during fertilization, acting in heterocomplexes with the related CrRLK1Ls HERK1 and ANJEA. FER is broadly expressed (absent only in mature pollen) and serves as a signaling hub that integrates hormone responses (abscisic acid, brassinosteroid, ethylene, auxin), mechanosensing, flowering-time control, plant immunity, and powdery-mildew susceptibility. Although FER is a genuine active kinase, several of its functions (notably pollen tube reception) can be supported by kinase-inactive FER, indicating scaffolding/co-receptor roles in addition to catalysis.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0004672 protein kinase activity | IEA GO_REF:0000002 | ACCEPT | Summary: FER is a bona fide protein kinase; this is a correct molecular function, though more general than the Ser/Thr-specific terms. Reason: Correct molecular function, also supported experimentally (IDA, PMID:17673660). The more precise core MF is the receptor serine/threonine kinase activity, but the general protein kinase activity term is accurate. Supporting Evidence: file:ARATH/FER/FER-uniprot.txt RecName: Full=Receptor-like protein kinase FERONIA |
| GO:0004674 protein serine/threonine kinase activity | IEA GO_REF:0000003 | ACCEPT | Summary: FER is a serine/threonine protein kinase (EC 2.7.11.1); this is a correct and central molecular function. Reason: UniProt assigns EC 2.7.11.1 and the Ser/Thr protein kinase family; the kinase domain (536-810) with active-site Asp-661 and ATP-binding Lys-565 is experimentally validated (K565R abolishes activity). FER also autophosphorylates on Thr residues in vitro. Supporting Evidence: file:ARATH/FER/FER-uniprot.txt Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. file:ARATH/FER/FER-uniprot.txt MUTAGEN 565 |
| GO:0004714 transmembrane receptor protein tyrosine kinase activity | IEA GO_REF:0000002 | MODIFY | Summary: The receptor-kinase framing is correct, but the tyrosine specificity is wrong - FER is a serine/threonine receptor kinase, not a tyrosine kinase. Reason: This IEA derives from InterPro IPR045272 (ANXUR1/2-like) mapped through a generic Tyr/Ser-Thr catalytic-domain signature (Pfam PK_Tyr_Ser-Thr). UniProt and Rhea assign FER only Ser/Thr activity (EC 2.7.11.1), and plant CrRLK1Ls are Ser/Thr (RD) kinases. The correct receptor molecular function is transmembrane receptor protein serine/threonine kinase activity (GO:0004675), which also captures the single-pass transmembrane receptor architecture. Proposed replacements: transmembrane receptor protein serine/threonine kinase activity Supporting Evidence: file:ARATH/FER/FER-uniprot.txt Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. |
| GO:0005524 ATP binding | IEA GO_REF:0000002 | KEEP AS NON CORE | Summary: FER binds ATP as the phosphate donor for its kinase activity. Reason: Correct cofactor-binding function supporting the kinase activity; FER has a defined ATP-binding site (residues 542-550 and Lys-565). Standard supporting MF for an active kinase rather than a core distinguishing function. Supporting Evidence: file:ARATH/FER/FER-uniprot.txt /ligand="ATP" |
| GO:0005886 plasma membrane | IEA GO_REF:0000120 | ACCEPT | Summary: Plasma membrane is the correct and core subcellular location of this single-pass receptor kinase. Reason: FER is a single-pass type I plasma-membrane protein, confirmed by multiple IDA/HDA studies; the electronic localization agrees with experiment. Supporting Evidence: file:ARATH/FER/FER-uniprot.txt Single-pass type I membrane protein |
| GO:0106310 protein serine kinase activity | IEA GO_REF:0000116 | KEEP AS NON CORE | Summary: Consistent with FER being a Ser/Thr kinase; RALF-activated FER is phosphorylated on serines and autophosphorylates. Reason: Rhea-based electronic annotation for the serine-directed half of the Ser/Thr kinase reaction. Correct and supported (FER phosphosites Ser-858/871/874), but redundant with the broader serine/threonine kinase term that is the core MF. Supporting Evidence: file:ARATH/FER/FER-uniprot.txt Phosphorylated at Ser-858, Ser-871 and Ser-874 upon activation by RALF1. |
| GO:0005515 protein binding | IPI PMID:20876100 FERONIA receptor-like kinase regulates RHO GTPase signaling ... | KEEP AS NON CORE | Summary: Captures the FER-ROPGEF1 (and ROP2) interaction underlying RAC/ROP-ROS signaling, but the bare "protein binding" term is uninformative. Reason: The interactions with ROPGEF1/ROP GTPase are biologically central, but GO:0005515 does not convey the upstream regulator-of-RAC/ROP function. The informative function is captured in core_functions (cell-surface regulator of RAC/ROP-NADPH oxidase ROS signaling). Per curation guidelines, bare protein binding is not retained as core. Supporting Evidence: PMID:20876100 FER was pulled down by ROP2 GTPase in a guanine nucleotide-regulated manner |
| GO:0005515 protein binding | IPI PMID:24458638 A peptide hormone and its receptor protein kinase regulate p... | KEEP AS NON CORE | Summary: Records the FER-RALF1 ligand-receptor interaction, but the bare term hides that RALF1 is FER's activating peptide ligand. Reason: This IPI is to RALF1 (UniProtKB:Q9SRY3), the secreted peptide ligand that binds and activates FER. The functionally meaningful annotation is RALF peptide ligand binding / receptor activation (see core_functions), not generic protein binding. Supporting Evidence: PMID:24458638 specific binding of RALF to FERONIA |
| GO:0005515 protein binding | IPI PMID:31867824 CrRLK1L receptor-like kinases HERK1 and ANJEA are female det... | KEEP AS NON CORE | Summary: Captures FER interaction with the CrRLK1L co-receptors HERK1 and ANJEA (and LRE) that form pollen-tube-reception heterocomplexes. Reason: Real and relevant (FER-HERK1/ANJ-LRE complexes at the filiform apparatus), but the bare term is uninformative; the function is reflected in the pollen tube reception annotations and core_functions. Supporting Evidence: PMID:31867824 Both ANJ and HERK1 associate with FER and its proposed co-receptor LORELEI (LRE) in planta |
| GO:0005515 protein binding | IPI PMID:40323783 RALF33-FERONIA signaling orchestrates postwounding root-tip ... | KEEP AS NON CORE | Summary: Captures the FER-TPR4 interaction in RALF33-FER signaling controlling wound-induced root-tip regeneration. Reason: Specific downstream interaction (FER phosphorylates TPR4 in a RALF33 module), relevant to a non-core regeneration process; bare protein binding is uninformative. Supporting Evidence: PMID:40323783 hinders FER-mediated phosphorylation of the transcriptional co-repressor TOPLESS-RELATED4 (TPR4) |
| GO:0005515 protein binding | IPI PMID:40348341 FERONIA interacts with NPL4 to regulate immunity gene mRNA n... | KEEP AS NON CORE | Summary: Captures FER-NPL4 interaction linking RALF-FER signaling to immunity-gene mRNA nucleocytoplasmic transport. Reason: Specific downstream immunity-related interaction; relevant but non-core, and bare protein binding is uninformative. Supporting Evidence: PMID:40348341 FER displays functional interactions with NPL4 |
| GO:0005515 protein binding | IPI PMID:35050671 RALF peptide signaling controls the polytubey block in Arabi... | KEEP AS NON CORE | Summary: Captures FER interaction with pollen-tube RALF6/7/16/36/37 peptides that establish the polytubey block. Reason: These are RALF peptide ligand interactions (a core ligand-binding theme) in the specific context of preventing polytubey/polyspermy; the bare term is uninformative and the function is reflected in core_functions and the reproduction annotations. Supporting Evidence: PMID:35050671 FERONIA, ANJEA, and HERCULES RECEPTOR KINASE 1 receptor-like kinases located at the septum interact with pollen tube-specific RALF6, 7, 16, 36, and 37 peptide ligands |
| GO:0005515 protein binding | IPI PMID:36527240 CAR modulates plasma membrane nano-organization and immune s... | KEEP AS NON CORE | Summary: Captures FER interaction with C2-domain ABA-related (CAR) proteins that organize PM nanodomains downstream of RALF1-FER. Reason: Specific downstream interaction relevant to PM nano-organization and immune signaling; relevant but non-core, and bare protein binding is uninformative. Supporting Evidence: PMID:36527240 FER ... physically interacts with C2 domain ABA-related (CAR) proteins to control the nano-organization of the PM |
| GO:0005515 protein binding | IPI PMID:36053485 Identification of Feronia-interacting proteins in Arabidopsi... | KEEP AS NON CORE | Summary: Captures Y2H/BiFC FER interactions with ARM-repeat, PUB9, IQD7 and HGL1 proteins as candidate intracellular signaling partners. Reason: Interaction-screen partners of uncertain functional weight; relevant but non-core, and bare protein binding is uninformative. Supporting Evidence: PMID:36053485 BiFC confirmed the in vivo interactions between these four proteins and AtFER |
| GO:0005886 plasma membrane | HDA PMID:14506206 Large-scale analysis of in vivo phosphorylated membrane prot... | ACCEPT | Summary: High-throughput PM phosphoproteomics localizing FER to the plasma membrane; consistent with its core PM location. Reason: PM proteomics detection agrees with the established single-pass PM localization of FER. This study also identified the FER phosphosite Ser-866. Supporting Evidence: file:ARATH/FER/FER-uniprot.txt Single-pass type I membrane protein |
| GO:0005886 plasma membrane | HDA PMID:17644812 A high content in lipid-modified peripheral proteins and int... | ACCEPT | Summary: PM proteomics of receptor kinases localizing FER to the plasma membrane; consistent with its core location. Reason: Plasma-membrane proteome study detecting FER among integral receptor kinases; corroborates the established PM localization. Supporting Evidence: file:ARATH/FER/FER-uniprot.txt Cell membrane {ECO:0000269|PubMed:17673660, |
| GO:0005886 plasma membrane | HDA PMID:22923678 Putative glycosyltransferases and other plant Golgi apparatu... | ACCEPT | Summary: LOPIT spatial-proteomics detection assigning FER to the plasma membrane; consistent with its core location. Reason: Spatial proteomics (LOPIT) detection corroborates PM localization of FER. Supporting Evidence: file:ARATH/FER/FER-uniprot.txt Single-pass type I membrane protein |
| GO:0009506 plasmodesma | HDA PMID:21533090 Arabidopsis plasmodesmal proteome. | KEEP AS NON CORE | Summary: Detected in a plasmodesmal proteome; plausible since the PM is continuous through plasmodesmata, but not a core functional location. Reason: High-throughput plasmodesmal proteomics detection. FER is a PM protein and plasmodesmal pores are PM-lined, so detection is plausible, but there is no functional evidence for a plasmodesma-specific role. Retain as non-core. Supporting Evidence: PMID:21533090 Arabidopsis plasmodesmal proteome |
| GO:0032922 circadian regulation of gene expression | IEP PMID:31948398 Receptor kinase FERONIA regulates flowering time in Arabidop... | KEEP AS NON CORE | Summary: FER expression oscillates diurnally (driven by CCA1) and fer mutants alter clock-gene expression patterns; a non-core regulatory linkage. Reason: Supported by expression-pattern (IEP) evidence that FER is clock-regulated and feeds back on clock-gene amplitude/period, linked to flowering-time control. This is a peripheral regulatory role, not a core FER function. Supporting Evidence: PMID:31948398 FER mRNA levels exhibit an oscillating pattern with a diurnal rhythm and that the clock oscillator CIRCADIAN CLOCK-ASSOCIATED1 (CCA1) up-regulates the expression of FER |
| GO:0005576 extracellular region | ISM GO_REF:0000122 | MARK AS OVER ANNOTATED | Summary: Misleading whole-protein localization prediction; FER is an integral single-pass plasma-membrane protein, not a secreted/extracellular protein. Reason: This is an electronic subcellular-localization prediction (AtSubP, GO_REF:0000122). FER has a large extracellular malectin-like ectodomain but is anchored in the plasma membrane via a transmembrane helix; "extracellular region" as the cellular location overstates the prediction. Plasma membrane is the correct, experimentally supported location. Supporting Evidence: file:ARATH/FER/FER-uniprot.txt Single-pass type I membrane protein |
| GO:0010118 stomatal movement | IGI PMID:29301953 The G Protein Ξ²-Subunit, AGB1, Interacts with FERONIA in RAL... | KEEP AS NON CORE | Summary: FER acts with the G-protein beta subunit AGB1 in RALF1-regulated stomatal aperture control; a non-core physiological role. Reason: Genetic-interaction (IGI with AGB1) evidence that RALF1-FER, via heterotrimeric G proteins, regulates stomatal opening/closure. A legitimate but peripheral guard-cell function relative to FER's core cell-surface signaling role. Supporting Evidence: PMID:29301953 RALF1 regulates stomatal apertures and does so in a G protein-dependent manner |
| GO:0005886 plasma membrane | IDA PMID:29042459 Environmental and Genetic Factors Regulating Localization of... | ACCEPT | Summary: Direct-assay plasma-membrane localization of FER; corroborates the core PM location. Reason: IDA plasma-membrane localization, consistent with all other lines of evidence that FER is a single-pass PM receptor kinase. Supporting Evidence: file:ARATH/FER/FER-uniprot.txt Single-pass type I membrane protein |
| GO:0005515 protein binding | IPI PMID:26052747 Glycosylphosphatidylinositol-anchored proteins as chaperones... | KEEP AS NON CORE | Summary: Captures the FER interaction with GPI-anchored co-receptors LLG1 and LRE (LORELEI), essential for FER trafficking and signaling. Reason: Functionally important interaction (LLG1/LRE bind the FER extracellular juxtamembrane region, control FER ER-to-PM transport, and are part of the RAC/ROP signaling complex), but the bare protein binding term is uninformative. The co-receptor relationship is reflected in core_functions. Supporting Evidence: PMID:26052747 LLG1) bind to the extracellular juxtamembrane region of FER |
| GO:0009788 negative regulation of abscisic acid-activated signaling pathway | IMP PMID:22908257 FERONIA receptor kinase pathway suppresses abscisic acid sig... | KEEP AS NON CORE | Summary: FER suppresses ABA signaling via the ROPGEF-ROP11/ARAC10-ABI2 module; fer mutants are ABA-hypersensitive. Reason: Well-supported by mutant analysis (IMP); the FER-GEF1/4/10-ROP11-ABI2 pathway down-regulates ABA responses. A genuine signaling output but one of several hormone-crosstalk roles, hence non-core relative to the cell-wall-integrity and RAC/ROP-ROS core. Supporting Evidence: PMID:22908257 suppress the abscisic acid (ABA) response through activation of ABI2 |
| GO:0030308 negative regulation of cell growth | IMP PMID:24458638 A peptide hormone and its receptor protein kinase regulate p... | ACCEPT | Summary: RALF1-activated FER inhibits cell expansion by phosphorylating and down-regulating the PM H+-ATPase (AHA2), raising apoplastic pH; a core output. Reason: Strong mutant and biochemical evidence (IMP) that FER mediates RALF-induced suppression of root cell elongation via AHA2 inhibition. This negative regulation of cell expansion is a defining cell-wall-integrity output of FER signaling. Supporting Evidence: PMID:24458638 a secreted peptide, RALF (rapid alkalinization factor), suppresses cell elongation of the primary root by activating the cell surface receptor FERONIA file:ARATH/FER/FER-deep-research-falcon.md FER is required for cellular responses to RALF1, a peptide that triggers extracellular alkalinization and growth inhibition. |
| GO:0048364 root development | IMP PMID:24458638 A peptide hormone and its receptor protein kinase regulate p... | KEEP AS NON CORE | Summary: fer mutants have altered root growth (longer roots, RALF1 insensitivity); a broad developmental term reflecting FER's role in root cell elongation. Reason: Supported by mutant phenotypes, but "root development" is a broad process term; the mechanistic, core FER function is the RALF-FER control of root cell expansion (captured by negative regulation of cell growth and core_functions). Supporting Evidence: PMID:24458638 The roots of both fer4 and ralf loss-of-function mutants were longer than wild-type roots |
| GO:0009723 response to ethylene | IMP PMID:20400488 FERONIA is a key modulator of brassinosteroid and ethylene r... | KEEP AS NON CORE | Summary: fer mutants show altered ethylene responsiveness in hypocotyl elongation; a hormone-crosstalk role, non-core. Reason: Supported by mutant analysis showing FER modulates ethylene responsiveness (fer-2 has heightened ethylene response). Legitimate but peripheral to FER's core cell-surface signaling function. Supporting Evidence: PMID:20400488 extreme responsiveness to even low levels of ethylene |
| GO:0009741 response to brassinosteroid | IMP PMID:20400488 FERONIA is a key modulator of brassinosteroid and ethylene r... | KEEP AS NON CORE | Summary: fer mutants show altered brassinosteroid responsiveness in hypocotyls; a hormone-crosstalk role, non-core. Reason: Supported by mutant analysis (etiolated fer-2 is partially BR-insensitive); FER is also transcriptionally induced by BR and acts with HERK1/THE1 in a largely BR-independent cell-elongation pathway. A peripheral hormone-response role. Supporting Evidence: PMID:20400488 etiolated fer-2 seedlings being partially brassinosteroid insensitive with regard to promotion of hypocotyl elongation |
| GO:0010483 pollen tube reception | IMP PMID:21071669 Conserved molecular components for pollen tube reception and... | ACCEPT | Summary: FER controls pollen tube reception in synergids; loss causes pollen tube overgrowth and failed fertilization. A core reproductive function. Reason: Repeatedly demonstrated by mutant analysis (IMP) that FER is required in the female gametophyte for pollen tube arrest and sperm release, including control of NORTIA/MLO relocalization. This is a defining FER function. Supporting Evidence: PMID:21071669 both control PT reception in synergids |
| GO:0043680 filiform apparatus | IDA PMID:21071669 Conserved molecular components for pollen tube reception and... | ACCEPT | Summary: FER accumulates at the synergid filiform apparatus, the site of pollen tube reception; a specific functional localization. Reason: Direct imaging (IDA) shows asymmetric FER accumulation at the filiform apparatus, directly tied to its pollen-tube-reception function. Specific and well-supported subcellular location. Supporting Evidence: file:ARATH/FER/FER-uniprot.txt Accumulates asymmetrically in the female gametophyte synergid membrane at the filiform apparatus. |
| GO:0050832 defense response to fungus | IMP PMID:21071669 Conserved molecular components for pollen tube reception and... | KEEP AS NON CORE | Summary: fer mutants are resistant to powdery mildew, i.e. FER normally promotes susceptibility to this fungus; captured by a broad defense term with an acts_upstream qualifier. Reason: Supported by mutant analysis (IMP) that loss of FER confers powdery-mildew resistance, revealing FER as a susceptibility factor. The broad term plus the acts_upstream_of_or_within qualifier captures the regulatory linkage. A non-core, immunity-related role; note the directionality (FER promotes susceptibility) is opposite to a classic defensive function. Supporting Evidence: PMID:21071669 Homozygous fer mutants also display PM resistance, revealing a new function for FER |
| GO:0009791 post-embryonic development | IMP PMID:19383785 Three related receptor-like kinases are required for optimal... | KEEP AS NON CORE | Summary: fer RNAi mutants are dwarfed due to impaired cell elongation during vegetative growth; a broad developmental term. Reason: Supported by mutant analysis showing FER is required for optimal cell elongation (with HERK1/THE1). "Post-embryonic development" is a very general process term; the mechanistic core is cell-wall-integrity/cell-expansion control. Supporting Evidence: PMID:19383785 fer RNAi mutants displayed striking dwarf phenotypes |
| GO:0010483 pollen tube reception | IMP PMID:17673660 The FERONIA receptor-like kinase mediates male-female intera... | ACCEPT | Summary: The original FER characterization; fer synergids fail to arrest the pollen tube, which overgrows. Core reproductive function. Reason: Foundational mutant evidence (IMP) that FER mediates female control of pollen tube reception. Independent support for the core reproductive role. Supporting Evidence: PMID:17673660 the pollen tube fails to arrest and thus continues to grow inside the female gametophyte file:ARATH/FER/FER-deep-research-falcon.md In a large fraction of fer mutant female gametophytes, the penetrated pollen tube |
| GO:0004672 protein kinase activity | IDA PMID:17673660 The FERONIA receptor-like kinase mediates male-female intera... | ACCEPT | Summary: Direct demonstration of FER kinase activity; the kinase-dead K565R mutant loses activity. Core molecular function (though general term). Reason: Experimental (IDA) confirmation that FER is an active protein kinase. FER is a genuine active kinase, though some signaling outputs (e.g. pollen tube reception) are kinase-independent/scaffolding. The Ser/Thr-specific term is the most precise core MF. Supporting Evidence: file:ARATH/FER/FER-uniprot.txt MUTAGEN 565 |
| GO:0005886 plasma membrane | IDA PMID:17673660 The FERONIA receptor-like kinase mediates male-female intera... | ACCEPT | Summary: Direct demonstration that FER is a plasma-membrane-localized receptor kinase. Core location. Reason: IDA localization in the foundational FER paper; consistent with all other evidence for PM localization. Supporting Evidence: PMID:17673660 plasma membrane-localized receptor-like kinase |
| GO:0043680 filiform apparatus | IDA PMID:17673660 The FERONIA receptor-like kinase mediates male-female intera... | ACCEPT | Summary: Original demonstration that FER accumulates asymmetrically at the synergid filiform apparatus, the site of pollen tube reception. Reason: Foundational IDA localization tied directly to FER's pollen-tube-reception function; specific and well-supported. Supporting Evidence: file:ARATH/FER/FER-uniprot.txt Accumulates asymmetrically in the female gametophyte synergid membrane at the filiform apparatus. file:ARATH/FER/FER-deep-research-falcon.md In ovules, FER-GFP localizes prominently at the filiform apparatus |
| GO:0046777 protein autophosphorylation | IDA PMID:17673660 The FERONIA receptor-like kinase mediates male-female intera... | ACCEPT | Summary: FER autophosphorylates; a direct biochemical activity central to its function as an active receptor kinase. Reason: Direct experimental evidence (IDA) of FER autophosphorylation, also seen in cell-free assays and on Thr residues (T559/T664). Autophosphorylation is a hallmark of FER's active receptor-kinase function and contributes to RALF-induced activation. Supporting Evidence: file:ARATH/FER/FER-uniprot.txt Autophosphorylated. |
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Download this section (compressed HTML)Q: Which RALF peptide(s) and cell-wall ligands activate FER in each biological context (root cell expansion, root hair growth, pollen tube reception, immunity), and how is signaling specificity achieved through different LLG/LRE co-receptors?
Suggested experts: Plant peptide-signaling researchers, CrRLK1L receptor biologists
Q: Which FER functions require catalytic kinase activity versus scaffolding, and what are the bona fide in vivo phosphorylation substrates of FER beyond AHA2?
Suggested experts: Plant receptor-kinase biochemists, Phosphoproteomics specialists
Q: How does FER mechanistically convert cell-wall perturbation into RAC/ROP-ROS output, and what role does the malectin-like domain's pectin/polygalacturonic-acid binding play?
Suggested experts: Cell-wall integrity signaling researchers
Experiment: Complement fer-4 with kinase-dead (K565R) versus wild-type FER and quantitatively assay pollen tube reception/sperm release, micropylar ROS, and RALF1-induced root growth inhibition and AHA2 phosphorylation in parallel.
Hypothesis: FER's pollen-tube-reception function is kinase-independent (scaffolding) whereas its RALF-induced root growth inhibition requires catalytic activity.
Experiment: Use purified FER ectodomain binding assays against defined pectin fragments (polygalacturonic acid, de-/methyl-esterified) combined with in planta ROS imaging after enzymatic cell-wall modification in wild-type versus fer mutants.
Hypothesis: FER directly senses cell-wall pectin status via its malectin-like domain to trigger RAC/ROP-ROS signaling.
Experiment: Reconstitute FER with LLG1, LLG2/3, or LRE in protoplasts/heterologous systems and measure binding and signaling responses to a panel of RALF peptides.
Hypothesis: Distinct LLG/LRE co-receptors define FER ligand specificity and tissue- specific outputs.
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