Gene Research for GO Annotation Review

Target

• Gene symbol: FER
• Organism: Arabidopsis thaliana

UniProt Context

=== UNIPROT METADATA ===
UniProt ID: Q9SCZ4
Entry Name: FERON_ARATH
Gene Name: FER
Locus Tag: At3g51550 {ECO:0000312|Araport:AT3G51550}
Gene Synonyms: AAK1, SIR {ECO:0000303|PubMed:12620194}, SRN
Protein Name: Receptor-like protein kinase FERONIA
EC Number: 2.7.11.1
Organism: Arabidopsis thaliana (Mouse-ear cress)
NCBI Taxonomy ID: 3702
Function: Receptor-like protein kinase that mediates the female control of male gamete delivery during fertilization, including growth cessation of compatible pollen tubes ensuring a reproductive isolation barriers, by regulating MLO7 subcellular polarization upon pollen tube perception in the female gametophyte synergids. Required for cell elongation during vegetative growth, mostly in a brassinosteroids- (BR-) independent manner. Acts as an upstream regulator for the Rac/Rop-signaling pathway that controls ROS-mediated root hair development. Seems to regulate a cross-talk between brassinosteroids and ethylene signaling pathways during hypocotyl elongation. Negative regulator of brassinosteroid response in light- grown hypocotyls, but required for brassinosteroid response in etiolated seedlings. Mediates sensitivity to powdery mildew (e.g. Golovinomyces orontii). Positive regulator of auxin-promoted growth that represses the abscisic acid (ABA) signaling via the activation of ABI2 phosphatase. Required for RALF1-mediated extracellular alkalinization in a signaling pathway preventing cell expansion.
Subcellular Location: Cell membrane
Subunit: Interacts with ROPGEF1 (PubMed:20876100). Interacts with RALF1; triggering phosphorylation status and subsequent activation (PubMed:24458638). Interacts with LRE and LLG1 (PubMed:26052747). Interacts, via its extracellular domain, with FERONIA at the synergid cell surface (PubMed:27524487).
======================

Research Objective

Prepare a comprehensive literature-backed research report for GO annotation review of the target gene.

Focus on:

1. The core biochemical activity of the gene product and any substrate specificity.
2. The activation or maturation mechanism of the protein, including proteolytic processing if relevant.
3. The best-supported subcellular localization and complexes where the active protein functions.
4. The strongest experimentally supported biological processes in the target organism, or in very close orthologs when transfer is justified.
5. Which annotations appear to reflect core function versus context-specific, pleiotropic, or over-extended roles.
6. Any evidence bearing on apoptosis, developmental cell death, neuronal roles, inflammatory signaling, pyroptosis, synaptic remodeling, protein processing, and localization to cytoplasm, cytosol, nucleus, or signaling complexes.

Output Requirements

Structure the report as:

1. Executive summary
2. Molecular function
3. Biological process roles
4. Cellular localization and complexes
5. Annotation-risk assessment
6. Key literature

Use citations for all substantive claims.

Gene Research Report for GO Annotation Review

Target

• Gene symbol: FER (FERONIA)
• Organism: Arabidopsis thaliana
• UniProt: Q9SCZ4 (FERONIA_ARATH)

1. Executive summary

FERONIA (FER) is a plasma-membrane (cell-surface) malectin-like receptor kinase of the CrRLK1L family that functions in extracellular peptide perception and cell-wall–coupled signaling. The best-supported core role in Arabidopsis is in female-controlled pollen tube reception, where FER in synergid cells is required for pollen tube bursting/rupture and sperm release, and mutants show strong, quantifiable fertility defects (e.g., ~80% of fer female gametophytes fail to trigger pollen-tube bursting; fer/fer plants produce ~20% of wild-type seed set) (cheung2024feroniaareceptor pages 3-4).

Mechanistically, FER forms a cell-surface coreceptor complex with LORELEI/LLG-family GPI-anchored proteins and binds RALF peptides; structural work (summarized in a 2024 Annual Review) includes a solved RALF23–LLG2–FER extracellular heterocomplex (cheung2024feroniaareceptor pages 8-9, cheung2024feroniaareceptor pages 31-36). Downstream, FER couples to ROPGEFs → RAC/ROP GTPases → NADPH oxidase–dependent ROS that are required for tip growth and cell integrity, supporting roles in root hair development/integrity and ROS-associated growth control (li2016feroniaandher pages 4-5, cheung2024feroniaareceptor pages 31-36).

Recent (2024) mechanistic work adds regulation of FER kinase activity by a phosphatase: the clade-H PP2C PP2C12 binds FER and dephosphorylates its activation-loop Thr696, tuning RALF1 sensitivity and root hair phenotypes (preprint evidence; quantitative assays n>100 per genotype, ANOVA P<0.01) (hou2024thephosphatasepp2c12 pages 9-14).

FER is also repeatedly described as pleiotropic, with context-dependent roles in ABA and salt-stress responses and in immunity; these are supported by phenotypes and pathway associations but are higher risk for over-broad GO biological-process annotations compared with the core reproductive and RALF/ROS tip-growth modules (cheung2024feroniaareceptor pages 3-4, cheung2024feroniaareceptor pages 31-36).

2. Molecular function

2.1 Key concepts and definitions (current understanding)

Receptor-like protein kinase / Ser/Thr kinase: FER is a single-pass transmembrane receptor kinase with a cytosolic Ser/Thr kinase domain (minkoff2017acellfreemethod pages 1-2). The 2024 review explicitly notes FER’s self-phosphorylation and places it as a signaling hub in cell-surface perception modules (cheung2024feroniaareceptor pages 1-3).

Malectin-like extracellular domains: FER contains tandem malectin-like domains (MALA/MALB). Canonical carbohydrate-binding residues are not conserved, but the domain architecture is consistent with a role in binding peptide ligands and possibly cell-wall–associated cues (cheung2024feroniaareceptor pages 3-4, cheung2024feroniaareceptor pages 8-9).

RALF peptides: RAPID ALKALINIZATION FACTOR peptides are secreted peptides that can induce extracellular alkalinization and growth changes. FER is one of the best-characterized RALF receptors, especially for RALF1 and RALF23 in reviewed literature (cheung2024feroniaareceptor pages 3-4).

LLG/LRE co-receptors (GPI-anchored proteins): LORELEI (LRE) and LLG1 are GPI-anchored proteins that act as chaperones and co-receptors, promoting FER plasma-membrane delivery and functioning in FER signaling complexes (li2015glycosylphosphatidylinositolanchoredproteinsas pages 1-2, li2015glycosylphosphatidylinositolanchoredproteinsas pages 8-11).

2.2 Core biochemical activity and substrate specificity

Kinase activity: FER has demonstrable protein kinase activity. In vitro reconstitution in lipid nanodiscs increased FER kinase activity versus soluble protein, and active-site residues (K565, K663) coordinating ATP were identified by ATP-analog labeling and mutagenesis (Minkoff et al., Apr 2017, JBC; https://doi.org/10.1074/jbc.m116.761981) (minkoff2017acellfreemethod pages 1-2).

In vivo targets/substrates: The retrieved primary excerpts provide strong pathway placement (e.g., ROPGEF/ROP signaling; RALF-induced receptor phosphorylation), but limited direct in vivo substrate mapping. The 2024 review summarizes that FER phosphorylates multiple targets including PhyB, and transcription factors MYC2 and ABI5, affecting nuclear accumulation/stability of these targets; however, these are summarized statements rather than assay details in the excerpts provided here (cheung2024feroniaareceptor pages 18-19).

Regulatory phosphosites: A 2024 preprint demonstrates biochemical regulation of FER phosphorylation state: PP2C12 dephosphorylates FER’s cytoplasmic domain in vitro and phosphoproteomics implicates Thr696 in the FER activation loop as a PP2C12-sensitive site (Hou et al., Nov 2024, bioRxiv; https://doi.org/10.1101/2024.11.05.622083) (hou2024thephosphatasepp2c12 pages 9-14). This provides unusually direct, site-level evidence relevant to kinase regulation.

2.3 Ligand binding and activation mechanism

RALF binding: Multiple lines of evidence support FER as a RALF receptor. RALF1 binds directly to the FER extracellular domain and RALF1 treatment enhances FER phosphorylation at C-terminal Ser residues (li2016feroniaandher pages 4-5). RALF1 association with a FER–LLG1 complex is supported by MBP-RALF1 pull-down capturing coexpressed FER and LLG1 (li2015glycosylphosphatidylinositolanchoredproteinsas pages 11-13). Structural evidence summarized in 2024 includes a solved RALF23–LLG2–FER extracellular heterocomplex, supporting a tripartite ligand–co-receptor–receptor activation architecture (cheung2024feroniaareceptor pages 8-9).

Co-receptor dependence and trafficking as part of activation competence: LLG1/LRE are pivotal for FER to reach the plasma membrane and signal. Loss of LLG1 causes FER-GFP retention in ER-like reticulate/perinuclear structures; co-expression of GPI-anchored LLG1 restores membrane localization, while a GPI-anchor–defective LLG1ΔC is much less effective (li2015glycosylphosphatidylinositolanchoredproteinsas pages 8-11). These data support that complex formation and trafficking are integral to functional receptor availability at the cell surface.

Proteolytic processing/maturation: No evidence in the retrieved excerpts supports proteolytic processing or maturation of FER itself (no receptor cleavage/ectodomain shedding/propeptide removal reported) (cheung2024feroniaareceptor pages 3-4, cheung2024feroniaareceptor pages 31-36).

3. Biological process roles

3.1 Strongest experimentally supported core processes

Pollen tube reception and sperm release (female fertility)

FER is a founding factor required for male–female communication at fertilization. In a large fraction of fer mutant female gametophytes, the penetrated pollen tube fails to burst, preventing sperm release and fertilization (cheung2024feroniaareceptor pages 3-4). Quantitative phenotypes summarized in the 2024 Annual Review include:
- ~80% of fer mutant female gametophytes: pollen tube fails to burst (cheung2024feroniaareceptor pages 3-4).
- Self-fertilized fer/fer plants produce ~20% of wild-type seed set (cheung2024feroniaareceptor pages 3-4).
- ~80% of ovules from fer/fer plants are sterile (cheung2024feroniaareceptor pages 3-4).

This is the single best-supported biological process annotation candidate for FER.

Root hair development / tip growth integrity and ROS signaling

FER is a key regulator of polarized growth processes, particularly root hairs. Loss of FER (and of LLG1) causes emerging root hairs to extrude cytoplasm and collapse, consistent with weakened cell wall/integrity (li2015glycosylphosphatidylinositolanchoredproteinsas pages 8-11). FER functions upstream of RAC/ROP activation and is required for NADPH oxidase–dependent ROS production, linking it to ROS-mediated growth and integrity (li2016feroniaandher pages 4-5, cheung2024feroniaareceptor pages 31-36).

RALF1-mediated growth inhibition and extracellular alkalinization

FER is required for cellular responses to RALF1, a peptide that triggers extracellular alkalinization and growth inhibition. fer mutants are described as RALF-insensitive in this context, and RALF1 induces FER phosphorylation changes (wolf2014growthcontrola pages 1-2, li2016feroniaandher pages 4-5). A 2024 preprint further ties RALF1 sensitivity to FER phosphorylation-state regulation by PP2C12 (hou2024thephosphatasepp2c12 pages 9-14).

3.2 Context-specific / pleiotropic processes (supported but higher GO-annotation risk)

ABA-related phenotypes

FER intersects with ABA-associated pathways: fer seedlings are hypersensitive to ABA-suppressed seedling growth and are defective in stomatal aperture closure regulation (cheung2024feroniaareceptor pages 3-4). This supports an ABA-response role, but its mechanistic proximity to core receptor function is less direct than in reproduction and RALF response.

Salt stress response

FER buffers high-salinity stress; under high salt conditions fer seedlings show root cell bursting and arrested root growth (cheung2024feroniaareceptor pages 31-36). This phenotype is robust but likely emerges from the broader cell-wall integrity and ROS signaling network, so GO terms should be chosen carefully to avoid implying FER is a dedicated salt sensor.

Immunity modulation

FER is implicated in immune outputs, including altered flg22-triggered ROS/MAPK responses and pathogen susceptibility patterns, as summarized in older reviews/perspectives and in pleiotropy discussions (wolf2014growthcontrola pages 1-2, li2016feroniaandher pages 2-4). However, immune-related annotations are particularly prone to over-extension because FER may modulate immunity indirectly through cell-wall integrity, ROS, and receptor-complex cross-talk.

4. Cellular localization and complexes

4.1 Best-supported localization

Plasma membrane (cell membrane): FER is described and experimentally supported as a plasma-membrane receptor. In wild-type vegetative tissues, pFER::FER-GFP localizes predominantly at the cell membrane, with negligible intracellular signal (li2015glycosylphosphatidylinositolanchoredproteinsas pages 8-11). The 2024 Annual Review also explicitly states FER is located in the cell membrane (cheung2024feroniaareceptor pages 3-4).

Filiform apparatus (synergid cell region): In ovules, FER-GFP localizes prominently at the filiform apparatus—a membrane-enriched cell-wall region where pollen tube reception occurs (li2015glycosylphosphatidylinositolanchoredproteinsas pages 8-11).

Endoplasmic reticulum (trafficking/retention): FER can accumulate in ER-like reticulate structures when LLG1/LRE are missing. ER-Tracker staining and RFP-ER co-localization support ER retention, consistent with a chaperone/co-receptor role for GPI-anchored LLG/LRE in FER secretory trafficking (li2015glycosylphosphatidylinositolanchoredproteinsas pages 8-11).

4.2 Complexes and interaction partners (experimentally supported)

FER–LLG1 / FER–LRE complex (coreceptor/chaperone): LLG1/LRE bind FER’s extracellular juxtamembrane region and are required for efficient FER plasma-membrane localization; interactions are supported by localization rescue, pull-downs, co-immunoprecipitation, and BiFC (li2015glycosylphosphatidylinositolanchoredproteinsas pages 1-2, li2015glycosylphosphatidylinositolanchoredproteinsas pages 11-13).

FER–RALF complexes: RALF1 association with a FER–LLG1 complex is supported by MBP-RALF1 pull-down capturing FER and LLG1 (li2015glycosylphosphatidylinositolanchoredproteinsas pages 11-13). Structural evidence summarized in 2024 supports a RALF23–LLG2–FER extracellular heterocomplex (cheung2024feroniaareceptor pages 8-9).

FER–ROPGEF interaction: FER interacts directly with ROPGEFs (cheung2024feroniaareceptor pages 3-4), providing a direct mechanistic link to RAC/ROP activation.

FER–PP2C12 complex: PP2C12 associates with FER (co-IP in N. benthamiana and Arabidopsis; BiFC peripheral signal) and dephosphorylates FER’s cytoplasmic domain (hou2024thephosphatasepp2c12 pages 9-14). This is recent (2024) and potentially important for GO annotation as “regulation of kinase activity” evidence.

5. Annotation-risk assessment (core vs over-extended)

5.1 High-confidence “core function” annotation set

1. Receptor kinase activity / protein Ser/Thr kinase activity: Strong biochemical evidence from nanodisc reconstitution and active-site mapping (minkoff2017acellfreemethod pages 1-2).
2. Plasma membrane receptor complex mediating peptide (RALF) signaling: Physical complex and ligand association evidence (FER–LLG1/LRE; FER–RALF; structural RALF23–LLG–FER complex) (li2015glycosylphosphatidylinositolanchoredproteinsas pages 11-13, cheung2024feroniaareceptor pages 8-9).
3. Pollen tube reception and pollen tube bursting control: Quantified fertility defects and mechanistic ROS-linked pollen tube rupture context (cheung2024feroniaareceptor pages 3-4, wolf2014growthcontrola pages 1-2).
4. Root hair development / tip growth integrity via RAC/ROP→ROS: Strong phenotype and mechanistic linkage (li2015glycosylphosphatidylinositolanchoredproteinsas pages 8-11, li2016feroniaandher pages 4-5).

These are most appropriate as “core” GO annotations.

5.2 Medium-confidence, context-dependent annotations

• ABA response / seedling growth suppression / stomatal regulation: Clear phenotypic evidence, but may be indirect through broader signaling network (cheung2024feroniaareceptor pages 3-4).
• Salt stress response: Strong stress phenotype (root cell bursting and growth arrest) but likely via cell wall integrity/ROS and should be scoped narrowly (cheung2024feroniaareceptor pages 31-36).
• Immunity modulation: Evidence exists for altered immune responses/pathogen outcomes, but causal molecular mechanisms may be indirect; avoid assigning overly specific immune signaling terms unless primary data support direct receptor complex roles (wolf2014growthcontrola pages 1-2, li2016feroniaandher pages 2-4).

5.3 High-risk annotations to avoid without additional evidence

• Apoptosis / pyroptosis / inflammatory signaling / neuronal or synaptic roles: Not biologically applicable and not supported by any evidence in plants (wolf2014growthcontrola pages 1-2, cheung2024feroniaareceptor pages 3-4).
• Programmed cell death (PCD) as a direct FER function: Some sources use “cell death” language in mutant phenotype summaries or reproductive contexts, but the excerpts primarily describe mechanical rupture/bursting (pollen tube bursting; root hair/cell bursting) and do not provide canonical PCD markers. Therefore, annotating FER directly to PCD/apoptosis is not justified from the available evidence (li2016feroniaandher pages 2-4, cheung2024feroniaareceptor pages 31-36, hofte2015theyinand pages 9-10).
• Nuclear localization of FER: Although FER’s kinase activity affects nuclear targets (MYC2, ABI5) per review summaries, none of the retrieved excerpts provide direct evidence that FER localizes to the nucleus; avoid GO cellular component annotations to nucleus for FER based solely on downstream nuclear signaling (cheung2024feroniaareceptor pages 18-19).
• Proteolytic processing/maturation of FER: No support in retrieved evidence (cheung2024feroniaareceptor pages 31-36).

6. Recent developments and applications (2023–2024 prioritized)

6.1 2024: Structural consolidation and network framing

The 2024 Annual Review of Plant Biology article frames FER as a global signaling hub and highlights structural advances including the RALF23–LLG2–FER extracellular heterocomplex, supporting a ligand–co-receptor–receptor model for signal perception and emphasizing FER’s pleiotropic integration with cell wall, membrane, cytoplasmic, and nuclear signaling networks (Cheung, Jul 2024; https://doi.org/10.1146/annurev-arplant-102820-103424) (cheung2024feroniaareceptor pages 8-9, cheung2024feroniaareceptor pages 31-36).

6.2 2024: Kinase regulation by PP2C12 (fine-tuning RALF/LRX/FER module)

Hou et al. (Nov 2024 preprint) provides a direct mechanistic connection between a PP2C phosphatase and FER kinase activation-loop phosphorylation. Key GO-relevant findings include:
- PP2C12 interacts with FER (co-IP; BiFC) (hou2024thephosphatasepp2c12 pages 9-14).
- PP2C12 dephosphorylates FERCD in vitro, with phosphoproteomics suggesting dephosphorylation at Thr696 (hou2024thephosphatasepp2c12 pages 9-14).
- PP2C12-GFP overexpression reduces RALF1 sensitivity; quantitative phenotyping was performed with n>100 per genotype and significant differences (P<0.01) (hou2024thephosphatasepp2c12 pages 9-14).

These data support curated annotations around regulation of receptor kinase activity and cell wall integrity signaling, while noting preprint status.

6.3 Real-world implementations and translational framing

FER is widely discussed as a leverage point for growth and resilience engineering because it integrates RALF signaling, cell wall integrity, and stress responses; the 2024 Annual Review explicitly highlights the potential applications of FER-family modules for improving plant growth and resilience (cheung2024feroniaareceptor pages 3-4). While specific deployed agronomic products are not in the provided evidence, the described mechanisms (stress buffering; growth–defense balance) represent a plausible translational axis.

7. Evidence-to-annotation table

Table: This table maps the strongest GO-relevant evidence for Arabidopsis FERONIA to molecular function, biological process, and cellular component claims. It is designed to help distinguish core annotations from context-specific or high-risk overextensions during GO review.

8. Key literature (GO-relevant; with publication dates and URLs)

1. Cheung, A.Y. (Jul 2024). FERONIA: A Receptor Kinase at the Core of a Global Signaling Network. Annual Review of Plant Biology 75:345–375. https://doi.org/10.1146/annurev-arplant-102820-103424 (cheung2024feroniaareceptor pages 3-4, cheung2024feroniaareceptor pages 8-9)
2. Hou, X. et al. (Nov 2024). The phosphatase PP2C12 is a negative player in LRX-RALF-FER-mediated cell wall integrity sensing. bioRxiv. https://doi.org/10.1101/2024.11.05.622083 (hou2024thephosphatasepp2c12 pages 9-14)
3. Li, C. et al. (Jun 2015). GPI-anchored proteins as chaperones and co-receptors for FERONIA receptor kinase signaling in Arabidopsis. eLife 4:e06587. https://doi.org/10.7554/eLife.06587 (li2015glycosylphosphatidylinositolanchoredproteinsas pages 8-11, li2015glycosylphosphatidylinositolanchoredproteinsas pages 11-13)
4. Li, C. et al. (Jun 2016). FERONIA and Her Pals: Functions and Mechanisms. Plant Physiology 171:2379–2392. https://doi.org/10.1104/pp.16.00667 (li2016feroniaandher pages 4-5, li2016feroniaandher pages 2-4)
5. Minkoff, B.B. et al. (Apr 2017). Cell-free expression and reconstitution enables functional characterization of FERONIA. Journal of Biological Chemistry 292:5932–5942. https://doi.org/10.1074/jbc.m116.761981 (minkoff2017acellfreemethod pages 1-2)
6. Wolf, S. & Höfte, H. (May 2014). Growth Control: A Saga of Cell Walls, ROS, and Peptide Receptors. The Plant Cell 26:1848–1856. https://doi.org/10.1105/tpc.114.125518 (wolf2014growthcontrola pages 1-2)
7. Höfte, H. (Feb 2015). The yin and yang of cell wall integrity control: brassinosteroid and FERONIA signaling. Plant & Cell Physiology 56:224–231. https://doi.org/10.1093/pcp/pcu182 (hofte2015theyinand pages 9-10)

References

1. (cheung2024feroniaareceptor pages 3-4): Alice Y. Cheung. Feronia: a receptor kinase at the core of a global signaling network. Jul 2024. URL: https://doi.org/10.1146/annurev-arplant-102820-103424, doi:10.1146/annurev-arplant-102820-103424. This article has 78 citations and is from a domain leading peer-reviewed journal.

2. (cheung2024feroniaareceptor pages 8-9): Alice Y. Cheung. Feronia: a receptor kinase at the core of a global signaling network. Jul 2024. URL: https://doi.org/10.1146/annurev-arplant-102820-103424, doi:10.1146/annurev-arplant-102820-103424. This article has 78 citations and is from a domain leading peer-reviewed journal.

3. (cheung2024feroniaareceptor pages 31-36): Alice Y. Cheung. Feronia: a receptor kinase at the core of a global signaling network. Jul 2024. URL: https://doi.org/10.1146/annurev-arplant-102820-103424, doi:10.1146/annurev-arplant-102820-103424. This article has 78 citations and is from a domain leading peer-reviewed journal.

4. (li2016feroniaandher pages 4-5): Chao Li, H.-M. Wu, and Alice Y. Cheung. Feronia and her pals: functions and mechanisms1[open]. Plant Physiology, 171:2379-2392, Jun 2016. URL: https://doi.org/10.1104/pp.16.00667, doi:10.1104/pp.16.00667. This article has 216 citations and is from a highest quality peer-reviewed journal.

5. (hou2024thephosphatasepp2c12 pages 9-14): Xiaoyu Hou, Kyle W. Bender, Gabor Kadler, Shibu Gupta, Mona Häfliger, Amandine Guérin, Anouck Diet, Stefan Roffler, Daniela Campanini, Thomas Wicker, Cyril Zipfel, and Christoph Ringli. The phosphatase pp2c12 is a negative player in lrx-ralf-fer-mediated cell wall integrity sensing. bioRxiv, Nov 2024. URL: https://doi.org/10.1101/2024.11.05.622083, doi:10.1101/2024.11.05.622083. This article has 1 citations.

6. (minkoff2017acellfreemethod pages 1-2): Benjamin B. Minkoff, Shin-ichi Makino, Miyoshi Haruta, Emily T. Beebe, Russell L. Wrobel, Brian G. Fox, and Michael R. Sussman. A cell-free method for expressing and reconstituting membrane proteins enables functional characterization of the plant receptor-like protein kinase feronia. Journal of Biological Chemistry, 292:5932-5942, Apr 2017. URL: https://doi.org/10.1074/jbc.m116.761981, doi:10.1074/jbc.m116.761981. This article has 27 citations and is from a domain leading peer-reviewed journal.

7. (cheung2024feroniaareceptor pages 1-3): Alice Y. Cheung. Feronia: a receptor kinase at the core of a global signaling network. Jul 2024. URL: https://doi.org/10.1146/annurev-arplant-102820-103424, doi:10.1146/annurev-arplant-102820-103424. This article has 78 citations and is from a domain leading peer-reviewed journal.

8. (li2015glycosylphosphatidylinositolanchoredproteinsas pages 1-2): Chao Li, Fang-Ling Yeh, Alice Y Cheung, Qiaohong Duan, Daniel Kita, Ming-Che Liu, Jacob Maman, Emily J Luu, Brendan W Wu, Laura Gates, Methun Jalal, Amy Kwong, Hunter Carpenter, and Hen-Ming Wu. Glycosylphosphatidylinositol-anchored proteins as chaperones and co-receptors for feronia receptor kinase signaling in arabidopsis. eLife, Jun 2015. URL: https://doi.org/10.7554/elife.06587, doi:10.7554/elife.06587. This article has 370 citations and is from a domain leading peer-reviewed journal.

9. (li2015glycosylphosphatidylinositolanchoredproteinsas pages 8-11): Chao Li, Fang-Ling Yeh, Alice Y Cheung, Qiaohong Duan, Daniel Kita, Ming-Che Liu, Jacob Maman, Emily J Luu, Brendan W Wu, Laura Gates, Methun Jalal, Amy Kwong, Hunter Carpenter, and Hen-Ming Wu. Glycosylphosphatidylinositol-anchored proteins as chaperones and co-receptors for feronia receptor kinase signaling in arabidopsis. eLife, Jun 2015. URL: https://doi.org/10.7554/elife.06587, doi:10.7554/elife.06587. This article has 370 citations and is from a domain leading peer-reviewed journal.

10. (cheung2024feroniaareceptor pages 18-19): Alice Y. Cheung. Feronia: a receptor kinase at the core of a global signaling network. Jul 2024. URL: https://doi.org/10.1146/annurev-arplant-102820-103424, doi:10.1146/annurev-arplant-102820-103424. This article has 78 citations and is from a domain leading peer-reviewed journal.

11. (li2015glycosylphosphatidylinositolanchoredproteinsas pages 11-13): Chao Li, Fang-Ling Yeh, Alice Y Cheung, Qiaohong Duan, Daniel Kita, Ming-Che Liu, Jacob Maman, Emily J Luu, Brendan W Wu, Laura Gates, Methun Jalal, Amy Kwong, Hunter Carpenter, and Hen-Ming Wu. Glycosylphosphatidylinositol-anchored proteins as chaperones and co-receptors for feronia receptor kinase signaling in arabidopsis. eLife, Jun 2015. URL: https://doi.org/10.7554/elife.06587, doi:10.7554/elife.06587. This article has 370 citations and is from a domain leading peer-reviewed journal.

12. (wolf2014growthcontrola pages 1-2): Sebastian Wolf and Herman Höfte. Growth control: a saga of cell walls, ros, and peptide receptors. Plant Cell, 26:1848-1856, May 2014. URL: https://doi.org/10.1105/tpc.114.125518, doi:10.1105/tpc.114.125518. This article has 127 citations and is from a highest quality peer-reviewed journal.

13. (li2016feroniaandher pages 2-4): Chao Li, H.-M. Wu, and Alice Y. Cheung. Feronia and her pals: functions and mechanisms1[open]. Plant Physiology, 171:2379-2392, Jun 2016. URL: https://doi.org/10.1104/pp.16.00667, doi:10.1104/pp.16.00667. This article has 216 citations and is from a highest quality peer-reviewed journal.

14. (hofte2015theyinand pages 9-10): Herman Höfte. The yin and yang of cell wall integrity control: brassinosteroid and feronia signaling. Plant & cell physiology, 56 2:224-31, Feb 2015. URL: https://doi.org/10.1093/pcp/pcu182, doi:10.1093/pcp/pcu182. This article has 80 citations and is from a domain leading peer-reviewed journal.

15. (li2015glycosylphosphatidylinositolanchoredproteinsas pages 16-17): Chao Li, Fang-Ling Yeh, Alice Y Cheung, Qiaohong Duan, Daniel Kita, Ming-Che Liu, Jacob Maman, Emily J Luu, Brendan W Wu, Laura Gates, Methun Jalal, Amy Kwong, Hunter Carpenter, and Hen-Ming Wu. Glycosylphosphatidylinositol-anchored proteins as chaperones and co-receptors for feronia receptor kinase signaling in arabidopsis. eLife, Jun 2015. URL: https://doi.org/10.7554/elife.06587, doi:10.7554/elife.06587. This article has 370 citations and is from a domain leading peer-reviewed journal.