Affinage

FBXW8

F-box/WD repeat-containing protein 8 · UniProt Q8N3Y1

Length
598 aa
Mass
67.4 kDa
Annotated
2026-06-09
23 papers in source corpus 17 papers cited in narrative 17 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 7/7 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

FBXW8 is the substrate-recognition subunit of a heterotypic cullin-RING E3 ubiquitin ligase that controls protein turnover governing cell cycle progression, growth signaling, and developmental processes (PMID:12481031, PMID:16880526). It assembles with SKP1 and CUL7 into a CRL7FBXW8 module, but unlike canonical CRLs this module is catalytically inert on its own: cryo-EM and reconstitution show CUL7-RBX1 holds its RING domain in an orientation incompatible with engaging E2~ubiquitin, so CRL7FBXW8 functions as a substrate receptor that must couple via SKP1-FBXW8 to a separate neddylated CUL1-RBX1 catalytic module to achieve ubiquitination (PMID:35982156). CUL1 binds the FBXW8 N-terminus through SKP1 while CUL7 binds its C-terminus directly, and loss of either cullin abrogates binding of the other, making FBXW8 the obligate bridge of the supercomplex (PMID:16880526, PMID:34478796). The ligase recognizes substrates marked by upstream phosphorylation and degrades them by the proteasome: ERK-cascade phosphorylation of cyclin D1 at Thr286 directs its cytoplasmic degradation during S phase (PMID:17205132), and FBXW8 attenuates β-TrCP1 in a MAPK-dependent manner to permit the Cdc25A-driven G1-to-S transition (PMID:33742524). FBXW8 activity is itself regulated by signaling — mTORC2 phosphorylates FBXW8 at Ser86 to stabilize it and promote cytosolic IRS-1 degradation, linking it to insulin signaling and insulin resistance (PMID:23142081). Additional substrates include HPK1, whose recognition is gated by PP4 dephosphorylation at Thr355 (PMID:24362026), MRFAP1 during the anaphase-telophase transition (PMID:29228602), PPT1 to suppress EMT in hepatocellular carcinoma (PMID:40659255), and NANOG in embryonic stem cells, where KAP1 competes for NANOG to block its degradation and sustain pluripotency (PMID:40759604). Genetic ablation in mice causes intrauterine and postnatal growth retardation with abnormal placental development, establishing an in vivo role in embryonic and placental growth (PMID:16880526, PMID:17998335).

Mechanistic history

Synthesis pass · year-by-year structured walk · 16 steps
  1. 2002 High

    Established that FBXW8 is not a generic SCF F-box protein but the dedicated substrate receptor of a CUL7-based ligase, defining a distinct proteolysis pathway.

    Evidence Mass spectrometry, reciprocal Co-IP, and biochemical reconstitution showing CUL7 binds SKP1·FBXW8 selectively over SKP1 alone or other F-box proteins

    PMID:12481031

    Open questions at the time
    • Substrates of the complex not yet identified
    • Catalytic architecture and dependence on a second cullin not yet defined
  2. 2006 High

    Assigned the complex its first substrate and showed phosphodegron-dependent recognition, linking FBXW8 to cell cycle control downstream of Ras/MAPK.

    Evidence siRNA knockdown, cyclin D1 degradation and fractionation assays, ERK modulation, and rescue with the cyclin D1-T286A non-phosphorylatable mutant

    PMID:17205132

    Open questions at the time
    • Direct in vitro ubiquitination of cyclin D1 by reconstituted complex not shown
    • Did not resolve how cytoplasmic vs nuclear pools are partitioned
  3. 2006 High

    Demonstrated in vivo that FBXW8 is required for CUL7-CUL1 association and for normal embryonic and placental growth, connecting the biochemistry to physiology.

    Evidence Fbxw8-null mouse model with Co-IP of Cul7/Cul1 in null vs WT cells and placental histology

    PMID:16880526

    Open questions at the time
    • Substrate(s) responsible for growth phenotype not identified
    • Mechanism of Cul1 requirement at structural level unknown
  4. 2007 High

    Independent knockout corroborated growth retardation and placed FBXW8-CUL7 in an IGF-binding-protein growth pathway.

    Evidence Gene-trap mouse, expression profiling, and Western blot of IGFBP2 in null fibroblasts

    PMID:17998335

    Open questions at the time
    • IGFBPs shown as correlates, not direct ubiquitination substrates
    • Causal chain from FBXW8 to IGFBP levels unresolved
  5. 2012 High

    Identified FBXW8 as a regulated node in insulin signaling, with mTORC2 phosphorylation at Ser86 controlling FBXW8 stability and IRS-1 degradation.

    Evidence mTORC2 knockdown, phospho-specific analysis, fractionation, IRS-1 ubiquitination/degradation assays, and Ser86Ala mutant

    PMID:23142081

    Open questions at the time
    • Whether IRS-1 is a direct CRL7FBXW8 substrate vs indirect not fully resolved
    • Physiological insulin resistance link tested in cells, not whole animal
  6. 2013 High

    Extended the phosphodegron logic to HPK1 and showed a phosphatase (PP4) gates substrate recognition, adding a layer of upstream control.

    Evidence Co-IP, ubiquitination assay, phosphatase-dead PP4 mutant, Thr355 mutagenesis, and siRNA knockdown in pancreatic cancer cells

    PMID:24362026

    Open questions at the time
    • Kinase generating the Thr355 phosphodegron not defined
    • In vivo relevance in tumors not tested
  7. 2012 Medium

    Implicated FBXW8 in clearance of ATXN2, suggesting a role in neurodegenerative protein homeostasis.

    Evidence Co-IP in vitro and in vivo, solubility fractionation, overexpression, and SCA2 knock-in transcriptome profiling

    PMID:22956915

    Open questions at the time
    • Direct ubiquitination of ATXN2 not demonstrated
    • Single-lab correlative data; reciprocal validation limited
  8. 2015 Medium

    Refined the ATXN2 connection, showing FBXW8 transcript is selectively induced by polyQ expansion and FBXW8/PARK2 are sequestered into insoluble aggregates.

    Evidence Reciprocal Co-IP, solubility fractionation, and qPCR in SCA2 patient cells

    PMID:25790475

    Open questions at the time
    • Functional consequence of FBXW8 upregulation in SCA2 unknown
    • Whether sequestration is cause or consequence unresolved
  9. 2017 Medium

    Added MRFAP1 as a mitotic substrate, linking FBXW8 to genomic stability at the anaphase-telophase transition.

    Evidence IP-proteomics, Co-IP, ubiquitination assay, cycloheximide chase, and cell-death assays

    PMID:29228602

    Open questions at the time
    • Phosphodegron or recognition signal on MRFAP1 not mapped
    • Single-lab; no in vivo confirmation
  10. 2021 Medium

    Showed FBXW8 controls oscillation of β-TrCP1 levels to enable the Cdc25A-driven G1-to-S transition, integrating it with another ligase axis.

    Evidence Biochemical assays, flow cytometry, immunofluorescence, MAPK inhibition, and siRNA in cell cycle staging

    PMID:33742524

    Open questions at the time
    • Direct ubiquitination of β-TrCP1 by reconstituted complex not shown
    • Single-lab study
  11. 2021 Medium

    Defined the architectural requirement that CUL1 and CUL7 synergistically and cooperatively bind FBXW8, with binding to distinct FBXW8 termini, and linked the complex to migration via β-catenin.

    Evidence Co-IP, site-directed mutagenesis, docking, ubiquitination, migration assay, and β-catenin reporter

    PMID:34478796

    Open questions at the time
    • Stoichiometry and dynamics of the supercomplex not resolved at this stage
    • Docking models not validated structurally
  12. 2022 High

    Resolved the central mechanistic puzzle: cryo-EM revealed CRL7FBXW8 is catalytically inert and acts as a substrate receptor that must couple to a neddylated CUL1-RBX1 module for ubiquitination.

    Evidence Cryo-EM structure, in vitro auto-neddylation and ubiquitination assays, reconstitution, and mutagenesis

    PMID:35982156

    Open questions at the time
    • Structure of the full CUL7-CUL1 supercomplex with substrate engaged not determined
    • How substrate is transferred between modules unresolved
  13. 2024 Medium

    Revealed an unconventional degradation route, showing FBXW8 adds K48 chains to a viral nucleocapsid that are routed to autophagy rather than the proteasome.

    Evidence Overexpression/knockdown, K48-specific ubiquitination assay, Co-IP with NDP52, autophagic vs proteasomal assays, and promoter luciferase

    PMID:39624099

    Open questions at the time
    • Whether the CUL1-CUL7 catalytic logic applies to this substrate not tested
    • Generality of autophagic routing for FBXW8 substrates unknown
  14. 2025 Medium

    Identified NUMB hyper-degradation by CRL7FBXW8 as a driver of breast cancer transformation, providing a therapeutic rationale.

    Evidence RNAi E3-ligase screen, genetic and pharmacological inhibition, and PDX models with NUMB rescue

    PMID:40411418

    Open questions at the time
    • Phosphodegron/recognition signal on NUMB not mapped
    • Pharmacological agent specificity not fully characterized
  15. 2025 Medium

    Showed FBXW8 degrades PPT1 to suppress SNAIL/ZEB1-driven EMT and HCC invasion, assigning a tumor-suppressive role in this context.

    Evidence Proteomics, Co-IP, ubiquitination assay, overexpression/knockdown, and in vitro/in vivo EMT-marker functional assays

    PMID:40659255

    Open questions at the time
    • Recognition signal on PPT1 not defined
    • Single-lab study
  16. 2025 Medium

    Established FBXW8 as a regulator of pluripotency by degrading NANOG, with KAP1 acting as a competitive stabilizer.

    Evidence Co-IP, KAP1 coiled-coil domain mapping, overexpression/knockdown, ubiquitination assay, and cycloheximide chase

    PMID:40759604

    Open questions at the time
    • Phosphodegron on NANOG not characterized
    • In vivo pluripotency consequence not demonstrated

Open questions

Synthesis pass · forward-looking unresolved questions
  • How a single FBXW8 ligase selects among its many phospho-regulated substrates in different cellular contexts, and whether all substrates require the CUL1 catalytic module, remains unresolved.
  • No unified phosphodegron consensus across substrates
  • Substrate-specific contribution of CUL1 vs CUL7 modules untested for most substrates
  • Tissue-specific substrate prioritization unknown

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0140096 catalytic activity, acting on a protein 6 GO:0016874 ligase activity 3 GO:0060090 molecular adaptor activity 3
Localization
GO:0005829 cytosol 2
Pathway
R-HSA-1266738 Developmental Biology 3 R-HSA-162582 Signal Transduction 3 R-HSA-1640170 Cell Cycle 3 R-HSA-392499 Metabolism of proteins 2
Partners
ATXN2CUL1CUL7KAP1NDP52PARK2RBX1SKP1
Complex memberships
CRL7FBXW8 (SKP1-CUL7-FBXW8-RBX1)CUL1-SKP1-FBXW8-CUL7 supercomplex

Evidence

Reading pass · 17 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2002 CUL7 assembles an SCF-ROC1-like E3 ubiquitin ligase complex consisting of SKP1, CUL7, FBXW8 (Fbx29), and ROC1. CUL7 selectively interacts with the SKP1·FBXW8 complex but not with SKP1 alone or with SKP1 bound to other F-box proteins (βTrCP2, Skp2), defining a distinct ubiquitin-dependent proteolysis pathway. Mass spectrometry identification of CUL7 as ROC1-interacting protein; co-immunoprecipitation; biochemical complex reconstitution Proceedings of the National Academy of Sciences of the United States of America High 12481031
2006 FBXW8 acts as the E3 ligase substrate-recognition subunit that mediates ubiquitination and cytoplasmic degradation of cyclin D1 during S phase. This process requires Thr286 phosphorylation of cyclin D1 driven by the Ras/Raf/MEK/ERK cascade. FBXW8 is predominantly cytoplasmic during G1 and S phase; depletion causes cyclin D1 accumulation and CDK1 cytoplasmic sequestration, severely reducing cancer cell proliferation. siRNA knockdown, cyclin D1 degradation assay, subcellular fractionation/immunofluorescence, rescue with cyclin D1-T286A mutant, ERK1/2 signaling modulation PloS one High 17205132
2006 FBXW8 is essential for Cul7–Cul1 heterodimeric complex formation; in Fbxw8-null mouse cells, Cul7 fails to associate with Cul1. Loss of Fbxw8 causes intrauterine growth retardation and abnormal placental development (reduced spongiotrophoblast layer, abnormal labyrinth vessels), phenocopying aspects of Cul7-null mice. Gene-targeted (knockout) mouse model; co-immunoprecipitation of Cul7 and Cul1 in wild-type vs. Fbxw8-null cells; histological analysis of placenta Molecular and cellular biology High 16880526
2007 Fbxw8 knockout mice display pre- and postnatal growth retardation. Fbxw8-null embryos and placentas are smaller than wild-type; approximately 70% die in utero. IGFBP1 transcript levels are elevated in Fbxw8-null embryos, and IGFBP2 protein is increased in both Cul7-null and Fbxw8-null fibroblasts, placing FBXW8-CUL7 in a growth-regulatory pathway involving IGF-binding proteins. Gene-trap mouse model; expression profiling; Western blot for IGFBP2 in fibroblasts; organ size measurement Molecular and cellular biology High 17998335
2008 The CUL7/FBXW8 E3 ubiquitin ligase targets insulin receptor substrate-1 (IRS-1) for ubiquitination and proteasomal degradation, implicating this enzyme in the regulation of insulin signaling downstream of mTORC1/S6K phosphorylation of IRS-1. Commentary/interpretation of Xu et al. experimental data (Co-IP, ubiquitination assay referenced in the primary paper); mechanistic framework confirmed by cited experiments Developmental cell Medium 18539111
2012 mTORC2 stabilizes FBXW8 by phosphorylating it at Ser86 and promotes insulin-stimulated translocation of FBXW8 to the cytosol, where FBXW8 mediates IRS-1 degradation. Disruption of mTORC2 attenuates FBXW8 expression and phosphorylation, causing inactive IRS-1 to accumulate and contributing to insulin resistance. mTORC2 component knockdown, phospho-specific analysis, subcellular fractionation, IRS-1 ubiquitination and degradation assays, Ser86Ala FBXW8 mutant Molecular cell High 23142081
2012 FBXW8 co-localizes and co-immunoprecipitates with ATXN2 in vitro and in vivo, and FBXW8 overexpression decreases the level of expanded insoluble ATXN2 protein, indicating FBXW8 participates in degradation of both wild-type and polyQ-expanded ATXN2. Co-immunoprecipitation (in vitro and in vivo); cell culture overexpression; Western blot for ATXN2 soluble/insoluble fractions; transcriptome profiling of knock-in mouse cerebellum PLoS genetics Medium 22956915
2013 The CUL7/FBXW8 E3 ubiquitin ligase targets hematopoietic progenitor kinase 1 (HPK1) for proteasomal degradation. HPK1 ubiquitination requires its kinase activity and autophosphorylation. Phosphatase PP4 dephosphorylates HPK1 at Thr-355, inhibiting FBXW8-HPK1 interaction and FBXW8-mediated ubiquitination. Fbxw8 knockdown restores HPK1 levels and inhibits pancreatic cancer cell proliferation. Co-immunoprecipitation; ubiquitination assay; phosphatase-dead PP4 mutant; site-directed mutagenesis (Thr355); siRNA knockdown; proteasome inhibitor treatment The Journal of biological chemistry High 24362026
2015 FBXW8 co-immunoprecipitates with ATXN2 and PARK2 both in vitro and in vivo. Expanded polyQ ATXN2 drives both FBXW8 and PARK2 proteins into insolubility. FBXW8 transcript is selectively upregulated by ATXN2 expansion (confirmed by qPCR in SCA2 patient fibroblasts and blood), whereas PARK2 transcript is not dysregulated. Co-immunoprecipitation (in vitro and in vivo); solubility fractionation; qPCR in patient-derived cells; co-localization immunofluorescence PloS one Medium 25790475
2017 MRFAP1 is an interactor and substrate of FBXW8; the CUL7/FBXW8 ubiquitin ligase ubiquitinates and degrades MRFAP1 during the mitotic anaphase-telophase transition. FBXW8 overexpression increases MRFAP1 polyubiquitination and decreases its stability; FBXW8 knockdown prolongs MRFAP1 half-life. Forced MRFAP1 expression causes genomic instability and mitotic cell death. Immunoprecipitation-based proteomics screen; co-immunoprecipitation; ubiquitination assay; cycloheximide chase; overexpression and siRNA knockdown; cell death assay Oncotarget Medium 29228602
2021 FBXW8 directs proteasomal degradation of β-TrCP1 in a MAPK pathway-dependent manner, controlling oscillation of β-TrCP1 levels during cell cycle G1 and S phases. Attenuation of β-TrCP1 by FBXW8 is required for Cdc25A-mediated G1-to-S transition and DNA damage-free S phase progression. Biochemical assays, flow cytometry, immunofluorescence, siRNA knockdown, MAPK pathway inhibition, cell cycle staging The FEBS journal Medium 33742524
2021 CUL1 and CUL7 cooperatively and synergistically bind FBXW8 to form a CUL1-SKP1-FBXW8-CUL7 functional ubiquitin ligase complex; absence of either cullin abrogates binding of the other. CUL1 binds the N-terminus of FBXW8 via SKP1 while CUL7 binds the C-terminus directly. This complex maintains basal β-TrCP1 levels and promotes cell migration via β-catenin activation through β-TrCP1 degradation. Co-immunoprecipitation (in vitro and in vivo); site-directed mutagenesis; computational docking; ubiquitination assay; migration assay; β-catenin reporter International journal of biological macromolecules Medium 34478796
2022 Cryo-EM and biochemical analysis reveal the structure of CRL7FBXW8: CUL7's selectivity for FBXW8 among all F-box proteins is due to an F-box-independent binding mode. Within CRL7FBXW8, the RBX1 RING domain is constrained in an orientation incompatible with binding E2~NEDD8 or E2~ubiquitin intermediates; purified recombinant CRL7FBXW8 lacks auto-neddylation and ubiquitination activities. Instead, CRL7 functions as a substrate receptor linked via SKP1-FBXW8 to a neddylated CUL1-RBX1 catalytic module that mediates ubiquitination. Cryo-EM structure determination; in vitro auto-neddylation assay; in vitro ubiquitination assay; biochemical reconstitution; mutagenesis Nature structural & molecular biology High 35982156
2024 FBXW8 suppresses porcine deltacoronavirus (PDCoV) replication by catalyzing K48-linked polyubiquitination of the viral nucleocapsid (N) protein at a lysine-rich region, but the ubiquitinated N protein is degraded via NDP52-dependent autophagy rather than the proteasome. PDCoV infection increases FBXW8 expression through p65-mediated promoter activation. Overexpression and knockdown; ubiquitination assay specifying K48 linkage; co-immunoprecipitation of N protein with NDP52; autophagic vs. proteasomal degradation assays; promoter luciferase assay Frontiers in immunology Medium 39624099
2025 CRL7FBXW8 is the E3 ligase complex responsible for NUMB protein hyper-degradation in breast cancer. Identified by RNAi-based screening; genetic and pharmacological inhibition of CRL7FBXW8 rescues NUMB protein levels and reverses transformation-related phenotypes in breast cancer cell lines and patient-derived xenografts. RNAi-based E3 ligase screen; genetic knockdown; pharmacological inhibition; PDX models; Western blot for NUMB levels; functional transformation assays Advanced science Medium 40411418
2025 FBXW8 ubiquitinates and promotes proteasomal degradation of PPT1 (palmitoyl-protein thioesterase 1). FBXW8-mediated PPT1 degradation suppresses EMT by reducing expression of SNAIL and ZEB1 transcription factors, inhibiting HCC cell migration and invasion. Proteomic analysis; co-immunoprecipitation; ubiquitination assay; FBXW8 overexpression and knockdown; in vitro/in vivo functional assays; Western blot for EMT markers Biochimica et biophysica acta. Molecular basis of disease Medium 40659255
2025 FBXW8 targets NANOG for ubiquitination and proteasomal degradation in embryonic stem cells. KAP1 competes with FBXW8 for binding to NANOG, thereby blocking FBXW8-mediated NANOG degradation and stabilizing NANOG protein to maintain stem cell pluripotency. Co-immunoprecipitation; domain-mapping (Kap1 coiled-coil domain); overexpression and siRNA knockdown; ubiquitination assay; cycloheximide chase International journal of stem cells Medium 40759604

Source papers

Stage 0 corpus · 23 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2006 A critical role for FBXW8 and MAPK in cyclin D1 degradation and cancer cell proliferation. PloS one 171 17205132
2002 CUL7: A DOC domain-containing cullin selectively binds Skp1.Fbx29 to form an SCF-like complex. Proceedings of the National Academy of Sciences of the United States of America 136 12481031
2012 mTOR complex 2 regulates proper turnover of insulin receptor substrate-1 via the ubiquitin ligase subunit Fbw8. Molecular cell 91 23142081
2012 ATXN2-CAG42 sequesters PABPC1 into insolubility and induces FBXW8 in cerebellum of old ataxic knock-in mice. PLoS genetics 76 22956915
2007 Disruption of the Fbxw8 gene results in pre- and postnatal growth retardation in mice. Molecular and cellular biology 47 17998335
2006 Fbxw8 is essential for Cul1-Cul7 complex formation and for placental development. Molecular and cellular biology 47 16880526
2017 The long non-coding RNA MALAT1 interacted with miR-218 modulates choriocarcinoma growth by targeting Fbxw8. Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie 40 29096355
2013 The CUL7/F-box and WD repeat domain containing 8 (CUL7/Fbxw8) ubiquitin ligase promotes degradation of hematopoietic progenitor kinase 1. The Journal of biological chemistry 39 24362026
2015 Both ubiquitin ligases FBXW8 and PARK2 are sequestrated into insolubility by ATXN2 PolyQ expansions, but only FBXW8 expression is dysregulated. PloS one 25 25790475
2022 Structure of CRL7FBXW8 reveals coupling with CUL1-RBX1/ROC1 for multi-cullin-RING E3-catalyzed ubiquitin ligation. Nature structural & molecular biology 24 35982156
2010 Fbxw8 is involved in the proliferation of human choriocarcinoma JEG-3 cells. Molecular biology reports 22 20878477
2014 MicroRNA-218 inhibits the proliferation of human choriocarcinoma JEG-3 cell line by targeting Fbxw8. Biochemical and biophysical research communications 17 24973709
2021 uc.77- Downregulation Promotes Colorectal Cancer Cell Proliferation by Inhibiting FBXW8-Mediated CDK4 Protein Degradation. Frontiers in oncology 15 34094975
2021 FBXW8 regulates G1 and S phases of cell cycle progression by restricting β-TrCP1 function. The FEBS journal 11 33742524
2021 Co-operative binding of SKP1, Cullin1 and Cullin7 to FBXW8 results in Cullin1-SKP1-FBXW8-Cullin7 functional complex formation that monitors cellular function of β-TrCP1. International journal of biological macromolecules 11 34478796
2017 FBXW8-dependent degradation of MRFAP1 in anaphase controls mitotic cell death. Oncotarget 9 29228602
2024 FBXW8 suppresses PDCoV proliferation via the NPD52-dependent autophagic degradation of a viral nucleocapsid protein. Frontiers in immunology 6 39624099
2025 The CRL7FBXW8 Complex Controls the Mammary Stem Cell Compartment through Regulation of NUMB Levels. Advanced science (Weinheim, Baden-Wurttemberg, Germany) 5 40411418
2008 Shooting the messenger: CULLIN' insulin signaling with Fbw8. Developmental cell 3 18539111
2025 FBXW8-mediated degradation of PPT1 suppresses epithelial-mesenchymal transition and metastasis in hepatocellular carcinoma. Biochimica et biophysica acta. Molecular basis of disease 2 40659255
2022 Structure-based drug design of potential inhibitors of FBXW8, the substrate recognition component of Cullin-RING ligase 7. Molecular diversity 2 36322340
2017 Assessment of a FBXW8 frameshift mutation, c.1312_1313delGT, in breast cancer patients and controls from Central Europe. Cancer genetics 1 29310837
2025 Kap1 Regulates Protein Stability of Nanog by Interfering with Fbxw8-Dependent Ubiquitination. International journal of stem cells 0 40759604

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