Affinage

FUT8

Alpha-(1,6)-fucosyltransferase · UniProt Q9BYC5

Length
575 aa
Mass
66.5 kDa
Annotated
2026-06-09
100 papers in source corpus 43 papers cited in narrative 42 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 6/6 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

FUT8 is the sole mammalian α-1,6-fucosyltransferase, transferring fucose from GDP-β-L-fucose to the innermost GlcNAc of N-glycans (core fucosylation) and thereby tuning the signaling, stability, and trafficking of a broad set of glycoprotein targets (PMID:15352059, PMID:27008861). Structurally it comprises an N-terminal α-helical (coiled-coil) domain, a GT-B fold catalytic domain that binds the GDP-fucose donor through a Rossmann fold, and a C-terminal SH3 domain, and it operates by a rapid-equilibrium random mechanism with induced-fit donor binding that preferentially modifies G0 biantennary complex N-glycans (PMID:17172260, PMID:16344263, PMID:33004438, PMID:35662980). The SH3 domain (His-535) is itself required for catalysis and for Golgi/cell-surface trafficking and mediates a stimulatory interaction with the oligosaccharyltransferase subunit RPN1, while the α-helical stem region drives homodimerization/multimerization and protein stability (PMID:32350116, PMID:32147455, PMID:36336076). Through core fucosylation FUT8 governs growth factor and cytokine receptor signaling—including TGF-β, activin, EGFR, IGF-1R, VEGFR-2, and TNF receptors—with consequences for receptor activation, dimerization, trafficking, and downstream MAPK/PI3K-AKT/NF-κB output, and loss of Fut8 in mice produces emphysema-like lung destruction via TGF-β and VEGFR-2 dysregulation (PMID:17132494, PMID:19179362, PMID:23796784, PMID:32888953, PMID:30712666, PMID:34857735). FUT8 stabilizes or traffics numerous substrates by core fucosylation, including the immune checkpoint B7H3 (whose defucosylation triggers HSC70-mediated chaperone-mediated autophagy degradation), the ciliary transition-zone protein TMEM67, GLUT1, mucins, and the alphacoronavirus entry receptor aminopeptidase N, and core fucosylation of platelet receptors GPVI and integrin αIIbβ3 promotes platelet activation and thrombosis (PMID:32888953, PMID:33976130, PMID:36252012, PMID:37537172, PMID:40728580, PMID:42237907, PMID:41027183, PMID:42149951). These activities place FUT8 as a driver of cancer invasion and metastasis, immune evasion, ciliogenesis, and reproductive and neuronal development, and its enzymatic mechanism has been exploited by GDP-dependent mechanism-based small-molecule inhibitors (PMID:28982386, PMID:28609658, PMID:39340265, PMID:42237907, PMID:40473957).

Mechanistic history

Synthesis pass · year-by-year structured walk · 18 steps
  1. 2004 High

    Establishing FUT8 as the enzyme catalyzing core α-1,6-fucosylation defined its molecular activity and revealed that this modification governs antibody effector function.

    Evidence Sequential biallelic FUT8 knockout in CHO cells with ADCC and FcγRIIIa binding assays

    PMID:15352059

    Open questions at the time
    • Did not resolve enzyme structure or catalytic residues
    • Scope of native glycoprotein substrates not defined
  2. 2005 High

    Kinetic and structural characterization of donor binding clarified how FUT8 recognizes GDP-fucose and which residues drive catalysis.

    Evidence Recombinant human FUT8 kinetics, GDP-fucose analogue inhibition, and X-ray crystallography revealing coiled-coil, GT-B/Rossmann catalytic, and SH3 domains

    PMID:16344263 PMID:17172260

    Open questions at the time
    • Acceptor N-glycan binding mode not yet resolved
    • Functional role of the SH3 domain not addressed
  3. 2006 High

    Fut8 knockout mice connected core fucosylation to receptor signaling in vivo, showing that loss of fucosylation dysregulates TGF-β, EGF, PDGF, and LRP-1-dependent processes.

    Evidence Fut8-null mouse models with ligand rescue, gene reintroduction, endocytosis assay, and serum IGFBP-3 measurement

    PMID:16567404 PMID:17132494

    Open questions at the time
    • Whether fucosylation acts directly on each receptor versus secondary effects not fully separated
    • Site-specific glycan determinants not mapped
  4. 2009 Medium

    Linking Fut8 loss to reduced VEGFR-2 and elevated ceramide-driven apoptosis extended the emphysema phenotype to a defined survival-receptor axis.

    Evidence Fut8 knockout mouse and siRNA in A549/TGP49 cells with TUNEL and ceramide measurements

    PMID:19179362

    Open questions at the time
    • Mechanism coupling fucosylation loss to VEGFR-2 transcription unclear
    • Single-lab findings
  5. 2013 Medium

    FUT8 was shown to exert opposing, context-dependent effects on TGF-β-superfamily signaling and to control lineage outputs such as neuritogenesis and erythroid differentiation.

    Evidence siRNA/shRNA knockdown, overexpression, domain/loop mutagenesis, and rescue in PC12, MEL, and K562 cells

    PMID:23609441 PMID:23796784

    Open questions at the time
    • Molecular basis of positive versus negative signaling outcomes not unified
    • Single-lab observations
  6. 2016 High

    Demonstrating GnT-I-independent fucosylation of high-mannose glycans broadened FUT8's substrate range beyond complex-type N-glycans.

    Evidence Stable FUT8 knockdown/overexpression in HEK293S GnT-I-/- cells with glycan mass spectrometry of EPO

    PMID:27008861

    Open questions at the time
    • Physiological relevance of high-mannose core fucosylation not defined
    • Single rigorous study
  7. 2017 High

    Glycoproteomic and functional studies established FUT8 as a driver of cancer invasion and metastasis acting through specific substrates such as TGF-β receptors and L1CAM.

    Evidence shRNA/CRISPR loss-of-function, lentiviral gain-of-function, ligand binding assays, glycoproteomics, and in vivo metastasis/dissemination models in breast cancer and melanoma

    PMID:28609658 PMID:28982386

    Open questions at the time
    • Full repertoire of metastasis-relevant substrates incomplete
    • Quantitative contribution of each target not ranked
  8. 2020 High

    Domain dissection revealed that the SH3 domain (His-535) is required for catalysis and trafficking and recruits RPN1 to stimulate activity, while α-helical domains drive the active homodimer.

    Evidence Truncation/site-directed mutagenesis, in vivo cross-linking, cell-surface biotinylation, proteomics, and RPN1 knockdown

    PMID:32147455 PMID:32350116

    Open questions at the time
    • Structural model of the SH3/α-helical intermolecular interface not solved
    • Mechanism of RPN1 stimulation at atomic level unknown
  9. 2020 High

    Multiple ligand-bound crystal structures and acceptor specificity assays defined induced-fit donor binding and preference for the G0 biantennary glycan, refining substrate recognition rules.

    Evidence X-ray crystallography of FUT8 with GDP and four glycan acceptors plus active-site mutagenesis and kinetic analysis

    PMID:33004438

    Open questions at the time
    • Conformational dynamics in the membrane-anchored enzyme not captured
    • Acceptor recognition for non-canonical substrates incomplete
  10. 2020 High

    FUT8-EGFR core fucosylation was shown to control EGFR dimerization, trafficking, and downstream signaling across prostate cancer, keratinocytes, and tumor-associated fibroblasts.

    Evidence Overexpression/knockdown, EGFR surface and dimerization assays, trafficking assays, conditional KO psoriasis mouse, and CAF co-culture models

    PMID:32085441 PMID:32266093 PMID:32888953

    Open questions at the time
    • Site-specific EGFR glycan determinants not fully mapped
    • Whether effects generalize across tissues at endogenous levels untested
  11. 2021 High

    Substrate-stabilization mechanisms were defined, showing FUT8 core fucosylation protects target glycoproteins (B7H3, IGF-1R, mucins, TNFRs) from degradation or mislocalization, broadening its roles in immunosuppression, mucus biology, and apoptosis control.

    Evidence Knockdown/overexpression, protein stability and trafficking assays, immune functional assays, Fut8-/- mouse colon analysis, and in vivo therapy combination

    PMID:30712666 PMID:33976130 PMID:34857735 PMID:36252012

    Open questions at the time
    • Direct versus indirect stabilization not always separated
    • Glycosite-resolved mechanisms incomplete for some targets
  12. 2021 High

    STD NMR and glycopeptide assays refined the rules of FUT8 substrate selection, showing it reads both glycan structure and the underlying peptide and requires prior GDP binding for optimal acceptor recognition.

    Evidence STD NMR, in vitro assays with N-glycopeptide libraries, and CHO glycoengineering with glycoproteomics

    PMID:35662980

    Open questions at the time
    • Quantitative prediction of in vivo fucosylation site preference not established
  13. 2022 Medium

    Glycoproteomics expanded the FUT8 target catalogue and identified adhesion and cytokine-signaling substrates (integrin αvβ5, IL6ST) supporting metastatic phenotypes.

    Evidence Quantitative glycoproteomics of FUT8-KO versus WT breast cancer cells with LCA blotting, LC-MS/MS, and adhesion assays

    PMID:35303925

    Open questions at the time
    • Functional validation limited to a subset of 140 targets
    • Single-lab dataset
  14. 2022 Medium

    Transcriptional control of FUT8 was defined, placing it downstream of Wnt/β-catenin-TCF/LEF, Caveolin-1, c-Myc/c-Myb, and p53 in disease contexts.

    Evidence ChIP, RIP, EMSA, luciferase reporters, and overexpression/knockdown rescue in colorectal, hepatocellular, and microglial models

    PMID:32710651 PMID:34021424 PMID:36692036

    Open questions at the time
    • Relative weight of these regulators across tissues unknown
    • Single-lab mechanisms
  15. 2023 High

    Mechanistic studies tied FUT8 to degradation pathways and fibrosis signaling, showing defucosylation triggers chaperone-mediated autophagy of B7H3 and that FUT8-galectin-3 and FUT8-TLR3 axes drive fibrotic and inflammatory responses.

    Evidence Glycosite mutants, HSC70/LAMP2A co-IP, CMA assays, FUT8-Gal-3 co-IP, conditional FUT8 KO, and in vivo CRC, lung fibrosis, and renal IRI models

    PMID:36073215 PMID:37432656 PMID:37537172

    Open questions at the time
    • Generality of CMA-coupled degradation to other substrates untested
    • Direct versus indirect interactions for Gal-3 axis not fully resolved
  16. 2024 Medium

    FUT8 was established as a trafficking and stabilization factor for diverse glycoproteins—TMEM67 in cilia, SEMA7A, CD36, GLUT1, and Cntn2—linking core fucosylation to ciliogenesis, metabolism, apoptosis, and neuronal development.

    Evidence Co-IP, glycosite-specific mutants, autophagy/half-life assays, conditional and global Fut8 KO mice, and rescue experiments across cilia, neuron, kidney, and epithelial systems

    PMID:38548747 PMID:39563263 PMID:39604780 PMID:40728580 PMID:41027183

    Open questions at the time
    • Tissue-specific dominance among many substrates unclear
    • Several findings from single labs
  17. 2024 Medium

    Mechanism-based small-molecule FUT8 inhibitors that bind only in the presence of GDP were developed, validating the catalytic mechanism and enabling cellular suppression of core fucosylation.

    Evidence High-throughput screening, SPR, mechanistic covalent-inhibition studies, and cell-based EGFR/T-cell signaling assays

    PMID:39340265

    Open questions at the time
    • In vivo selectivity and pharmacology not fully characterized in this study
  18. 2025 High

    Genetic and pharmacological evidence established FUT8 as a regulator of platelet receptor function, thrombosis, viral entry, atherosclerosis, and reproduction, identifying defined substrates including GPVI, αIIbβ3, aminopeptidase N, and Unc5b.

    Evidence Glycoproteomics, binding/aggregometry assays, glycosite mutants, platelet-specific and global Fut8 KO mice, FDW028 inhibitor, viral entry assays, and ApoE-/- and ovary models

    PMID:36670464 PMID:40262667 PMID:40473957 PMID:42149951 PMID:42237907

    Open questions at the time
    • Therapeutic window for FUT8 inhibition across these systems undefined
    • Cross-species conservation of substrate sites incompletely mapped

Open questions

Synthesis pass · forward-looking unresolved questions
  • How FUT8 selects among its many substrates in a given cell type, and how its domain-mediated localization, dimerization, and RPN1 coupling are integrated to set fucosylation output in vivo, remains unresolved.
  • No unified model linking substrate-selection rules to in vivo glycoproteome
  • Atomic structure of the catalytically competent dimer/RPN1 complex lacking
  • Quantitative ranking of physiologically dominant substrates per tissue unknown

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0016740 transferase activity 5 GO:0140096 catalytic activity, acting on a protein 5
Localization
GO:0005783 endoplasmic reticulum 2 GO:0005794 Golgi apparatus 1 GO:0005886 plasma membrane 1
Pathway
R-HSA-162582 Signal Transduction 4 R-HSA-1643685 Disease 3 R-HSA-392499 Metabolism of proteins 3 R-HSA-168256 Immune System 2 R-HSA-109582 Hemostasis 1
Partners
B7H3EGFRHSPA8LGALS3RPN1SEMA7ATMEM67UNC5B

Evidence

Reading pass · 42 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2004 FUT8 encodes an α-1,6-fucosyltransferase that catalyzes transfer of fucose from GDP-fucose to the core N-acetylglucosamine of N-glycans via an α-1,6-linkage; knockout of both FUT8 alleles in CHO cells produces completely defucosylated antibodies with ~100-fold enhanced ADCC activity via stronger FcγRIIIa binding. Sequential homologous recombination knockout in CHO cells; ADCC assay; FcγRIIIa binding assay Biotechnology and bioengineering High 15352059
2006 Crystal structure of human FUT8 at 2.6 Å resolution reveals three domains: an N-terminal coiled-coil (α-helical) domain, a GT-B fold catalytic domain with a Rossmann fold for donor (GDP-fucose) binding, and a C-terminal SH3 domain. Conserved residues in three regions participate in the Rossmann fold and act as the donor binding site or in catalysis. X-ray crystallography at 2.6 Å resolution Glycobiology High 17172260
2005 FUT8 catalyzes GDP-fucose transfer via a rapid equilibrium random mechanism. The enzyme strongly recognizes the base portion and diphosphoryl group of GDP-β-L-fucose; two conserved neighboring arginine residues play an important role in donor substrate binding. Recombinant human FUT8 produced in baculovirus-infected insect cells; kinetic analysis; inhibition studies with GDP-fucose derivatives Glycobiology High 16344263
2006 In Fut8 knockout mice, TGF-β1 receptor activation and signaling are markedly dysregulated, causing overexpression of MMPs (MMP12, MMP13) and downregulation of extracellular matrix proteins such as elastin, contributing to emphysema-like lung destruction. Therapeutic administration of exogenous TGF-β1 rescued the knockout mice from emphysema. Loss of core fucosylation on EGF and PDGF receptors also downregulates receptor-mediated signaling; reintroduction of Fut8 rescues these signaling impairments. Fut8 knockout mouse model; TGF-β1 rescue experiment; Fut8 gene reintroduction into null cells Methods in enzymology High 17132494
2006 Loss of core fucosylation in Fut8-null mouse cells impairs LRP-1-mediated endocytosis of IGFBP-3, leading to markedly elevated serum IGFBP-3 levels in Fut8-/- mice. Re-introduction of Fut8 restores LRP-1 endocytic activity. Fut8 knockout mouse model; endocytosis assay; Fut8 gene reintroduction; serum IGFBP-3 measurement Journal of biochemistry High 16567404
2009 Fut8 is required for expression of VEGFR-2; loss of Fut8 in knockout mice suppresses VEGFR-2 mRNA and protein expression, increases ceramide levels (an apoptosis inducer), and increases TUNEL-positive septal cells, contributing to emphysema-like lung changes. Fut8 knockout mouse model; siRNA knockdown in A549 and TGP49 cells; TUNEL assay; ceramide measurement Journal of biochemistry Medium 19179362
2012 Donor substrate GDP-fucose binds FUT8 with guanine specifically recognized by His363 and Asp453, the pyrophosphate contributes major binding affinity, and Arg365 contacts both the β-phosphate and the fucose moiety simultaneously. STD NMR; surface plasmon resonance; molecular dynamics simulation; structural analogy with cePOFUT Biochimica et biophysica acta Medium 22982178
2013 Knockdown of Fut8 in PC12 cells promotes neurite formation and induction of neurofilament expression by increasing phospho-Smad2 levels via enhanced activin receptor signaling. α-1,6-Fucosylation on activin receptors negatively regulates activin-mediated signaling (reduced fucosylation on activin receptors in KD cells without changing total receptor expression). Restoration of Fut8 expression rescues these changes, demonstrating Fut8 plays a dual opposing role in TGF-β/activin-mediated signaling. siRNA knockdown; Fut8 gene restoration; phospho-Smad2 western blot; neurite formation assay; activin receptor inhibition FASEB journal Medium 23796784
2013 FUT8 overexpression inhibits hemoglobin production during erythroid differentiation of murine erythroleukemia and K562 human cells. The donor substrate-binding domain and a flexible loop of FUT8 are essential for this inhibitory function. c-Myc and c-Myb positively regulate Fut8 expression; FUT8 shRNA induces hemoglobin production and increases transferrin receptor/glycophorin A-positive cells. Overexpression and shRNA knockdown; hemoglobin assay; domain/loop mutagenesis; flow cytometry The Journal of biological chemistry Medium 23609441
2016 FUT8 (mammalian α1,6-fucosyltransferase) is the sole enzyme responsible for GnT-I-independent core fucosylation of high-mannose N-glycans; in HEK293S GnT-I-/- cells, FUT8 knockdown abolishes core fucosylation of Man5GlcNAc2 glycoforms, whereas FUT8 overexpression produces fully core-fucosylated high-mannose glycoforms. Stable FUT8 knockdown and overexpression in HEK293S GnT-I-/- cells; glycan mass spectrometry analysis of EPO The Journal of biological chemistry High 27008861
2017 FUT8-mediated core fucosylation of TGF-β receptor complexes facilitates TGF-β binding and enhances downstream signaling in breast carcinoma cells, promoting EMT and invasion. FUT8 knockdown (shRNA or CRISPR) suppresses invasiveness of highly aggressive breast cancer cells and impairs lung metastasis in vivo. Lentivirus gain-of-function; shRNA/CRISPR loss-of-function; lectin blot; luciferase assay; in vitro ligand binding assay; transwell invasion; mammary fat pad xenograft Breast cancer research : BCR High 28982386
2017 FUT8 is a driver of melanoma metastasis; FUT8 silencing suppresses invasion and tumor dissemination. Glycoprotein targets of FUT8 are enriched in cell migration proteins including L1CAM; core fucosylation by FUT8 impacts L1CAM cleavage and L1CAM-supported invasion. In vitro invasion assay; in vivo tumor dissemination model; glycoproteomic identification of FUT8 targets; FUT8 silencing Cancer cell High 28609658
2020 The SH3 domain of FUT8 is essential for enzymatic activity (both in cells and in vitro); His-535 in the SH3 domain is the critical residue for catalytic activity. The SH3 domain also controls FUT8 trafficking to the cell surface. FUT8 binds ribophorin I (RPN1), a subunit of the oligosaccharyltransferase complex, in an SH3-dependent manner; RPN1 knockdown decreases FUT8 activity and core fucose levels, indicating RPN1 stimulates FUT8 activity. Truncated FUT8 constructs; immunofluorescence; FACS; cell-surface biotinylation; proteomics; LC-ESI-MS; His-535 mutagenesis; RPN1 siRNA knockdown The Journal of biological chemistry High 32350116
2020 The α-helical (N-terminal coiled-coil) and SH3 domains of FUT8 are both required for full enzymatic activity and form the basis of FUT8 homodimerization via intermolecular hydrophobic interactions of α-helical domains. In vivo cross-linking experiments show the SH3 domain is positioned in close proximity to the α-helical domain in an intermolecular manner, forming the active quaternary structure. Domain truncation; site-directed mutagenesis; in vivo disulfide cross-linking; heterologous expression in Sf21/COS-1 cells; SDS-PAGE enzymatic activity assay Biochimica et biophysica acta. General subjects Medium 32147455
2020 FUT8 crystal structures in complex with a donor substrate analog (GDP) and four distinct glycan acceptors reveal: active site loop ordering correlates with increased GDP occupancy (induced-fit binding); binding site complementarity and steric hindrance tune substrate affinity; the G0 biantennary complex N-glycan is preferred. FUT8 structure comparison with other fucosyltransferases identifies conserved and divergent GT-B fold features for donor/acceptor recognition. X-ray crystallography of multiple FUT8-ligand complexes; active site mutagenesis with kinetic analysis; glycan acceptor library specificity assay The Journal of biological chemistry High 33004438
2020 FUT8 overexpression in prostate cancer cells upregulates cell-surface EGFR and corresponding downstream signaling, leading to increased cell survival in androgen-depleted conditions (castration resistance). Castration in xenograft models induces FUT8 overexpression associated with increased EGFR expression. Proteomic analysis; FUT8 overexpression; EGFR surface expression measurement; androgen deprivation in vitro and xenograft Cancers Medium 32085441
2020 FUT8 core fucosylation of EGFR is required for EGFR overactivation in keratinocytes; FUT8 loss-of-function reduces EGFR/AKT signaling, reduces ligand-induced EGFR dimerization, slows EGF-EGFR complex trafficking to the perinuclear region, and ameliorates psoriasis-like phenotype in a conditional knockout mouse model. shFUT8; FUT8 gain-of-function; EGFR signaling by western blot; EGFR dimerization assay; trafficking assay; conditional FUT8 KO in IL-23 psoriasis mouse model The Journal of investigative dermatology High 32888953
2021 FUT8 catalyzes core fucosylation of B7H3 (CD276) N-glycans in TNBC cells, which stabilizes B7H3 protein and maintains its high expression level, contributing to immunosuppression. FUT8 knockdown reduces glycosylated B7H3-mediated immunosuppressive function. FUT8 knockdown; glycoprotein stability assay; immune functional assay; combination with anti-PDL1 in B7H3-positive tumor model Nature communications High 33976130
2021 FUT8 substrate specificity is regulated by the glycan structure and protein/peptide environment. FUT8 recognizes all sugar units of the G0 N-glycan (shown by STD NMR) and most residues of the Asn-X-Thr sequon. Prior FUT8 binding to GDP is required for optimal N-glycan recognition. The underlying peptide influences fucosylation of paucimannose and high-mannose N-glycans but not complex-type N-glycans. STD NMR; in vitro FUT8 assay with N-glycopeptide library; CHO cell glycoengineering; glycoproteomic analysis ACS catalysis High 35662980
2021 FUT8 overexpression increases delivery of MUC1 to the plasma membrane and extracellular release of MUC2 and MUC5AC. Mucins secreted by FUT8-overexpressing cells are more resistant to removal from the cell surface. FUT8 KD causes intracellular MUC1 accumulation and alters the MUC2:MUC5AC ratio. Fut8-/- mice show a thinner proximal colon mucus layer with altered neutral-to-acidic mucin ratio. FUT8 overexpression/KD in HT29-18N2 cells; mucin trafficking assay; Fut8-/- mouse colonic mucus analysis; mucin resistance assay Proceedings of the National Academy of Sciences of the United States of America High 36252012
2021 FUT8 modifies α1,6-fucosylation of IGF-1 receptor (IGF-1R), regulates IGF-1-dependent activation of IGF-1R, and regulates downstream MAPK and PI3K/Akt signaling in trophoblastic cells. FUT8 knockdown suppresses proliferation, EMT, migration and invasion of JAR and JEG-3 cells. siRNA knockdown; immunoprecipitation; IGF-1R phosphorylation assay; functional cell assays Placenta Medium 30712666
2022 The FUT8 stem region (two α-helices) is essential for FUT8 multimer (oligomer) formation but not for catalytic activity per se. Loss of the stem region destabilizes FUT8 protein, increases ER localization, and shortens its half-life. The first helix of the stem region is critical for multimer formation. FUT8 stem deletion mutants expressed in FUT8-KO HEK293 cells; immunoprecipitation; native-PAGE; subcellular localization by immunofluorescence; half-life measurement The Journal of biological chemistry High 36336076
2023 FUT8-mediated core fucosylation is required for amyloid-β oligomer (AβO)-induced pro-inflammatory activation of human iPSC-derived microglia. FUT8/core fucosylation inhibition reduces pro-inflammatory cytokines, suppresses p38MAPK activation, and rectifies phagocytic deficits. p53 binds two consensus sites in the FUT8 promoter and p53 knockdown abolishes FUT8 overexpression in AβO-activated microglia, placing FUT8 downstream of p53 in microglial signaling. siRNA-mediated FUT8 KD in human iPSC-derived microglia; fucosylation inhibitor; cytokine assay; p38MAPK assay; phagocytosis assay; ChIP-like p53 promoter binding analysis; p53 siRNA Glia Medium 36692036
2023 FUT8 inhibition (by FUT8 silencing) causes defucosylation at N104 on B7-H3, which allows HSC70 (HSPA8) to bind the 106-110 SLRLQ motif of B7-H3 and drives lysosomal proteolysis of B7-H3 via chaperone-mediated autophagy (CMA) pathway. A selective small-molecule FUT8 inhibitor FDW028 recapitulates this mechanism and prolongs survival in CRC pulmonary metastasis models. FUT8 silencing; site-specific glycan mutants (N104); HSC70/LAMP2A co-IP; CMA pathway assay; FDW028 inhibitor characterization; in vivo mouse model Cell death & disease High 37537172
2023 FUT8 regulates TGF-β1-induced pulmonary fibroblast (MRC-5) proliferation, migration and fibrosis by interacting with galectin-3 (Gal-3), as demonstrated by co-immunoprecipitation. FUT8 silencing downregulates Gal-3 expression and inhibits FAK/Akt signaling; Gal-3 overexpression reverses the effects of FUT8 silencing. Co-immunoprecipitation; siRNA knockdown; western blot; CCK-8; wound healing; bleomycin mouse model with sh-FUT8 Nan fang yi ke da xue xue bao Medium 36073215
2024 FUT8 catalyzes core fucosylation of SEMA7A at N-linked glycosylation sites (Asn 105, 157, 258, 330, and 602) via direct protein-protein interaction. Core fucosylation is required for SEMA7A intracellular trafficking from cytoplasm to cytomembrane. EGF increases SEMA7A binding affinity to FUT8, enhancing fucosylation; TGF-β1 promotes SEMA7A glycosylation via EMT induction. Co-IP (FUT8-SEMA7A interaction); glycosite-specific mutants; subcellular trafficking assay; EGF/TGF-β1 treatment International journal of oral science Medium 38548747
2024 A selective FUT8 inhibitor with KD = 49 nM binds FUT8 only in the presence of GDP (product of the enzymatic reaction), generates a reactive naphthoquinone methide derivative at the active site that covalently reacts with FUT8 (mechanism-based inhibition). Prodrug derivatization enables cellular suppression of core fucose expression and subsequent EGFR and T-cell signaling. High-throughput screening; SPR binding assay; mechanistic inhibitor studies; cell-based EGFR and T-cell signaling assays Angewandte Chemie (International ed. in English) Medium 39340265
2024 FUT8 interacts with TMEM67 (a ciliary transition zone component) and catalyzes its core fucosylation, which stabilizes TMEM67 by preventing its degradation via autophagy. Loss of core fucosylation of TMEM67 causes mislocalization from the transition zone. Fut8-deficient mice exhibit ciliary defects in kidney, brain, and trachea. Mass spectrometry proteomics; Co-IP (FUT8-TMEM67); core fucosylation assay; autophagy degradation assay; Fut8-deficient mouse ciliary phenotype analysis The Journal of cell biology High 40728580
2024 FUT8 upregulates CD36 expression and its core fucosylation level in pericytes, contributing to activation of the mitochondrial-dependent apoptosis signaling pathway and pericyte-myofibroblast transition in AKI-to-CKD progression. IP and confocal immunofluorescence for CD36 core fucosylation; IRI mouse model; H/R cell model; flow cytometry apoptosis; JC-1 mitochondrial membrane potential Molecular medicine (Cambridge, Mass.) Medium 39563263
2023 Renal tubular epithelial cell-specific deletion of FUT8 ameliorates IRI-induced renal interstitial inflammation and fibrosis transition primarily via the TLR3 core fucosylation-NF-κB signaling pathway. TEC-specific FUT8 conditional knockout mouse; IRI model; TLR3-NF-κB pathway analysis FASEB journal Medium 37432656
2021 FUT8 modifies core fucosylation of TNF receptors (TNFRs) in osteosarcoma; lower fucosylation of TNFRs activates the non-canonical NF-κB signaling pathway, decreasing mitochondria-dependent apoptosis in OS cells. FUT8 gain/loss-of-function; TNF receptor core fucosylation assay; NF-κB pathway analysis; apoptosis assay Cell death & disease Medium 34857735
2020 FUT8-mediated core fucosylation of EGFR in cancer-associated fibroblasts (CAFs) promotes their cancer-promoting capacity in NSCLC; FUT8 overexpression in CAFs promotes invasive TME formation in vitro and in vivo via EGFR signaling regulation. 3D-printed co-culture device; in vivo CAF/NSCLC co-injection; EGFR signaling analysis; FUT8 overexpression/KD American journal of cancer research Medium 32266093
2025 FUT8-mediated core fucosylation of platelet adhesion receptors GPVI and integrin αIIbβ3 enhances their affinity/binding to type I collagen and fibrinogen respectively, leading to greater platelet activation and downstream signaling. Platelet-specific Fut8 deletion in two murine thrombosis models inhibits platelet activation and thrombus formation; FDW028 FUT8 inhibitor reduces platelet aggregation and protects mice from lethal thrombosis. Glycomics/glycoproteomics; binding affinity assay; platelet aggregometry; phospho-specific antibody signaling; murine thrombosis models; platelet-specific conditional KO; pharmacological FUT8 inhibition Arteriosclerosis, thrombosis, and vascular biology High 42237907
2025 FUT8 core fucosylation of GLUT1 at Asn45 (N45) increases GLUT1 protein half-life, enhancing glucose uptake and glycolytic flux (increased ECAR, ATP, lactate production) in HDM-stimulated bronchial epithelial cells; this drives EMT and release of IL-25 and IL-33. GLUT1 N45Q mutant (cannot be core-fucosylated) fails to rescue phenotype after FUT8 KD. FUT8 KD/OE; lectin pull-down; GLUT1 site-specific mutant (N45Q); ECAR measurement; IL-25/IL-33 ELISA; GLUT1 half-life assay Biochemical and biophysical research communications Medium 41027183
2021 Quantitative glycoproteomics identified 140 common core-fucosylated target glycoproteins of FUT8 in highly invasive breast cancer cells. Among novel targets, core fucosylation of integrin αvβ5 is crucial for cell adhesion to vitronectin, and core fucosylation of IL6ST supports enhanced IL-6 and oncostatin M signaling relevant to breast cancer EMT and metastasis. Quantitative glycoproteomics (FUT8-KO vs WT); LCA blotting; LC-MS/MS validation; integrin adhesion assay Breast cancer research : BCR Medium 35303925
2026 FUT8, via its fucosyltransferase activity, mediates core fucosylation of aminopeptidase N (APN) at specific N-glycosylation sites (pAPN N736, canine APN N747, feline APN N740), which is required for binding of alphacoronavirus spike proteins to APN and viral entry. pAPN lacking FUT8-mediated modification shows no binding to TGEV RBD. FUT8 KO cells; viral entry assay; APN glycoproteomic analysis; TGEV RBD binding assay PLoS pathogens High 42149951
2025 FUT8 regulates macrophage migration in atherosclerosis by mediating α-1,6 fucosylation of the guidance receptor Unc5b (primarily in the ER); hypofucosylation of Unc5b promotes macrophage emigration and delays atherosclerotic progression via activation of the CDC42/PAK pathway. Conversely, Fut8-mediated hyperfucosylation of Unc5b inactivates CDC42/PAK and reduces migration, promoting atherosclerosis via ferroptosis (P53/SLC7A11/GPX4 pathway). IP assay for Fut8-Unc5b interaction; Unc5b fucosylation site mutants; ApoE-/- mouse model; siRNA/OE of Unc5b; wound healing; CDC42/PAK pathway analysis; ferroptosis assay Cell & bioscience / Free radical biology & medicine Medium 36670464 40262667
2024 FUT8 deficiency in cerebellar granule neuron progenitors impairs their proliferation and differentiation, compromises neuronal development, synaptic physiology and motor coordination. Mechanistically, Fut8 deficiency reduces Contactin 2 (Cntn2/neural cell adhesion molecule) expression; ectopic Cntn2 rescues the neuronal defects caused by Fut8 deficiency. Conditional cerebellar GNP-specific Fut8 KO; proliferation/differentiation assays; synaptic physiology; motor coordination test; Cntn2 expression rescue Molecular neurobiology Medium 39604780
2019 HCV-induced FUT8 promotes proliferation of Huh7.5.1 cells by activating PI3K-AKT-NF-κB signaling and stimulates expression of drug-resistant proteins P-glycoprotein (P-gp) and MRP1, enhancing 5-FU chemoresistance. FUT8 silencing reduces proliferation and restores 5-FU sensitivity. FUT8 siRNA knockdown; PI3K-AKT-NF-κB pathway analysis; P-gp/MRP1 western blot; 5-FU cytotoxicity/LDH assay; flow cytometry Viruses Medium 31022917
2022 The transcription factor LEF1 directly regulates FUT8 transcription; the lncRNA LEF1-AS1 recruits MLL1 to the LEF1 promoter, inducing H3K4me3 methylation and LEF1 expression, which in turn activates FUT8 transcription via the Wnt/β-catenin pathway. FUT8 overexpression rescues the suppressive effects of LEF1-AS1 knockdown on colorectal cancer cell malignancy. ChIP; RIP; EMSA; luciferase reporter assay; rescue OE experiment Digestive diseases and sciences Medium 34021424
2020 Caveolin-1 promotes FUT8 expression by activating Wnt/β-catenin signaling, leading to downstream TCF/LEF binding to the FUT8 promoter and transcriptional activation. Cav-1 OE in low-Fut8 HCC cells induces Wnt/β-catenin activation and Fut8 upregulation; Cav-1 KD in high-Fut8 cells suppresses this. Cav-1 OE/KD; Wnt/β-catenin pathway analysis; TCF/LEF binding to FUT8 promoter; western blot Cell biology international Medium 32710651
2025 FUT8 ablation in granulosa cells reduces cAMP production following FSH stimulation (reduced FSHR signaling), and decreases expression of FIGLA and embryonic development genes. Fut8-/- mouse oocytes exhibit abnormal zona pellucida formation and impaired embryonic development. FUT8-KD human granulosa cells (KGN-KD); Fut8-/- mouse ovary; cAMP assay after FSH; FIGLA/zona pellucida gene expression; embryo development assay Journal of assisted reproduction and genetics Medium 40473957

Source papers

Stage 0 corpus · 100 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2004 Establishment of FUT8 knockout Chinese hamster ovary cells: an ideal host cell line for producing completely defucosylated antibodies with enhanced antibody-dependent cellular cytotoxicity. Biotechnology and bioengineering 432 15352059
2017 A Systems Biology Approach Identifies FUT8 as a Driver of Melanoma Metastasis. Cancer cell 248 28609658
2017 FUT8 promotes breast cancer cell invasiveness by remodeling TGF-β receptor core fucosylation. Breast cancer research : BCR 181 28982386
2021 FUT8-mediated aberrant N-glycosylation of B7H3 suppresses the immune response in triple-negative breast cancer. Nature communications 154 33976130
2004 Engineering Chinese hamster ovary cells to maximize effector function of produced antibodies using FUT8 siRNA. Biotechnology and bioengineering 123 15515168
2006 Crystal structure of mammalian alpha1,6-fucosyltransferase, FUT8. Glycobiology 117 17172260
2007 Double knockdown of alpha1,6-fucosyltransferase (FUT8) and GDP-mannose 4,6-dehydratase (GMD) in antibody-producing cells: a new strategy for generating fully non-fucosylated therapeutic antibodies with enhanced ADCC. BMC biotechnology 114 18047682
2010 Highly efficient deletion of FUT8 in CHO cell lines using zinc-finger nucleases yields cells that produce completely nonfucosylated antibodies. Biotechnology and bioengineering 113 20564614
2003 Expression of alpha1,6-fucosyltransferase (FUT8) in papillary carcinoma of the thyroid: its linkage to biological aggressiveness and anaplastic transformation. Cancer letters 82 14568171
2006 Phenotype changes of Fut8 knockout mouse: core fucosylation is crucial for the function of growth factor receptor(s). Methods in enzymology 73 17132494
2016 Comprehensive N-glycan profiles of hepatocellular carcinoma reveal association of fucosylation with tumor progression and regulation of FUT8 by microRNAs. Oncotarget 65 27533464
2013 Effects of microRNAs on fucosyltransferase 8 (FUT8) expression in hepatocarcinoma cells. PloS one 63 24130780
2021 FUT8 and Protein Core Fucosylation in Tumours: From Diagnosis to Treatment. Journal of Cancer 56 34093814
2018 Biallelic Mutations in FUT8 Cause a Congenital Disorder of Glycosylation with Defective Fucosylation. American journal of human genetics 56 29304374
2005 Reaction mechanism and substrate specificity for nucleotide sugar of mammalian alpha1,6-fucosyltransferase--a large-scale preparation and characterization of recombinant human FUT8. Glycobiology 56 16344263
2016 Mammalian α-1,6-Fucosyltransferase (FUT8) Is the Sole Enzyme Responsible for the N-Acetylglucosaminyltransferase I-independent Core Fucosylation of High-mannose N-Glycans. The Journal of biological chemistry 55 27008861
2023 FDW028, a novel FUT8 inhibitor, impels lysosomal proteolysis of B7-H3 via chaperone-mediated autophagy pathway and exhibits potent efficacy against metastatic colorectal cancer. Cell death & disease 50 37537172
2020 α1,6-Fucosyltransferase (FUT8) regulates the cancer-promoting capacity of cancer-associated fibroblasts (CAFs) by modifying EGFR core fucosylation (CF) in non-small cell lung cancer (NSCLC). American journal of cancer research 48 32266093
2021 FUT8-Directed Core Fucosylation of N-glycans Is Regulated by the Glycan Structure and Protein Environment. ACS catalysis 44 35662980
2011 Molecular cloning, characterization, genomic organization and promoter analysis of the α1,6-fucosyltransferase gene (fut8) expressed in the rat hybridoma cell line YB2/0. BMC biotechnology 42 21208406
2020 Impact of Increased FUT8 Expression on the Extracellular Vesicle Proteome in Prostate Cancer Cells. Journal of proteome research 38 32378902
2020 Characterizing human α-1,6-fucosyltransferase (FUT8) substrate specificity and structural similarities with related fucosyltransferases. The Journal of biological chemistry 38 33004438
2006 Loss of core fucosylation of low-density lipoprotein receptor-related protein-1 impairs its function, leading to the upregulation of serum levels of insulin-like growth factor-binding protein 3 in Fut8-/- mice. Journal of biochemistry 37 16567404
2022 The ulcerative colitis-associated gene FUT8 regulates the quantity and quality of secreted mucins. Proceedings of the National Academy of Sciences of the United States of America 35 36252012
2009 Requirement of Fut8 for the expression of vascular endothelial growth factor receptor-2: a new mechanism for the emphysema-like changes observed in Fut8-deficient mice. Journal of biochemistry 35 19179362
2021 FUT8-AS1 Inhibits the Malignancy of Melanoma Through Promoting miR-145-5p Biogenesis and Suppressing NRAS/MAPK Signaling. Frontiers in oncology 34 34094894
2013 α1,6-Fucosylation regulates neurite formation via the activin/phospho-Smad2 pathway in PC12 cells: the implicated dual effects of Fut8 for TGF-β/activin-mediated signaling. FASEB journal : official publication of the Federation of American Societies for Experimental Biology 33 23796784
2010 Enhancement of DNA uptake in FUT8-deleted CHO cells for transient production of afucosylated antibodies. Biotechnology and bioengineering 33 20564613
2020 The SH3 domain in the fucosyltransferase FUT8 controls FUT8 activity and localization and is essential for core fucosylation. The Journal of biological chemistry 32 32350116
2018 FUT8 drives the proliferation and invasion of trophoblastic cells via IGF-1/IGF-1R signaling pathway. Placenta 31 30712666
2011 Alteration in N-glycomics during mouse aging: a role for FUT8. Aging cell 31 21951615
2020 A Comprehensive Analysis of FUT8 Overexpressing Prostate Cancer Cells Reveals the Role of EGFR in Castration Resistance. Cancers 29 32085441
2000 Genomic structure and promoter analysis of the human alpha1, 6-fucosyltransferase gene (FUT8). Glycobiology 26 10814706
2021 Alpha-(1,6)-fucosyltransferase (FUT8) affects the survival strategy of osteosarcoma by remodeling TNF/NF-κB2 signaling. Cell death & disease 24 34857735
2017 Producing defucosylated antibodies with enhanced in vitro antibody-dependent cellular cytotoxicity via FUT8 knockout CHO-S cells. Engineering in life sciences 24 32624826
2020 A lectin-based glycomic approach identifies FUT8 as a driver of radioresistance in oesophageal squamous cell carcinoma. Cellular oncology (Dordrecht, Netherlands) 23 32474852
2018 Enhanced motility and proliferation by miR-10b/FUT8/p-AKT axis in breast cancer cells. Oncology letters 22 30008906
2012 Donor substrate binding and enzymatic mechanism of human core α1,6-fucosyltransferase (FUT8). Biochimica et biophysica acta 22 22982178
2023 Beyond antibody fucosylation: α-(1,6)-fucosyltransferase (Fut8) as a potential new therapeutic target for cancer immunotherapy. Antibody therapeutics 21 37077473
2022 HOTAIR modulates hepatocellular carcinoma progression by activating FUT8/core-fucosylated Hsp90/MUC1/STAT3 feedback loop via JAK1/STAT3 cascade. Digestive and liver disease : official journal of the Italian Society of Gastroenterology and the Italian Association for the Study of the Liver 21 35504805
2006 From glycomics to functional glycomics of sugar chains: Identification of target proteins with functional changes using gene targeting mice and knock down cells of FUT8 as examples. Biochimica et biophysica acta 21 17174880
2024 FUT8-mediated aberrant N-glycosylation of SEMA7A promotes head and neck squamous cell carcinoma progression. International journal of oral science 20 38548747
2023 The role of FUT8-catalyzed core fucosylation in Alzheimer's amyloid-β oligomer-induced activation of human microglia. Glia 20 36692036
2021 LncRNA LEF1-AS1/LEF1/FUT8 Axis Mediates Colorectal Cancer Progression by Regulating α1, 6-Fucosylationvia Wnt/β-Catenin Pathway. Digestive diseases and sciences 20 34021424
2020 FUT8 Remodeling of EGFR Regulates Epidermal Keratinocyte Proliferation during Psoriasis Development. The Journal of investigative dermatology 20 32888953
2022 Production of afucosylated antibodies in CHO cells by coexpression of an anti-FUT8 intrabody. Biotechnology and bioengineering 18 35509261
2021 Glycoproteomic Characterization of FUT8 Knock-Out CHO Cells Reveals Roles of FUT8 in the Glycosylation. Frontiers in chemistry 18 34778211
2019 Bioprocess development of a stable FUT8-/--CHO cell line to produce defucosylated anti-HER2 antibody. Bioprocess and biosystems engineering 18 30982137
2000 Ancestral exonic organization of FUT8, the gene encoding the alpha6-fucosyltransferase, reveals successive peptide domains which suggest a particular three-dimensional core structure for the alpha6-fucosyltransferase family. Molecular biology and evolution 18 11070054
1999 Mapping of the alpha-1,6-fucosyltransferase gene, FUT8, to human chromosome 14q24.3. Cytogenetics and cell genetics 18 10343104
2020 Caveolin-1 upregulates Fut8 expression by activating the Wnt/β-catenin pathway to enhance HCC cell proliferative and invasive ability. Cell biology international 17 32710651
2011 Association of fucosyltransferase 8 (FUT8) polymorphism Thr267Lys with pulmonary emphysema. Journal of human genetics 17 22011814
2022 Quantitative glycoproteomics analysis identifies novel FUT8 targets and signaling networks critical for breast cancer cell invasiveness. Breast cancer research : BCR 16 35303925
2022 FUT8 is regulated by miR-122-5p and promotes malignancies in intrahepatic cholangiocarcinoma via PI3K/AKT signaling. Cellular oncology (Dordrecht, Netherlands) 16 36348252
2021 SNHG1/miR-186/FUT8 regulates cell migration and invasion in oral squamous cell carcinoma. Oral diseases 16 33872442
2020 Involvement of the α-helical and Src homology 3 domains in the molecular assembly and enzymatic activity of human α1,6-fucosyltransferase, FUT8. Biochimica et biophysica acta. General subjects 16 32147455
2019 Hepatitis C Virus-Induced FUT8 Causes 5-FU Drug Resistance in Human Hepatoma Huh7.5.1 Cells. Viruses 15 31022917
2022 The stem region of α1,6-fucosyltransferase FUT8 is required for multimer formation but not catalytic activity. The Journal of biological chemistry 14 36336076
2013 α-1,6-Fucosyltransferase (FUT8) inhibits hemoglobin production during differentiation of murine and K562 human erythroleukemia cells. The Journal of biological chemistry 13 23609441
2024 Development of a FUT8 Inhibitor with Cellular Inhibitory Properties. Angewandte Chemie (International ed. in English) 10 39340265
2024 FUT8 upregulates CD36 and its core fucosylation to accelerate pericyte-myofibroblast transition through the mitochondrial-dependent apoptosis pathway during AKI-CKD. Molecular medicine (Cambridge, Mass.) 10 39563263
2023 Fucosyltransferase 8 (FUT8) and core fucose expression in oxidative stress response. PloS one 10 36780470
2023 FUT8-Mediated Core Fucosylation Promotes the Pulmonary Vascular Remodeling in Pulmonary Arterial Hypertension. Aging and disease 10 37196106
2023 Loss of FUT8 in renal tubules ameliorates ischemia-reperfusion injury-induced renal interstitial inflammation transition to fibrosis via the TLR3-NF-κB pathway. FASEB journal : official publication of the Federation of American Societies for Experimental Biology 10 37432656
2021 Appropriate aglycone modification significantly expands the glycan substrate acceptability of α1,6-fucosyltransferase (FUT8). The Biochemical journal 10 33734311
2016 Expression of α-1,6-fucosyltransferase (FUT8) in rice grain and immunogenicity evaluation of plant-specific glycans. Journal of biotechnology 10 28013072
2024 The Multifaceted Role of FUT8 in Tumorigenesis: From Pathways to Potential Clinical Applications. International journal of molecular sciences 9 38256141
2023 Hypofucosylation of Unc5b regulated by Fut8 enhances macrophage emigration and prevents atherosclerosis. Cell & bioscience 9 36670464
2023 N6 -methyladenosine-modified circFUT8 competitively interacts with YTHDF2 and miR-186-5p to stabilize FUT8 mRNA to promote malignant progression in lung adenocarcinoma. Thoracic cancer 9 37669906
2020 Role of FUT8 expression in clinicopathology and patient survival for various malignant tumor types: a systematic review and meta-analysis. Aging 9 33323540
2014 The α1,6-fucosyltransferase gene (fut8) from the Sf9 lepidopteran insect cell line: insights into fut8 evolution. PloS one 9 25333276
2024 Distinctive domains and activity regulation of core fucosylation enzyme FUT8. Biochimica et biophysica acta. General subjects 7 38218458
2021 Up-regulation of FUT8 inhibits TGF-β1-induced activation of hepatic stellate cells during liver fibrogenesis. Glycoconjugate journal 7 33608773
2025 Targeting fucosyltransferase FUT8 as a prospective therapeutic approach for DLBCL. Oncogenesis 6 39881135
2024 High-Throughput Mass Spectrometry Analysis of N-Glycans and Protein Markers after FUT8 Knockdown in the Syngeneic SW480/SW620 Colorectal Cancer Cell Model. Journal of proteome research 6 38507902
2023 FUT8-AS1/miR-944/Fused in Sarcoma/Transcription Factor 4 Feedback Loop Participates in the Development of Oral Squamous Cell Carcinoma through Activation of Wnt/β-Catenin Signaling Pathway. The American journal of pathology 5 36697118
2025 FUT8 Is a Critical Driver of Prostate Tumour Growth and Can Be Targeted Using Fucosylation Inhibitors. Cancer medicine 4 40387385
2025 Advances in cancer research on FUT8 molecular mechanisms and clinical applications. International journal of surgery (London, England) 4 40497775
2024 Identification of molecular characteristics of FUT8 and alteration of core fucosylation in kidney renal clear cell cancer. Aging 4 38277230
2023 The Association of the Polymorphisms in the FUT8-Related Locus with the Plasma Glycosylation in Post-Traumatic Stress Disorder. International journal of molecular sciences 4 36982780
2002 Assignment of FUT8 to chicken chromosome band 5q1.4 and to human chromosome 14q23.2-->q24.1 by in situ hybridization. Conserved and compared synteny between human and chicken. Cytogenetic and genome research 4 12438718
2024 FUT8 Regulates Cerebellar Neurogenesis and Development Through Maintaining the Level of Neural Cell Adhesion Molecule Cntn2. Molecular neurobiology 3 39604780
2022 Effect and Mechanism Analysis of Pig FUT8 Gene on Resistance to Escherichia coli F18 Infection. International journal of molecular sciences 3 36499043
2025 Fut8 regulated Unc5b hyperfucosylation reduces macrophage emigration and accelerates atherosclerosis development via the ferroptosis pathway. Free radical biology & medicine 2 40262667
2025 FUT8-mediated core fucosylation stabilizes TMEM67 to promote ciliogenesis. The Journal of cell biology 2 40728580
2022 Positive association of serum FUT8 activity with renal tubulointerstitial injury in IgA nephropathy patients. Immunity, inflammation and disease 2 36039648
2025 Exosomal miR-27a-5p inhibits indoxyl sulfate-induced cardiac dysfunction by targeting the USF2/FUT8 axis. Free radical biology & medicine 1 40992517
2022 [FUT8 modulates galectin-3 expression to regulate TGF-β1-mediated fibrosis of lung fibroblasts]. Nan fang yi ke da xue xue bao = Journal of Southern Medical University 1 36073215
2026 Huaier-derived neutral polysaccharide WHPB mitigates renal fibrosis via CSF-1R/PI3K/AKT-mediated FUT8 inhibition. Phytomedicine : international journal of phytotherapy and phytopharmacology 0 41505915
2026 CRISPR-based precise methylation of specific FUT8 promoter regions allows isolation of CHO cells with a fine-tuned glycoprofile. Journal of biotechnology 0 41506457
2026 Fut8-Mediated Core Fucosylation of Toll-Like Receptor 4 Exacerbates Periodontitis Via Hyperactivation of NF-κB Signalling. International dental journal 0 41653834
2026 Core fucosylation of NCEH1 by FUT8 promotes progression of high-grade serous ovarian cancer by driving tumor-associated macrophage M2 polarization. Oncogene 0 41786877
2026 FUT8 reprograms glycolytic metabolism to promote PKM2 lactylation and drive clear cell renal cell carcinoma progression. Cell death discovery 0 41857011
2026 FUT8-mediated core fucosylation of receptor APN drives entry of multiple alphacoronaviruses. PLoS pathogens 0 42149951
2026 FUT8-Dependent Core Fucosylation: Essential for Platelet Function and a Target in Thrombosis. Arteriosclerosis, thrombosis, and vascular biology 0 42237907
2025 Clinicopathologic significance of FUT8, STX4, and calpain2 expression in ovarian cancer. American journal of translational research 0 39959200
2025 Loss of FUT8 impairs embryonic development by reducing cAMP production in granulosa cells. Journal of assisted reproduction and genetics 0 40473957
2025 FUT8 promotes HDM-induced glycolysis, epithelial-mesenchymal transition and inflammation in bronchial epithelial cells by inducing N-glycosylation modification of GLUT1. Biochemical and biophysical research communications 0 41027183
2025 Genome-wide CRISPR screen identifies ALG5, ALG6, NF2, and FUT8 as key host proteins involved in transmissible gastroenteritis virus infection. International journal of biological macromolecules 0 41205942
2024 Knockdown of LINC01128 Downregulates FUT8 to Inhibit OxLDL-Induced Vascular Smooth Muscle Cell Apoptosis in Atherosclerosis. Discovery medicine 0 38531797

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