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GDP-6-alkynyl fucose + protein
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6-alkynyl fucose is efficiently incorporated onto EGF repeats, TSRs, and N-glycan on Lfng and N-glycans on a number of proteins in crude lysates of CHO cells, e.g. the O-fucosylation site in EGF3 of mouse Notch1 and elongated by Lfng, mass spectrometry analysis, overview. Using the Cu(I)-catalyzed azide-alkyne cycloaddition (CuAAC), or click reaction, azido-biotin allows tagging and detection of 6AF-modified proteins
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GDP-beta-L-fucose + factor VII EGF
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GDP-beta-L-fucose + protein
GDP + ?
GDP-Fuc + biotin-DHPCTQALGNPCLNGGSCVPREATYECLCPGGFSGLHCEKG
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peptide of the fourth EGF domain of agrin (EGF4) is used as an acceptor substrate with biotin conjugated at the N-terminus
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GDP-fucose + TSR1
GDP + fucosyl-TSR1
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GDP-fucose + TSR2
GDP + fucosyl-TSR2
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GDP-fucose + TSR3
GDP + fucosyl-TSR3
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GDP-fucose + TSR4
GDP + fucosyl-TSR4
GDP-L-fucose + micronemal protein 2
GDP + fucosylated micronemal protein 2
GDP-L-fucose + Notch protein
GDP + fucosylated Notch protein
the enzyme fucosylates the epidermal growth factor (EGF)-like domains found in cell-surface and secreted glycoproteins including Notch and its ligands
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GDP-L-fucose + protein
GDP + fucosylated protein
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GDP-L-fucose + transcription regulators DELLA
GDP + fucosylated transcription regulators DELLA
additional information
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GDP-beta-L-fucose + factor VII EGF
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GDP-beta-L-fucose + factor VII EGF
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GDP-beta-L-fucose + protein
GDP + ?
protein O-fucosyltransferases 1 and 2 (PoFUT1 and PoFUT2) are the enzymes responsible for this protein O-fucosylation and selectively glycosylate specific residues in epidermal growth factor-like (EGF) repeats and thrombospondin type I repeats (TSRs). PoFUT1 glycosylates epidermal growth factor-like (EGF) repeats within the consensus sequence C2-X-X-X-X-S/T-C3
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GDP-beta-L-fucose + protein
GDP + ?
protein O-fucosyltransferases 1 and 2 (PoFUT1 and PoFUT2) are the enzymes responsible for this protein O-fucosylation and selectively glycosylate specific residues in epidermal growth factor-like (EGF) repeats and thrombospondin type I repeats (TSRs). PoFUT2 glycosylates thrombospondin type I repeats (TSRs) containing Ser/Thr residues located in the consensus sequences C1-X-X-S/T-C2 or C2-X-X-S/T-C3 of TSRs of groups 1 and 2
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GDP-beta-L-fucose + protein
GDP + ?
SN1-like mechanism. PoFUT1 glycosylates epidermal growth factor-like (EGF) repeats within the consensus sequence C2-X-X-X-X-S/T-C3
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GDP-beta-L-fucose + protein
GDP + ?
SN2-like mechanism. PoFUT2 glycosylates thrombospondin type I repeats (TSRs) containing Ser/Thr residues located in the consensus sequences C1-X-X-S/T-C2 or C2-X-X-S/T-C3 of TSRs of groups 1 and 2
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GDP-beta-L-fucose + protein
GDP + ?
protein O-fucosyltransferases 1 and 2 (PoFUT1 and PoFUT2) are the enzymes responsible for this protein O-fucosylation and selectively glycosylate specific residues in epidermal growth factor-like (EGF) repeats and thrombospondin type I repeats (TSRs). PoFUT1 glycosylates epidermal growth factor-like (EGF) repeats within the consensus sequence C2-X-X-X-X-S/T-C3
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GDP-beta-L-fucose + protein
GDP + ?
protein O-fucosyltransferases 1 and 2 (PoFUT1 and PoFUT2) are the enzymes responsible for this protein O-fucosylation and selectively glycosylate specific residues in epidermal growth factor-like (EGF) repeats and thrombospondin type I repeats (TSRs). PoFUT2 glycosylates thrombospondin type I repeats (TSRs) containing Ser/Thr residues located in the consensus sequences C1-X-X-S/T-C2 or C2-X-X-S/T-C3 of TSRs of groups 1 and 2
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GDP-beta-L-fucose + protein
GDP + ?
SN1-like mechanism. PoFUT1 glycosylates epidermal growth factor-like (EGF) repeats within the consensus sequence C2-X-X-X-X-S/T-C3
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?
GDP-beta-L-fucose + protein
GDP + ?
SN2-like mechanism. PoFUT2 glycosylates thrombospondin type I repeats (TSRs) containing Ser/Thr residues located in the consensus sequences C1-X-X-S/T-C2 or C2-X-X-S/T-C3 of TSRs of groups 1 and 2
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GDP-beta-L-fucose + protein
GDP + ?
protein O-fucosyltransferases 1 and 2 (PoFUT1 and PoFUT2) are the enzymes responsible for this protein O-fucosylation and selectively glycosylate specific residues in epidermal growth factor-like (EGF) repeats and thrombospondin type I repeats (TSRs). PoFUT1 glycosylates epidermal growth factor-like (EGF) repeats within the consensus sequence C2-X-X-X-X-S/T-C3
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GDP-beta-L-fucose + protein
GDP + ?
SN1-like mechanism. PoFUT1 glycosylates epidermal growth factor-like (EGF) repeats within the consensus sequence C2-X-X-X-X-S/T-C3
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GDP-fucose + TSR4
GDP + fucosyl-TSR4
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GDP-fucose + TSR4
GDP + fucosyl-TSR4
GDP-fucose binding mode, overview. Activity with recombinant TSR4 mutants expressed in HEK293Tcells
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GDP-L-fucose + micronemal protein 2
GDP + fucosylated micronemal protein 2
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GDP-L-fucose + micronemal protein 2
GDP + fucosylated micronemal protein 2
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GDP-L-fucose + Notch
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Drosophila sp. (in: flies)
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O-fucosylation of Notch, catalytic and non-catalytic activities
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GDP-L-fucose + Notch
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Pofut1 transfers fucose in the endoplasmic reticulum, transfers fucose to Ser or Thr residues of epidermal growth factor-like repeats
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GDP-L-fucose + transcription regulators DELLA
GDP + fucosylated transcription regulators DELLA
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GDP-L-fucose + transcription regulators DELLA
GDP + fucosylated transcription regulators DELLA
O-fucosylation activates DELLA by promoting its interaction with key regulators in brassinosteroid- and light-signaling pathways, including BRASSINAZOLE-RESISTANT1 (BZR1), PHYTOCHROME-INTERACTING-FACTOR3 (PIF3), and PIF4
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additional information
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POFUT1s bind GDP-fucose and EGF repeats, and transfer this monosaccharide into small EGF repeats producing GDP during the reaction
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additional information
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enzyme POFUT2 fucosylates threonine preferentially over serine and relies on folded TSRs containing the minimal consensus sequence C-X-X-S/T-, substrate specificity, overview
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additional information
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enzyme POFUT2 fucosylates threonine preferentially over serine and relies on folded TSRs containing the minimal consensus sequence C-X-X-S/T-, substrate specificity, overview
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additional information
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fucosylates various synthetic peptides of EGF-1 domain of human factor VII, GDP-mannose, UDP-glucose, UDP-N-acetylglucosamine, UDP-galactose, UDP-H-acetylgalactosamine and UDP-xylose can replace GDP-fucose
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additional information
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links fucose through an O-glycosidic linkage to a conserved serine or threonine residue in of the EGF-1 domain of human factor VII, various synthetic peptides serve as substrates
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additional information
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essential for Notch signaling
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additional information
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Drosophila sp. (in: flies)
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enzyme that glycosylates epidermal growth factorlike domains of Notch, also has a distinct Notch chaperone activity
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additional information
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O-fucosylation of thrombospondin-1 at Ser 377, Thr 432 and Thr 489
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additional information
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adds o-fucose to epidermal growth factor-like repeats
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additional information
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adds o-fucose to epidermal growth factor-like repeats
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additional information
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may be involved in intracellular quality control
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additional information
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the enzyme catalyzes the addition of O-linked fucose to the epidermal growth factor-like repeats of Notch
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additional information
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the enzyme catalyzes the addition of O-linked fucose to the epidermal growth factor-like repeats of Notch
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additional information
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fucose is added exclusively to properly folded Epidermal Growth Factor-like (EGF) repeats and Thrombospondin Type 1 Repeats (TSRs)
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additional information
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fucose is added exclusively to properly folded Epidermal Growth Factor-like (EGF) repeats and Thrombospondin Type 1 Repeats (TSRs)
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additional information
?
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fucose is added exclusively to properly folded Epidermal Growth Factor-like (EGF) repeats and Thrombospondin Type 1 Repeats (TSRs). The O-linked fucose can also be elongated with other sugars
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additional information
?
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fucose is added exclusively to properly folded Epidermal Growth Factor-like (EGF) repeats and Thrombospondin Type 1 Repeats (TSRs). The O-linked fucose can also be elongated with other sugars
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additional information
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enzyme is an essential core member of Notch signaling pathways in mammals
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additional information
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Pofut1 adds fucose to Ser or Thr in the C2-x-x-x-x-(S/T)-C3 consensus sequence. Eliminating any of three highly conserved O-fucose sites at EGF 12, 26, or 27 within mouse Notch1 alters activity.
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additional information
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protein O-fucosyltransferase 1 and protein O-fucosyltransferase 2 add O-linked fucose at distinct consensus sequences in properly folded epidermal growth factor (EGF)-like repeats and thrombospondin type-1 (TSR) repeats, respectively
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additional information
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the enzyme catalyzes O-fucosylation of Notch proteins, twenty potential O-fucosylation sites on EGF-like repeats are present on mouse Notch1, and 13 are known to be modified by O-fucose. Notch2 and Notch3 receptors have 21 and 15 potential O-fucosylation sites, respectively, and are probably predominantly O-fucosylated
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additional information
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the enzyme catalyzes O-fucosylation of Notch proteins, twenty potential O-fucosylation sites on EGF-like repeats are present on mouse Notch1, and 13 are known to be modified by O-fucose. Notch2 and Notch3 receptors have 21 and 15 potential O-fucosylation sites, respectively, and are probably predominantly O-fucosylated
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additional information
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links fucose through an O-glycosidic linkage to a conserved serine or threonine residue in of the EGF-1 domain of human factor VII, various synthetic peptides serve as substrates
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Abortion, Spontaneous
poFUT1 promotes endometrial decidualization by enhancing the O-fucosylation of Notch1.
Abortion, Spontaneous
poFUT1 promotes uterine angiogenesis and vascular remodeling via enhancing the O-fucosylation on uPA.
Abortion, Spontaneous
Progesterone promotes embryo adhesion by upregulating c-Fos/c-Jun transcription factor-mediate poFUT1 expression.
Abortion, Threatened
LIF upregulates poFUT1 expression and promotes trophoblast cell migration and invasion at the fetal-maternal interface.
Adenocarcinoma
POFUT1 as a Promising Novel Biomarker of Colorectal Cancer.
Adenoma
Molecular characterization of colorectal adenomas reveals POFUT1 as a candidate driver of tumor progression.
Breast Neoplasms
Overexpression of Pofut1 and activated Notch1 may be associated with poor prognosis in breast cancer.
Carcinogenesis
PLAGL2 and POFUT1 are regulated by an evolutionarily conserved bidirectional promoter and are collaboratively involved in colorectal cancer by maintaining stemness.
Carcinoma
Bioinformatics insight into glycosyltransferase gene expression in gastric cancer: POFUT1 is a potential biomarker.
Carcinoma
Protein O-fucosyltransferase 1: A potential diagnostic marker and therapeutic target for human oral cancer.
Carcinoma, Ductal
Overexpression of Pofut1 and activated Notch1 may be associated with poor prognosis in breast cancer.
Carcinoma, Hepatocellular
Author Correction: Caveolin-1 promotes invasion and metastasis by upregulating Pofut1 expression in mouse hepatocellular carcinoma.
Carcinoma, Hepatocellular
Caveolin-1 promotes invasion and metastasis by upregulating Pofut1 expression in mouse hepatocellular carcinoma.
Carcinoma, Hepatocellular
Overexpression of protein O-fucosyltransferase 1 accelerates hepatocellular carcinoma progression via the Notch signaling pathway.
Colorectal Neoplasms
Functional Characterization of POFUT1 Variants Associated with Colorectal Cancer.
Colorectal Neoplasms
PLAGL2 and POFUT1 are regulated by an evolutionarily conserved bidirectional promoter and are collaboratively involved in colorectal cancer by maintaining stemness.
Colorectal Neoplasms
POFUT1 as a Promising Novel Biomarker of Colorectal Cancer.
Colorectal Neoplasms
POFUT1 promotes colorectal cancer development through the activation of Notch1 signaling.
Colorectal Neoplasms
Weighted gene coexpression analysis indicates that PLAGL2 and POFUT1 are related to the differential features of proximal and distal colorectal cancer.
Congenital, Hereditary, and Neonatal Diseases and Abnormalities
Analyzing the Effects of O-Fucosylation on Secretion of ADAMTS Proteins Using Cell-Based Assays.
Dysostoses
Diseases related to Notch glycosylation.
Enterocolitis
Intestinal deletion of Pofut1 in the mouse inactivates notch signaling and causes enterocolitis.
Esophageal Neoplasms
Upregulation of Fucosyltransferase 3, 8 and protein O-Fucosyltransferase 1, 2 genes in esophageal cancer stem-like cells (CSLCs).
Glioblastoma
Histology-based expression profiling yields novel prognostic markers in human glioblastoma.
Glioblastoma
POFUT1 acts as a tumor promoter in glioblastoma by enhancing the activation of Notch signaling.
Glioma
Focused microarray analysis of glyco-gene expression in human glioblastomas.
Heart Failure
Uncontrolled angiogenic precursor expansion causes coronary artery anomalies in mice lacking Pofut1.
Hidradenitis
Novel POFUT1 mutation associated with hidradenitis suppurativa-Dowling-Degos disease firm up a role for Notch signalling in the pathogenesis of this disorder.
Hidradenitis
Novel POFUT1 mutation associated with hidradenitis suppurativa-Dowling-Degos disease firm up a role for Notch signalling in the pathogenesis of this disorder: reply from the authors.
Hidradenitis Suppurativa
A new nonsense mutation in the POGLUT1 gene in two sisters with Dowling-Degos disease.
Hidradenitis Suppurativa
A novel mutation in POFUT1 gene associated with Dowling-Degos disease and hidradenitis suppurativa.
Hyperpigmentation
Phenotypic expansion of POFUT1 loss of function mutations in a disorder featuring segmental dyspigmentation with eczematous and folliculo-centric lesions.
Hyperpigmentation
Variant in human POFUT1 reduces enzymatic activity and likely causes a recessive microcephaly, global developmental delay with cardiac and vascular features.
Hypopigmentation
Mutations in POFUT1, Encoding Protein O-fucosyltransferase 1, Cause Generalized Dowling-Degos Disease.
Infections
Protein O-fucosylation in Plasmodium falciparum ensures efficient infection of mosquito and vertebrate hosts.
Infections
Protein O-Fucosyltransferase 2 Is Not Essential for Plasmodium berghei Development.
Infections
Protein O-fucosyltransferase 2-mediated O-glycosylation of the adhesin MIC2 is dispensable for Toxoplasma gondii tachyzoite infection.
Keratosis, Seborrheic
Novel deletion of the POFUT1 gene associated with multiple seborrheic keratosis Dowling-Degos disease.
Liver Diseases
Variant in human POFUT1 reduces enzymatic activity and likely causes a recessive microcephaly, global developmental delay with cardiac and vascular features.
Lung Neoplasms
Fucosylation genes as circulating biomarkers for lung cancer.
Lymphatic Metastasis
Overexpression of Pofut1 and activated Notch1 may be associated with poor prognosis in breast cancer.
Lymphatic Metastasis
POFUT1 mRNA expression as an independent prognostic parameter in muscle-invasive bladder cancer.
Malaria
Protein O-fucosylation in Plasmodium falciparum ensures efficient infection of mosquito and vertebrate hosts.
Malaria
Protein O-Fucosyltransferase 2 Is Not Essential for Plasmodium berghei Development.
Malignant Atrophic Papulosis
Variant in human POFUT1 reduces enzymatic activity and likely causes a recessive microcephaly, global developmental delay with cardiac and vascular features.
Microcephaly
Variant in human POFUT1 reduces enzymatic activity and likely causes a recessive microcephaly, global developmental delay with cardiac and vascular features.
Mouth Neoplasms
Protein O-fucosyltransferase 1: A potential diagnostic marker and therapeutic target for human oral cancer.
Muscular Dystrophies, Limb-Girdle
Diseases related to Notch glycosylation.
Myocardial Infarction
Uncontrolled angiogenic precursor expansion causes coronary artery anomalies in mice lacking Pofut1.
Neoplasm Metastasis
Author Correction: Caveolin-1 promotes invasion and metastasis by upregulating Pofut1 expression in mouse hepatocellular carcinoma.
Neoplasm Metastasis
Caveolin-1 promotes invasion and metastasis by upregulating Pofut1 expression in mouse hepatocellular carcinoma.
Neoplasm Metastasis
Overexpression of Pofut1 and activated Notch1 may be associated with poor prognosis in breast cancer.
Neoplasm Metastasis
POFUT1 mRNA expression as an independent prognostic parameter in muscle-invasive bladder cancer.
Neoplasms
Bioinformatics insight into glycosyltransferase gene expression in gastric cancer: POFUT1 is a potential biomarker.
Neoplasms
Caveolin-1 promotes invasion and metastasis by upregulating Pofut1 expression in mouse hepatocellular carcinoma.
Neoplasms
Diseases related to Notch glycosylation.
Neoplasms
Downregulated protein O-fucosyl transferase 1 (Pofut1) expression exerts antiproliferative and antiadhesive effects on hepatocytes by inhibiting Notch signalling.
Neoplasms
Fucosylation genes as circulating biomarkers for lung cancer.
Neoplasms
Functional Characterization of POFUT1 Variants Associated with Colorectal Cancer.
Neoplasms
Integrated analysis of genome-wide copy number alterations and gene expression in microsatellite stable, CpG island methylator phenotype-negative colon cancer.
Neoplasms
Molecular characterization of colorectal adenomas reveals POFUT1 as a candidate driver of tumor progression.
Neoplasms
Overexpression of Pofut1 and activated Notch1 may be associated with poor prognosis in breast cancer.
Neoplasms
PLAGL2 and POFUT1 are regulated by an evolutionarily conserved bidirectional promoter and are collaboratively involved in colorectal cancer by maintaining stemness.
Neoplasms
POFUT1 acts as a tumor promoter in glioblastoma by enhancing the activation of Notch signaling.
Neoplasms
POFUT1 and PLAGL2 gene pair linked by a bidirectional promoter: the two in one of tumour progression in colorectal cancer?
Neoplasms
POFUT1 as a Promising Novel Biomarker of Colorectal Cancer.
Neoplasms
POFUT1 mRNA expression as an independent prognostic parameter in muscle-invasive bladder cancer.
Neoplasms
POFUT1 promotes colorectal cancer development through the activation of Notch1 signaling.
Neoplasms
Protein O-fucosyltransferase 1: A potential diagnostic marker and therapeutic target for human oral cancer.
Neoplasms
Structure of human POFUT1, its requirement in ligand-independent oncogenic Notch signaling, and functional effects of Dowling-Degos mutations.
Neoplasms
Upregulation of Fucosyltransferase 3, 8 and protein O-Fucosyltransferase 1, 2 genes in esophageal cancer stem-like cells (CSLCs).
Neoplasms
Weighted gene coexpression analysis indicates that PLAGL2 and POFUT1 are related to the differential features of proximal and distal colorectal cancer.
peptide-o-fucosyltransferase deficiency
POFUT1 is dispensable for structure, function and survival of mouse podocytes.
peptide-o-fucosyltransferase deficiency
Protein O-fucosyltransferase 1 (Pofut1) regulates lymphoid and myeloid homeostasis through modulation of notch receptor ligand interactions.
peptide-o-fucosyltransferase deficiency
Recognition of EGF-like domains by the Notch-modifying O-fucosyltransferase POFUT1.
Psoriasis
Genetic diagnosis history and osteoarticular phenotype of a non-transfusion secondary hemochromatosis.
Skin Diseases
Phenotypic expansion of POFUT1 loss of function mutations in a disorder featuring segmental dyspigmentation with eczematous and folliculo-centric lesions.
Squamous Cell Carcinoma of Head and Neck
Protein O-fucosyltransferase 1: A potential diagnostic marker and therapeutic target for human oral cancer.
Stomach Neoplasms
Bioinformatics insight into glycosyltransferase gene expression in gastric cancer: POFUT1 is a potential biomarker.
Teratoma
O-fucosylation of thrombospondin type 1 repeats restricts epithelial to mesenchymal transition (EMT) and maintains epiblast pluripotency during mouse gastrulation.
Urinary Bladder Neoplasms
POFUT1 mRNA expression as an independent prognostic parameter in muscle-invasive bladder cancer.
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evolution
CePOFUT1 is a member of the GT65 family and contains four conserved disulfide bridges through the GT65 family
evolution
POFUT2 belongs to the classical GT-B fold family of glycosyltransferases with two closely interacting Rossmann-like domains. POFUT2 shows a variation of the classical GT-B fold
evolution
the highly correlated presence of POFUT1 and fucosylatable hEGFs has accompanied animal evolution
malfunction
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CHO cells lacking Pofut1 express Notch receptors on the cell surface at similar levels to wild-type cells
malfunction
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deletion of Pofut1 leads to global defects in Notch signaling and death of mice at E9.5, with a phenotype consistent with inactivation of signaling by the four Notch receptors. Embryonic stem cells lacking Pofut1 express Notch receptors on the cell surface at similar levels to wild-type cells. In mouse somites, there is evidence of altered Notch trafficking in the absence of Pofut1, consistent with reduced cell surface expression
malfunction
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embryonic stem cells lacking Pofut1 are deficient in Notch ligand binding, have wild-type levels of cell surface Notch receptors. Pofut1-/- embryonic stem cells do not bind Notch ligands or exhibit Notch signaling. Overexpression of fucosyltransferase-defective Pofut1 R245A in Pofut1-/- cells partially rescues ligand binding and Notch signaling, but this effect is not specific. Under certain conditions, mammalian Notch receptors can bind Notch ligands and transduce a Notch signal in the absence of Pofut1 and O-fucose
malfunction
Drosophila sp. (in: flies)
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in ofut1 mutant cells, Notch goes to the membrane, is internalized and accumulates in an uncharacterized endocytic compartment. Knockdown of Ofut1 using doublestranded RNA in cultured cells inhibits the secretion of a soluble version of the Notch extracellular domain. In ofut1 mutant cells, Notch does not accumulate at adherens junctions but instead accumulates into intracellular dots. A low level of Notch is also present at the surface of ofut1 mutant cells
malfunction
Drosophila sp. (in: flies)
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loss of OFUT1 results in the phenotype that is characteristic of Notch loss of function. Loss of OFUT1 leads to the loss of cell surface expression and the intracellular accumulation of Notch receptors. Secretion of Notch is impaired in OFUT1-depleted S2 cells and the abnormal endoplasmic reticulum accumulation of Notch receptors is observed in Ofut1 mutant clones in Drosophila wing imaginal discs
malfunction
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loss of Pofut1 results in the phenotype that is characteristic of Notch loss of function
malfunction
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neural crest cell-specific Pofut1-knockout mice die within 1 day of birth, accompanied by a defect of enteric nervous system development. Sox10 expression is decreased in Pofut1-null enteric neural crest cells, whereas the number of enteric neural crest cells that express Mash1, a potent repressor of Sox10, is increased in the Pofut1-null mouse. Enteric neural crest cells lacking Pofut1 show premature neurogenesis and a decrease in the number of glial progenitors
malfunction
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Pofut1 deletion inactivates Notch signaling, giving rise to smaller but viable mice. Dysplastic foci in Pofut1-deficient small intestine with occasional progression to tumor formation. Inactivation of Pofut1 leads to intestinal inflammation. Mucus hypersecretion upon Pofut1 inactivation is accompanied by alteration of the mucus-associated flora, which likely contributes to the development of enterocolitis
malfunction
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Pofut1-null mouse shows a similar phenotype to the RBP-Jk null mouse. Cardiac development in the Pofut1-/- mice is severely affected in valve formation, which is characterized in the lack of mesenchymal cells as seen in RBP-Jk null embryos and embryonic development is arrested at E9.0. Pofut1-null cells do not possess normally localized Notch1 receptors. Abnormal accumulation of the Notch1 receptor in the endoplasmic reticulum and cytoplasm in Pofut1-null mouse embryos
malfunction
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siRNAs eliminating Pofut1 transcripts in CHO cells. CHO cells deficient in Pofut1 have reduced Notch signaling and ligand binding. Under certain conditions, mammalian Notch receptors can bind Notch ligands and transduce a Notch signal in the absence of Pofut1 and O-fucose
malfunction
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elimination of Pofut1 in mice causes embryonic lethality with Notch-like phenotypes, elimination of Pofut2 results in an early embryonic lethal phenotype in mice
malfunction
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elimination of Pofut1 in mice has a profound effect on ligand binding in both embryonic stem cells and lymphoid cells. A small decrease in cell surface expression of Notch proteins is seen in embryonic stem cells lacking Pofut1 and in somites from mice with a hypomorphic allele of Pofut1, cax
malfunction
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mice lacking Pofut1 show myeloid hyperplasia and impaired lymphopoiesis. Mx-Cre/Pofut1F/F mice splenomegaly show in the bone marrow a decrease in T and B lymphocytes and an expansion of mature granulocytes and myeloid progenitors, mutant mice phenotypes, detailed overview. Mx-Cre/Pofut1F/F marrow progenitors have defective T lymphopoiesis and enhanced myeloid development in vitro that is correlated with decreased Notch ligand binding.. Defective T-cell development and myeloid hyperplasia are rescued by reinstating Notch1 signaling. Heterozygosity of Pofut1 affects rescue of FX-/- mice myeloid hyperplasia by exogenous fucose
malfunction
cell proliferation of POFUT1 knockdown cells is significantly inhibited compared with that of control cells, phenotypes, overview
malfunction
knockdown and overexpression of Pofut1 inhibits and accelerates the growth, migration and invasion of hepatocellular carcinoma cells, respectively
malfunction
phenotype of Pofut1-/- mouse embryos resembles embryos lacking downstream components of Notch signaling, like CBF1/RBP-Jkappa. Mutation on the O-fucosylation site in mouse Notch1 EGF12 results in a hypomorphic allele affecting the Notch-ligand interaction. Pofut1 knockdown decreases Pax7 and disrupts the expression of myogenic markers. Downregulation of gene Pofut1 significantly lowers the quantity of cleaved Notch intracellular domain and the expression levels of genes Rbpj and Hes1 but without modification of the cell surface expression pattern of Notch1, phenotype, overview
malfunction
CRISPR-mediated knockout of POFUT1 in U2OS cells suppresses both normal Notch1 signaling, and the ligand-independent signaling associated with leukemogenic mutations of Notch1. Normal and oncogenic signaling are rescued by wild-type POFUT1 but rescue is impaired by an active-site R240A mutation
malfunction
genetic disruption of POFUT2 in Plasmodium falciparum results in ookinetes that are attenuated for colonizing the mosquito midgut, an essential step in malaria transmission. Some POFUT2-deficient parasites mature into salivary gland sporozoites although they are impaired for gliding motility, cell traversal, hepatocyte invasion, and production of exoerythrocytic forms in humanized chimeric liver mice
malfunction
heterozygous mutations in POFUT1 are linked to a rare skin condition, Dowling-Degos Disease. Amplification of POFUT1 is associated with several types of cancer
malfunction
loss-of-function mutants display impaired sexual reproduction that is linked to a defective male gamete. oft1 Mutant pollen tubes are ineffective at penetrating the stigma-style interface leading to a drastic reduction in seed set and a nearly 2000-fold reduction in pollen transmission
physiological function
-
is essential for Notch signalling
physiological function
Drosophila sp. (in: flies)
-
is essential for Notch signalling. Ability of OFUT1 to promote Notch secretion does not depend on its enzyme activity, suggesting the chaperon-like role of OFUT1
physiological function
-
Notch receptors require Pofut1 for the generation of optimally functional Notch receptors, but Pofut1 is not required for stable cell surface expression of Notch
physiological function
-
Notch receptors require Pofut1 for the generation of optimally functional Notch receptors, but Pofut1 is not required for stable cell surface expression of Notch
physiological function
-
Pofut1 is required for Notch signaling upstream of NICD1
physiological function
Drosophila sp. (in: flies)
-
roles in the folding of Notch in the endoplasmic reticulum, in Notch-ligand binding and in endocytic trafficking of Notch. The carboxy-terminal extremity of Ofut1 contains a Lys-Asp-Glu-Leu (KDEL)-like motif that is dispensable for its catalytic activity but is required for both endoplasmic reticulum retention and function. Ofut1 is required only for Fringe-dependent signaling events
physiological function
-
Notch is a transmembrane receptor that shares homology with proteins containing epidermal growth factor-like repeats and mediates the cell-cell interactions necessary for many cell fate decisions. O-fucosyltransferase 1 catalyzes the O-fucosylation of these epidermal growth factor-like repeats. This O-fucose elongates, resulting in an O-linked tetrasaccharide that regulates the signaling activities of Notch. Fucosylation occurs in the lumen of the endoplasmicreticulum and Golgi. GDP-fucose uptake into the ER and Golgi is essential for fucosylation, Efr, a multifunctional nucleotide sugar transporter, and Golgi GDP-fucose transporter Gfr are involved in the biosynthesis of heparan sulfate-glycosaminoglycan chains and the O-fucosylation of Notch. Gfr but not Efr is crucial for the fucosylation of N-glycans, overview
physiological function
-
O-fucosylation is universally required for all Notch signaling. O-Fucose and O-glucose glycans on Notch occur at specific consensus sequences within the context of EGF repeats, which make up the majority of the Notch extracellular domain. Molecular mechanisms by which O-fucose and O-glucose glycans affect Notch function
physiological function
-
O-fucosylation is universally required for all Notch signaling. O-Fucose and O-glucose glycans on Notch occur at specific consensus sequences within the context of EGF repeats, which make up the majority of the Notch extracellular domain. Ofut1 might have a chaperone-like activity in Drosophila that is required for cell-surface expression of Notch in flies. Molecular mechanisms by which O-fucose and O-glucose glycans affect Notch function, overview
physiological function
-
O-fucosylation of Notch is essential for its function
physiological function
protein O-fucosyltransferase 2 catalyzes the protein O-fucosylation, a post-translational modification found on serine/threonine residues of thrombospondin type 1 repeats
physiological function
critical role of Pofut1 on Notch pathway activation during myogenic differentiation, overview. Both active Pofut1 and O-fucosylation of Notch are required for the canonical Notch signaling by Delta1 or Jagged1
physiological function
protein O-fucosyltransferase 2 is an essential enzyme that fucosylates serine and threonine residues of folded thrombospondin type 1 repeats
physiological function
the enzyme adds O-fucose through O-glycosidic linkage to conserved serine or threonine residues in the epidermal growth factor-like repeats of a number of cellular surface and secreted proteins. ENzyme POFUT1 expression can contribute to cancer progression
physiological function
the enzyme catalyzes the addition of O-linked fucose to the epidermal growth factor-like repeats of Notch. Pofut1 overexpression accelerates cell proliferation and migration in hepatocellular carcinoma cells and it promotes the binding of Notch ligand Dll1 to Notch receptor, and hence activates Notch signaling pathway in hepatocellular carcinoma cells
physiological function
AtOFT1 plays a critical role in pollen tube penetration through the stigma/style in Arabidopsis
physiological function
both POFUT1 and POFUT2 are proposed to participate in non-canonical endoplasmic reticulum quality control pathways for the folding of Epidermal Growth Factor-like (EGF) repeats and Thrombospondin Type 1 Repeats (TSRs), respectively
physiological function
both POFUT1 and POFUT2 participate in non-canonical endoplasmic reticulum quality control pathways for the folding of Epidermal Growth Factor-like (EGF) repeats and Thrombospondin Type 1 Repeats (TSRs), respectively
physiological function
protein O-fucosylation is an important glycosylation modification and plays an important role in embryonic development. Protein O-fucosyltransferase 1 promotes trophoblast cell proliferation through activation of MAPK and PI3K/Akt signaling pathways
physiological function
protein O-fucosyltransferases 1 and 2 (PoFUT1 and PoFUT2) are the enzymes responsible for this protein O-fucosylation and selectively glycosylate specific residues in epidermal growth factor-like (EGF) repeats and thrombospondin type I repeats (TSRs). PoFUT1 glycosylates epidermal growth factor-like (EGF) repeats within the consensus sequence C2-X-X-X-X-S/T-C3
physiological function
protein O-fucosyltransferases 1 and 2 (PoFUT1 and PoFUT2) are the enzymes responsible for this protein O-fucosylation and selectively glycosylate specific residues in epidermal growth factor-like (EGF) repeats and thrombospondin type I repeats (TSRs). PoFUT1 glycosylates epidermal growth factor-like (EGF) repeats within the consensus sequence C2-X-X-X-X-S/T-C3
physiological function
protein O-fucosyltransferases 1 and 2 (PoFUT1 and PoFUT2) are the enzymes responsible for this protein O-fucosylation and selectively glycosylate specific residues in epidermal growth factor-like (EGF) repeats and thrombospondin type I repeats (TSRs). PoFUT1 glycosylates epidermal growth factor-like (EGF) repeats within the consensus sequence C2-X-X-X-X-S/T-C3
physiological function
protein O-fucosyltransferases 1 and 2 (PoFUT1 and PoFUT2) are the enzymes responsible for this protein O-fucosylation and selectively glycosylate specific residues in epidermal growth factor-like (EGF) repeats and thrombospondin type I repeats (TSRs). PoFUT2 glycosylates thrombospondin type I repeats (TSRs) containing Ser/Thr residues located in the consensus sequences C1-X-X-S/T-C2 or C2-X-X-S/T-C3 of TSRs of groups 1 and 2
physiological function
protein O-fucosyltransferases 1 and 2 (PoFUT1 and PoFUT2) are the enzymes responsible for this protein O-fucosylation and selectively glycosylate specific residues in epidermal growth factor-like (EGF) repeats and thrombospondin type I repeats (TSRs). PoFUT2 glycosylates thrombospondin type I repeats (TSRs) containing Ser/Thr residues located in the consensus sequences C1-X-X-S/T-C2 or C2-X-X-S/T-C3 of TSRs of groups 1 and 2
physiological function
the enzyme (Pofut1), which transfers O-fucose to the EGF domains of the Notch1 receptor, is indispensable for Notch signaling activation
physiological function
the enzyme activates nuclear growth repressor DELLA. SPY-dependent protein O-fucosylation plays a key role in regulating plant development
physiological function
the enzyme is responsible for O-glycosylating of the sporozoite surface proteins CSP and TRAP. The enzyme (POFUT2) ensures the trafficking of Plasmodium thrombospondin repeat proteins as part of a non-canonical glycosylation-dependent endoplasmic reticulum protein quality control mechanism
physiological function
the enzyme O-glycosylates micronemal protein 2 (MIC2). This glycan is dispensable in Toxoplasma gondii tachyzoites and for Toxoplasma gondii infectivity
physiological function
-
the enzyme O-glycosylates micronemal protein 2 (MIC2). This glycan is dispensable in Toxoplasma gondii tachyzoites and for Toxoplasma gondii infectivity
-
additional information
GDP-fucose is bound in a conserved cavity formed mainly by amino acids from the C-terminal domain, it is localised in the interface where the two domains face each other, localisation of EGF repeat binding site in CePOFUT1, active site and ligand binding structure analysis, detailed overview
additional information
-
O-glycome of Drosophila melanogaster by mass spectrometry, using beta-elimination to release the O-linked sugar modifications from total protein extracts of fly embryos, overview
additional information
recognition of a small conserved 3D structural motif and mechanism of enzyme-protein substrate specificity. POFUT2 features a unique loop, residues 265-285, located on the opposite side of the large cleft, which protrudes from the C-terminal domain and which is attached to the N-terminal domain via a completely conserved tryptophan residue, W273 is involved in controlling movements of the N- and C-terminal domain relative to each other during the catalytic cycle, and 90% activity is lost in mutant W273A. Structure-function analysis of POFUT2 and comparison to POFUT1
additional information
-
recognition of a small conserved 3D structural motif and mechanism of enzyme-protein substrate specificity. POFUT2 features a unique loop, residues 265-285, located on the opposite side of the large cleft, which protrudes from the C-terminal domain and which is attached to the N-terminal domain via a completely conserved tryptophan residue, W273 is involved in controlling movements of the N- and C-terminal domain relative to each other during the catalytic cycle, and 90% activity is lost in mutant W273A. Structure-function analysis of POFUT2 and comparison to POFUT1
additional information
enzyme in complex with GDP and human thrombospondin type 1 repeat shows an inverting mechanism for fucose transfer assisted by a catalytic base and shows that nearly half of the thrombospondin type 1 repeat is embraced by CePOFUT2. A small number of direct interactions and a large network of water molecules maintain the complex, role of interstitial water in the complex interface, water-mediated interactions, overview
additional information
-
enzyme in complex with GDP and human thrombospondin type 1 repeat shows an inverting mechanism for fucose transfer assisted by a catalytic base and shows that nearly half of the thrombospondin type 1 repeat is embraced by CePOFUT2. A small number of direct interactions and a large network of water molecules maintain the complex, role of interstitial water in the complex interface, water-mediated interactions, overview
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D242A
site-directed mutagenessis, altered mutant temperature dependence and GDP-fucose/GDP dissociation constants compared to the wild-type, the mutant shows about 10% increased activity compared to the wild-type enzyme
D244A
site-directed mutagenessis, altered mutant temperature dependence and GDP-fucose/GDP dissociation constants compared to the wild-type, the mutant shows reduced activity compared to the wild-type enzyme
D309N
site-directed mutagenessis, altered mutant temperature dependence and GDP-fucose/GDP dissociation constants compared to the wild-type, the mutant shows reduced activity compared to the wild-type enzyme
F199A
site-directed mutagenessis, altered mutant temperature dependence and GDP-fucose/GDP dissociation constants compared to the wild-type, the mutant shows reduced activity compared to the wild-type enzyme
F261A
site-directed mutagenessis, altered mutant temperature dependence and GDP-fucose/GDP dissociation constants compared to the wild-type, the mutant shows reduced activity compared to the wild-type enzyme
F357A
site-directed mutagenessis, altered mutant temperature dependence and GDP-fucose/GDP dissociation constants compared to the wild-type, the mutant shows reduced activity compared to the wild-type enzyme
G19Q
site-directed mutagenesis, the mutation affects both secretion and fucosylation
G19R
site-directed mutagenesis, the mutation affects both secretion and fucosylation
G20H
site-directed mutagenesis, the mutation affects both secretion and fucosylation
N43A
site-directed mutagenessis, altered mutant temperature dependence and GDP-fucose/GDP dissociation constants compared to the wild-type, the mutant shows highly reduced activity compared to the wild-type enzyme
R240A
site-directed mutagenessis, altered mutant temperature dependence and GDP-fucose/GDP dissociation constants compared to the wild-type, inactive mutant
R240K
site-directed mutagenessis, altered mutant temperature dependence and GDP-fucose/GDP dissociation constants compared to the wild-type, inactive mutant
R298K/R299K
site-directed mutagenesis, the mutant enzyme is stable against proteolysis and similarly active as the wild-type. The mutant enzymes is capable of fucosylating TSRs not only of group 1 but also of group 2, it not only recognizes and reacts with TSRs showing slightly different structures but also accepts TSRs with very low sequence identity. Residue Glu52 of mutant CePOFUT is the catalytic base
R40A
site-directed mutagenessis, altered mutant temperature dependence and GDP-fucose/GDP dissociation constants compared to the wild-type, the mutant shows reduced activity compared to the wild-type enzyme
S15D
site-directed mutagenesis, the mutant shows increased secretion, but a significant reduction in fucosylation, suggesting that HsPOFUT2 is highly selective for amino acids in the Xa position
S15Q
site-directed mutagenesis, the mutant shows increased secretion, but a significant reduction in fucosylation, suggesting that HsPOFUT2 is highly selective for amino acids in the Xa position
V16H
site-directed mutagenesis, the mutation affects both secretion and fucosylation
W245A
site-directed mutagenessis, altered mutant temperature dependence and GDP-fucose/GDP dissociation constants compared to the wild-type, the mutant shows reduced activity compared to the wild-type enzyme
R254A
-
expression of a mutant, Ofut1R245A, lacking fucosyltransferase activity, rescues the requirement for Ofut1 in embryonic neurogenesis. Lack of requirement for O-fucosylation is further supported by the absence of embryonic phenotypes in Gmd mutants, which lack all forms of fucosylation. Requirements for O-fucose during imaginal development are evaluated by characterizing clones of cells expressing only Ofut1R245A. These clones phenocopy fringe mutant clones, indicating that the absence of O-fucose is functionally equivalent to the absence of elongated O-fucose
R275A
Drosophila sp. (in: flies)
-
is catalytically dead. Ofut1 and mutant both bind the Notch extracellular domain, and expression of the mutant in cultured cells can increase both the amount and the ligand-binding activity of secreted Notch extracellular domain. Complete loss of ofut1 activity results in a strong phenotype mimicking a loss of Notch activity that is rescued to larval viability by the expression of mutant R275A, it rescues Notch receptor activity in these ofut1 mutant cells and leads to phenotypes mimicking a loss of fringe activity
D297A
site-directed mutagenesis, the mutant shows 15% activity compared to the wild-type enzyme
E396A
site-directed mutagenesis, the mutant shows 8% activity compared to the wild-type enzyme
E54A
site-directed mutagenesis, inactive mutant
R294A
site-directed mutagenesis, inactive mutant
W273a
site-directed mutagenesis, W273 is involved in controlling movements of the N- and C-terminal domain relative to each other during the catalytic cycle, and 90% activity is lost in mutant W273A
S1726A
-
mutant protein shows no activity, loss of O-fucosylation causes a gain of function for muscle agrin such that it stimulates acetylcholine receptors, clustering and MuSK phosphorylation in cultured myotubes at levels normally only found with the neural splice form
R245A
-
is fucosylation-defective, has a dominant negative effect on wild-type Pofut1, since Pofut1 activity in Pofut1-/- cells expressing Pofut1 R245A is markedly reduced in the in vitro assay
R245A
mutation disrupts O-fucosyltransferase activity destabilizes the protein and abolishes Notch1 signaling during mouse somitogenesis
additional information
mutants R40A, N43A and R240A/K are more stable while F199A, D309N, D242A, D244A, W245A, F261A and F357A are less stable than the wild-type. Mutants R40A, R240A/K, W245A and F357A show a decrease in binding to GDP, from this group, R40A and W245A bind better to GDP than F357A, R240K and R240A, with the latter being impaired in binding
additional information
-
down-regulation of enzyme by RNA interference in Notch-secreting cells inhibits both Delta-Notch and Serrate-Notch binding. Overexpression of enzyme in cultured cells increases Serrate-Notch binding but inhibits Delta-Notch binding
additional information
enzyme disruption mutant, enzyme is essential for Notch signaling, Fringe function, for physical interaction of Notch with its ligand Delta, and lateral inhibition during neuroblast segregation
additional information
-
analysis of O-fut 1 homozygous mutant cells shows that O-fut1 is required for the endocytic transportation of Notch to the early endosome which is shown to be independent of the O-fucosyltransferase activity of O-fut1
additional information
-
O-fut 1 overexpression and analysis of O-fut 1 homozygous mutant cells indicates that O-fut 1 promotes the turnover of Notch, which consequently downregulates Notch signaling
additional information
-
O-fut1 protein added to conditioned medium and endocytosed is sufficient to rescue normal Notch transportation to the early endosome in O-fut1 knockdown cells
additional information
-
using O-fut I knock out mutants it is shown that the localization of Notch in the region from the subapical complex (SAC) to the apical portion of the adherens junctions (AJs) depends on its O-fucosylation
additional information
-
an artificial O-glycosylation pathway to produce an O-fucosylated epidermal growth factor (EGF) domain in Saccharomyces cerevisiae is generated. The in vivo O-fucosylation system is constructed via expression of genes that encode protein O-fut1 and the EGF domain, along with genes whose protein products convert cytoplasmic GDP-mannose to GDP-fucose
additional information
-
enzyme deletion mutant, mouse embryose lacking enzyme die at midgestation with severe defects in somitogenesis, vasculinogenesis, cardiogenesis, and neurogenesis
additional information
-
deletion of Pofut1 in cultured primary myotubes and in adult skeletal muscle increases acetylcholine receptor aggregation
additional information
-
generation of Pofut1+/-/FX-/- mutant mice
additional information
generation of murine myoblastic Pofut1 knockdown C2C12 cell line, and analysis of the C2C12 cell line downregulated for Pofut1 expression by short hairpin RNA (shRNA) inhibition during the time course of differentiation. Knockdown of Pofut1 affects the signaling pathway activation by a reduction of the amount of cleaved Notch intracellular domain and a decrease in downstream Notch target gene expression. Depletion in Pax7/MyoD- cells and earlier myogenic program entrance are observed, leading to an increase in myotube quantity with a small number of nuclei, reflecting fusion defects. The rescue of Pofut1 expression in knockdown cells, by generation of Pofut1 knockdown C2C12 cell lines reexpressing shRNA-resistant Pofut1, restores Notch signaling activation and a normal course in C2C12 differentiation. Downregulation of gene Pofut1 significantly lowers the quantity of cleaved Notch intracellular domain and the expression levels of genes Rbpj and Hes1 but without modification of the cell surface expression pattern of Notch1, phenotype, overview
additional information
-
generation of murine myoblastic Pofut1 knockdown C2C12 cell line, and analysis of the C2C12 cell line downregulated for Pofut1 expression by short hairpin RNA (shRNA) inhibition during the time course of differentiation. Knockdown of Pofut1 affects the signaling pathway activation by a reduction of the amount of cleaved Notch intracellular domain and a decrease in downstream Notch target gene expression. Depletion in Pax7/MyoD- cells and earlier myogenic program entrance are observed, leading to an increase in myotube quantity with a small number of nuclei, reflecting fusion defects. The rescue of Pofut1 expression in knockdown cells, by generation of Pofut1 knockdown C2C12 cell lines reexpressing shRNA-resistant Pofut1, restores Notch signaling activation and a normal course in C2C12 differentiation. Downregulation of gene Pofut1 significantly lowers the quantity of cleaved Notch intracellular domain and the expression levels of genes Rbpj and Hes1 but without modification of the cell surface expression pattern of Notch1, phenotype, overview
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Cricetulus griseus, Rattus norvegicus
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Modification of epidermal growth factor-like repeats with O-fucose. Molecular cloning and expression of a novel GDP-fucose protein O-fucosyltransferase
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Candida elegans, Drosophila melanogaster, Mus musculus (Q91ZW2), Mus musculus, Homo sapiens (Q9H488), Homo sapiens
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Modulation of notch-ligand binding by protein O-fucosyltransferase 1 and fringe
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Drosophila melanogaster
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O-fucosylation of notch occurs in the endoplasmic reticulum
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2005
Homo sapiens
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Protein O-fucosyltransferase 1 is an essential component of Notch signaling pathways
Proc. Natl. Acad. Sci. USA
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2003
Mus musculus
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Chaperone activity of protein O-fucosyltransferase 1 promotes notch receptor folding
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Drosophila melanogaster
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neurotic, a novel maternal neurogenic gene, encodes an O-fucosyltransferase that is essential for Notch-Delta interactions
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2003
Drosophila melanogaster (Q9V6X7)
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Coherent electronic fringe structure in incommensurate silver-silicon quantum wells
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Drosophila sp. (in: flies)
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The O-fucosyltransferase O-fut1 is an extracellular component that is essential for the constitutive endocytic trafficking of Notch in Drosophila
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Drosophila melanogaster
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Polarized exocytosis and transcytosis of Notch during its apical localization in Drosophila epithelial cells
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Drosophila melanogaster
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Engineering of a mammalian O-glycosylation pathway in the yeast Saccharomyces cerevisiae: production of O-fucosylated epidermal growth factor domains
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O-fucosylation of muscle agrin determines its ability to cluster acetylcholine receptors
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Notch signaling is required for the maintenance of enteric neural crest progenitors
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Intestinal deletion of Pofut1 in the mouse inactivates notch signaling and causes enterocolitis
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Caenorhabditis elegans (Q18014)
brenda
Ma, L.; Dong, P.; Liu, L.; Gao, Q.; Duan, M.; Zhang, S.; Chen, S.; Xue, R.; Wang, X.
Overexpression of protein O-fucosyltransferase 1 accelerates hepatocellular carcinoma progression via the Notch signaling pathway
Biochem. Biophys. Res. Commun.
473
503-510
2016
Homo sapiens (Q9H488), Homo sapiens
brenda
Yokota, S.; Ogawara, K.; Kimura, R.; Shimizu, F.; Baba, T.; Minakawa, Y.; Higo, M.; Kasamatsu, A.; Endo-Sakamoto, Y.; Shiiba, M.; Tanzawa, H.; Uzawa, K.
Protein O-fucosyltransferase 1: a potential diagnostic marker and therapeutic target for human oral cancer
Int. J. Oncol.
43
1864-1870
2013
Homo sapiens (Q9H488), Homo sapiens
brenda
Der Vartanian, A.; Audfray, A.; Al Jaam, B.; Janot, M.; Legardinier, S.; Maftah, A.; Germot, A.
Protein O-fucosyltransferase 1 expression impacts myogenic C2C12 cell commitment via the Notch signaling pathway
Mol. Cell. Biol.
35
391-405
2015
Mus musculus (Q91ZW2), Mus musculus
brenda
Valero-Gonzalez, J.; Leonhard-Melief, C.; Lira-Navarrete, E.; Jimenez-Oses, G.; Hernandez-Ruiz, C.; Pallares, M.C.; Yruela, I.; Vasudevan, D.; Lostao, A.; Corzana, F.; Takeuchi, H.; Haltiwanger, R.S.; Hurtado-Guerrero, R.
A proactive role of water molecules in acceptor recognition by protein O-fucosyltransferase 2
Nat. Chem. Biol.
12
240-246
2016
Caenorhabditis elegans (Q8WR51), Caenorhabditis elegans
brenda
Lira-Navarrete, E.; Hurtado-Guerrero, R.
A perspective on structural and mechanistic aspects of protein O-fucosylation
Acta Crystallogr. Sect. F
74
443-450
2018
Caenorhabditis elegans (Q18014), Caenorhabditis elegans (Q8WR51), Mus musculus (Q91ZW2), Homo sapiens (Q9H488), Homo sapiens (Q9Y2G5)
brenda
Liu, C.; Liang, X.; Wang, J.; Zheng, Q.; Zhao, Y.; Khan, M.N.; Liu, S.; Yan, Q.
Protein O-fucosyltransferase 1 promotes trophoblast cell proliferation through activation of MAPK and PI3K/Akt signaling athways
Biomed. Pharmacother.
88
95-101
2017
Homo sapiens (Q9H488), Homo sapiens
brenda
Holdener, B.C.; Haltiwanger, R.S.
Protein O-fucosylation structure and function
Curr. Opin. Struct. Biol.
56
78-86
2019
Homo sapiens (Q9H488), Homo sapiens (Q9Y2G5)
brenda
Sanz, S.; Aquilini, E.; Tweedell, R.E.; Verma, G.; Hamerly, T.; Hritzo, B.; Tripathi, A.; Machado, M.; Churcher, T.S.; Rodrigues, J.A.; Izquierdo, L.; Dinglasan, R.R.
Protein O-fucosyltransferase 2 is not essential for Plasmodium berghei development
Front. Cell. Infect. Microbiol.
9
238
2019
Homo sapiens (Q9H488), Homo sapiens
brenda
McMillan, B.J.; Zimmerman, B.; Egan, E.D.; Lofgren, M.; Xu, X.; Hesser, A.; Blacklow, S.C.
Structure of human POFUT1, its requirement in ligand-independent oncogenic Notch signaling, and functional effects of Dowling-Degos mutations
Glycobiology
27
777-786
2017
Homo sapiens (Q9H488), Homo sapiens
brenda
Sadeghzadeh, Z.; Khosravi, A.; Jazi, M.S.; Asadi, J.
Upregulation of fucosyltransferase 3, 8 and protein O-fucosyltransferase 1, 2 genes in esophageal cancer stem-like cells (CSLCs)
Glycoconj. J.
37
319-327
2020
Homo sapiens (Q9H488), Homo sapiens (Q9Y2G5)
brenda
Khurana, S.; Coffey, M.J.; John, A.; Uboldi, A.D.; Huynh, M.H.; Stewart, R.J.; Carruthers, V.B.; Tonkin, C.J.; Goddard-Borger, E.D.; Scott, N.E.
Protein O-fucosyltransferase 2-mediated O-glycosylation of the adhesin MIC2 is dispensable for Toxoplasma gondii tachyzoite infection
J. Biol. Chem.
294
1541-1553
2019
Toxoplasma gondii (S7WCF5), Toxoplasma gondii, Toxoplasma gondii ATCC 50853 (S7WCF5)
brenda
Zentella, R.; Sui, N.; Barnhill, B.; Hsieh, W.; Hu, J.; Shabanowitz, J.; Boyce, M.; Olszewski, N.; Zhou, P.; Hunt, D.; Sun, T.
The Arabidopsis O-fucosyltransferase SPINDLY activates nuclear growth repressor della
Nat. Chem. Biol.
13
479-485
2017
Arabidopsis thaliana (Q96301), Arabidopsis thaliana
brenda
Li, Z.; Han, K.; Pak, J.E.; Satkunarajah, M.; Zhou, D.; Rini, J.M.
Recognition of EGF-like domains by the Notch-modifying O-fucosyltransferase POFUT1
Nat. Chem. Biol.
13
757-763
2017
Mus musculus (Q91ZW2), Mus musculus
brenda
Lopaticki, S.; Yang, A.S.P.; John, A.; Scott, N.E.; Lingford, J.P.; ONeill, M.T.; Erickson, S.M.; McKenzie, N.C.; Jennison, C.; Whitehead, L.W.; Douglas, D.N.; Kneteman, N.M.; Goddard-Borger, E.D.; Boddey, J.A.
Protein O-fucosylation in Plasmodium falciparum ensures efficient infection of mosquito and vertebrate hosts
Nat. Commun.
8
561
2017
Plasmodium falciparum (Q8I360), Plasmodium falciparum
brenda
Smith, D.; Harper, J.; Wallace, I.
A potential role for protein O-fucosylation during pollen-pistil interactions
Plant Signal. Behav.
13
e1467687
2018
Arabidopsis thaliana (Q9MA87), Arabidopsis thaliana
brenda
Ajima, R.; Suzuki, E.; Saga, Y.
Pofut1 point-mutations that disrupt O-fucosyltransferase activity destabilize the protein and abolish Notch1 signaling during mouse somitogenesis
PLoS ONE
12
e0187248
2017
Mus musculus (Q91ZW2), Mus musculus
brenda