Ask about this productRelated genes to: POFUT1 antibody
- Gene:
- POFUT1 NIH gene
- Name:
- protein O-fucosyltransferase 1
- Previous symbol:
- -
- Synonyms:
- O-FUT, O-Fuc-T, KIAA0180, FUT12
- Chromosome:
- 20q11.21
- Locus Type:
- gene with protein product
- Date approved:
- 2001-10-29
- Date modifiied:
- 2016-10-05
Related products to: POFUT1 antibody
Related articles to: POFUT1 antibody
- Protein -fucosyltransferase 1 (POFUT1) catalyzes the transfer of fucose to threonine or serine residues within epidermal growth factor-like domains (EGF-LDs) and is a therapeutic target for Notch-associated O-glycosylation disorders. Unlike classical inverting glycosyltransferases, POFUT1 employs a catalytic asparagine that tautomerizes to its imidic acid form during the reaction. How the enzyme subsequently restores the canonical amidic form of Asn51 has remained unclear. Here, quantum mechanics/molecular mechanics simulations reveal that active-site water molecules mediate Asn51 retautomerization through a Grotthuss-type proton relay involving a low free energy barrier (<6 kcal·mol). This process can occur regardless of the presence of product molecules in the active site, although it is most favorable after product release. These findings elucidate how POFUT1 resets its catalytic machinery after turnover, underscore the essential role of water molecules in enzyme catalysis, and suggest that similar water-mediated strategies may operate in other enzymes in which catalytic residues undergo protonation changes during turnover. - Source: PubMed
Publication date: 2026/04/10
Vidal-Gironès ÒscarTrizio EnricoKang PeilinParrinello MicheleRivas-Fernández José PabloRovira Carme - - Source: PubMed
Publication date: 2026/03/26
Solak Sezgi SarikayaGüvendi Hülya MürüvvetDoğan ArzuZhuri DrenusheGürkan Hakan - Identifying biological roles for glycosyltransferases is a continuing challenge and important for defining morbidities associated with congenital disorders of glycosylation. Here we investigate the consequences to intestinal development of conditionally deleting alone or and together in a mixed or -null genetic background. Each Fringe transfers N-acetylglucosamine (GlcNAc) to fucose (Fuc) attached to Ser or Thr by POFUT1 in a consensus sequence found in certain epithelial growth factor-like (EGF) repeats. EOGT transfers GlcNAc directly to Ser/Thr in a separate consensus sequence of the EGF repeat. Notch receptors and Notch ligands contain the largest number of EGF repeats with consensus sites for these O-glycans. Conditional deletion of in mouse intestine causes similar developmental defects to deletion of and or and . LFNG also contributes to optimal Notch signaling in mouse intestine. In this work, we generated [F/F]: -Cre and [F/F] [-/-] [-/-]: -Cre mice in which extension of O-Fuc on EGF repeats was inhibited or prevented in intestinal epithelium. Conditional deletion of either alone or all three Fringe activities together led to defective intestinal development with a marked increase in goblet and Paneth cells, increased crypt width and reduced villus length. Unexpectedly, in mice globally lacking EOGT, conditional inactivation of the three Fringe genes did not lead to defective intestinal development. Thus, the absence of EOGT prevented disruption of development in Fringe-null intestine, identifying a novel role for EOGT in regulating intestinal development. - Source: PubMed
Publication date: 2026/02/11
Nauman MohdStanley Pamela - - Source: PubMed
- Over the past decade, increasing evidence has linked the dysregulation of human protein O-fucosyltransferase 1 (POFUT1), overwhelmingly through gene overexpression, to tumor progression in multiple cancers, including colorectal, breast, gastric, lung, hepatocellular carcinoma, and glioblastoma. This review provides a comprehensive analysis of the molecular and cellular consequences of POFUT1 dysfunction in cancer. POFUT1 overexpression driven by copy number variations (CNVs), epigenetic alterations, and/or post-transcriptional modifications enhances tumorigenesis by activating key oncogenic pathways such as Notch, Wingless-type MMTV integration site family (Wnt)/β-catenin, and phosphoinositide 3-kinase/protein kinase B/mammalian target of rapamycin (PI3K/AKT/mTOR). These pathways promote cell proliferation, migration, and epithelial-mesenchymal transition (EMT) while simultaneously suppressing apoptosis. Additionally, POFUT1 promotes an immunosuppressive tumor microenvironment that contributes to treatment resistance by immune checkpoint inhibitors. Mainly, its overexpression is detectable at early stages of tumor development and in some cancer patient sera, highlighting its potential as a non-invasive biomarker for early cancer detection and disease monitoring. Given its role in immune evasion and therapy resistance, POFUT1 represents a promising therapeutic target, warranting further investigation into its clinical applications. - Source: PubMed
Publication date: 2025/08/07
Mazour OumaimaLegardinier SébastienBadaoui BouabidGermot Agnès