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
- Mutations in KRT5, POFUT1, POGLUT1, and PSENEN define four genetic subtypes of Dowling-Degos disease (DDD), with varied clinical and histologic expression including those previously reported as Galli-Galli disease. We report a case of DDD3 associated with a novel early nonsense variant in POGLUT1 (c.12G>A; p.Trp4*), representing, to the best of our knowledge, the first documented case in Spain. A 55-year-old man presented with recurrent pruritic erythematous scaly papules on the trunk and hyperkeratotic brown papules on the cervical and thoracic regions. Direct microscopic examination of scales from erythematous lesions revealed yeast cells and short hyphae compatible with Malassezia sp. Initial histopathologic evaluation of a pigmented papule was interpreted as simple lentigo. Subsequent biopsy demonstrated elongated rete ridges and focal suprabasal acantholysis without dyskeratosis, raising suspicion for DDD. Whole-exome sequencing identified a heterozygous nonsense variant in POGLUT1, confirming the diagnosis of DDD3. Previous studies have shown that diffuse cytokeratin 5 (CK5) expression throughout all epidermal layers may support the diagnosis of DDD3. This case highlights diagnostic pitfalls related to subtle and focal acantholysis, emphasizes the importance of clinicopathologic correlation and serial sectioning. - Source: PubMed
Publication date: 2026/05/27
González Fernández JoséGarcía García MarLarrosa Martínez DiegoAra Martín Marianode la Fuente Meira SoniaPrieto Torres Lucía - 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 Lfng alone or Lfng, Mfng and Rfng together in a mixed or Eogt-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 an EGF repeat. Notch receptors and Notch ligands contain the largest number of EGF repeats with consensus sites for these O-glycans. Conditional deletion of Pofut1 in mouse intestine causes similar developmental defects to deletion of Notch1 and Notch2 or Dll1 and Dll4. LFNG also contributes to optimal Notch signaling in mouse intestine. In this work, we generated Lfng[F/F]:Villin-Cre and Lfng[F/F]Mfng[-/-]Rfng[-/-]:Villin-Cre mice in which extension of O-Fuc on EGF repeats was respectively inhibited or prevented in intestinal epithelium. Conditional deletion of either Lfng 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: 2026/06/09
Nauman MohdZhang JinghangStanley Pamela - Preeclampsia (PE) is a severe pregnancy disorder caused by placental dysfunction. Protein O-fucosylation is a type of protein post translational modification that is catalyzed by protein O-fucosyltransferases (poFUTs). However, the role and underlying mechanisms of O-fucosylation/poFUT1 in PE remain elusive. Here, we revealed a lower level of poFUT1 in the plasma and placental tissues of PE patients than in normal pregnancy (NP) women. Moreover, poFUT1 deletion induced PE-like phenotypes in a mouse model. Mechanistically, we globally screened O-fucosylated proteins and identified EDIL3 with an O-fucosylation site at threonine 88. Furthermore, O-fucosylation-EDIL3 can directly interact with LIFR on trophoblasts, consequently activating the STAT3 signaling pathway, promoting the invasion and vascular remodeling ability of trophoblasts. Conversely, de-O-fucosylation-EDIL3 aggravated PE-like phenotypes by attenuating placental development in vitro and in vivo. Our data elucidate the function of poFUT1/O-fucosylation EDIL3/LIFR axis during placental development, providing glycol-based target for diagnostic and therapeutic of preeclampsia. - Source: PubMed
Publication date: 2026/05/13
Li YaqiWu HongpanLei YuyuBai ShuyuWang JiaoYan BinLiu YuboLiu Shuai - Aberrant protein O-fucosylation mediated by protein O-fucosyltransferase 1 (POFUT1), has emerged as a hallmark of tumorigenesis that regulates key signaling pathways, including Notch, which is frequently dysregulated in cancers. Protein O-fucosylation, catalyzed by POFUT1, regulates Notch signaling and has been implicated in individual cancers, but its pan-cancer expression patterns, clinical significance, and relationship to tumor immunity remain incompletely characterized. - Source: PubMed
Publication date: 2026/04/23
Ullah ZakirPei XiaosongAli PerbhatUllah IkramLi YaqiLiu Shuai - 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