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the reported Dowling-Degos mutations of POFUT1, except for M262T, fail to rescue Notch1 signaling efficiently in the CRISPR-engineered POFUT1-/- background; these studies identify POFUT1 as a potential target for cancers driven by Notch1 mutations and provide a structural roadmap for its inhibition
The results suggest that this N-glycan of POFUT1 is not required for its proper enzymatic function, and that the p.Ser162Leu mutation of POFUT1 likely causes global developmental delay, microcephaly with vascular and cardiac defects.
Our findings suggested that overexpression of Pofut1 and activated Notch1 signaling may be associated with a poor prognosis in breast cancer.
POFUT1 gene expression in gastric cancer
POFUT1, POGLUT1 and ADAM10 are processing enzymes that are involved in different steps of Notch receptor activation in the epidermis; the roles of these unique enzymes in a single pathway may explain both the overlapping and distinct clinical features of DDD and RAK patients
High expression of POFUT1 correlates with aggressive clinicopathological characteristics and poor prognosis of hepatocellular carcinoma patients.
The upregulation of poFUT1 by LIF facilitated trophoblast cell migration and invasion through activating the PI3K/Akt signaling pathway.
Silencing of Pofut1 expression exerted antiproliferative and antiadhesive effects on hepatocytes.
Only a novel 1-bp deletion (c.246+5delG) in POFUT1 was found in a Chinese family with Dowling-Degos disease (DDD). No other novel mutation or this deletion was detected in POFUT1 in a second DDD family and a sporadic DDD case by Sanger Sequencing.
Identification of six pathogenic POFUT1 mutations in Dowling-Degos disease patients of different ethnic origin.
POFUT1 expression can contribute to cancer progression and that POFUT1 may serve as a diagnostic marker and a therapeutic target for OSCCs.
The protein product of POFUT1 plays a significant and conserved role in melanin synthesis and transport.
fucosyltransferases, O-FucT-1 is a soluble protein that localizes to the endoplasmic reticulum and recognizes properly folded epidermal growth factor-like repeats.
Pofut1 and O-fucose have roles in mammalian Notch signaling
POFUT1 inactivation disrupts angiogenic signaling events and results in excessive angiogenic cell proliferation and plexus formation, leading to anomalous coronary arteries, myocardial infarction and heart failure.
both wild-type and mutant Pofut1 proteins were degraded through lysosome dependent machinery. Pofut1 protein loss in the point mutant embryos caused the same phenotypes as those observed in Pofut1 null embryos
The POFUT1 binds EGF-like domains of the hEGF type and that the highly correlated presence of POFUT1 and fucosylatable hEGFs has accompanied animal evolution.
Loss of Pofut1 expression is associated with Muscle Aging-Related Phenotypes.
results demonstrated that POFUT1-mediated O-fucosylation of NOTCH receptors regulates myogenic cell differentiation and affects postnatal muscle growth in mice
results establish the critical role of Pofut1 on Notch pathway activation during myogenic differentiation
mDLL1 O-fucosylation by POFUT1 is dispensable for ligand function
Loss of Pofut1 is associated with myeloid hyperplasia and impaired lymphopoiesis.
Pofut1 is required for Notch signaling upstream of NICD1.
These data are consistent with a role for Pofut1 in AChR aggregation during synaptogenesis via the regulation of the synaptogenic activity of muscle agrin.
Reduced POFUT1 levels might affect Notch trafficking or overall O-fucosylation.
This gene encodes a member of the glycosyltransferase O-Fuc family. This enzyme adds O-fucose through an O-glycosidic linkage to conserved serine or threonine residues in the epidermal growth factor-like repeats of a number of cell surface and secreted proteins. O-fucose glycans are involved in ligand-induced receptor signaling. Alternative splicing of this gene results in two transcript variants encoding different isoforms.
GDP-fucose protein O-fucosyltransferase 1
, putative protein-O-fucosyltransferase
, peptide-O-fucosyltransferase 1
, protein-O-fucosyltransferase 1
, protein O-fucosyltransferase 1
, o-fucosyltransferase protein