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Protein O-fucosyltransferase 1

Pofut1, protein O-fucosyltransferase 1
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. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: fucosyltransferase, Epidermal Growth Factor, CAN, p300, FATE
Papers using Pofut1 antibodies
Gaussian 09, RevisionA.
Song Haiwei, In PLoS ONE, 2008
... POFUT1 (swissprot: locus OFUT1_ CAEEL; accession Q18014; GeneID: C15C7.7),
Papers on Pofut1
Dowling-Degos disease co-presenting with Darier disease.
Mousdicas et al., Indianapolis, United States. In Clin Exp Dermatol, Jan 2016
DDD results from mutations in the genes encoding keratin 5 (KRT5), protein O-glucosyltransferase 1 (POGLUT1) or protein O-fucosyltransferase 1 (POFUT1), while DD results from mutations in the ATP2A2 gene.
O-fucose monosaccharide of Drosophila Notch has a temperature-sensitive function and cooperates with O-glucose glycan in Notch transport and Notch signaling activation.
Matsuno et al., Chiba, Japan. In J Biol Chem, Feb 2015
N has many epidermal growth factor-like repeats that are O-fucosylated by the protein O-fucosyltransferase 1 (O-Fut1), and the O-fut1 gene is essential for N signaling.
Protein O-fucosyltransferase 1 expression impacts myogenic C2C12 cell commitment via the Notch signaling pathway.
Germot et al., Limoges, France. In Mol Cell Biol, 2015
O-fucosylation on Notch receptor epidermal growth factor (EGF)-like repeats is catalyzed by the protein O-fucosyltransferase 1 (Pofut1) and primarily controls Notch interaction with its ligands.
O-fucosylation of DLL3 is required for its function during somitogenesis.
Gossler et al., Hannover, Germany. In Plos One, 2014
Here, we show that i) both proteins interact, ii) epidermal growth factor like repeats 2 and 5 of DLL3 are O-fucosylated at consensus sites for POFUT1, and iii) further modified by FNG proteins in vitro.
Novel roles for O-linked glycans in protein folding.
Haltiwanger et al., Stony Brook, United States. In Glycoconj J, 2014
Notably, Protein O-fucosyltransferase 1 (Ofut1/Pofut1), a soluble, ER localized enzyme that fucosylates Epidermal Growth Factor-like (EGF) repeats, functions as a chaperone involved in the proper localization of the Notch receptor in certain contexts.
Downregulated protein O-fucosyl transferase 1 (Pofut1) expression exerts antiproliferative and antiadhesive effects on hepatocytes by inhibiting Notch signalling.
Zhang et al., Dalian, China. In Biomed Pharmacother, 2014
Critical to this process is the influence of Pofut1 whose function is to fucosylate Notch receptors and ligands on the cell surface for proper interaction.
Prognostic relevance of glycosylation-associated genes in breast cancer.
Müller et al., Hamburg, Germany. In Breast Cancer Res Treat, 2014
In the second cohort, six of the 24 relevant genes were of prognostic significance (FUT1, FUCA1, POFUT1, MAN1A1, RPN1 and DPM1), whereas a trend was observed for three additional probesets (GCNT4, ST3GAL6 and UGCG).
Mutations in POGLUT1, encoding protein O-glucosyltransferase 1, cause autosomal-dominant Dowling-Degos disease.
Betz et al., Bonn, Germany. In Am J Hum Genet, 2014
Recently, mutations in POFUT1, which encodes protein O-fucosyltransferase 1, were also reported to be responsible for DDD.
Protein O-fucosyltransferase 1: a potential diagnostic marker and therapeutic target for human oral cancer.
Uzawa et al., Chiba, Japan. In Int J Oncol, 2013
Protein O-fucosyltransferase 1 (POFUT1) is the enzyme that 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.
Analysis of POFUT1 gene mutation in a Chinese family with Dowling-Degos disease.
Zhang et al., Hefei, China. In Plos One, 2013
Though KRT5 has been identified to be the causal gene of DDD, the heterogeneity of this disease was displayed: for example, POFUT1 and POGLUT1 were recently identified and confirmed to be additional pathogenic genes of DDD.
O-fucosylation of the notch ligand mDLL1 by POFUT1 is dispensable for ligand function.
Gossler et al., Hannover, Germany. In Plos One, 2013
Fucosylation of Epidermal Growth Factor-like (EGF) repeats by protein O-fucosyltransferase 1 (POFUT1 in vertebrates, OFUT1 in Drosophila) is pivotal for NOTCH function.
Metabolism and transportation pathways of GDP-fucose that are required for the O-fucosylation of Notch.
Matsuno et al., Noda, Japan. In Adv Exp Med Biol, 2011
Some of these EGF-like repeats are O-fucosylated by protein O-fucosyltransferase 1 (O-fut1), which is essential for Notch signaling in Drosophila and mouse.
Protein O-fucosyltransferase 1 (Pofut1) regulates lymphoid and myeloid homeostasis through modulation of Notch receptor ligand interactions.
Zhou et al., Cleveland, United States. In Blood, 2011
Loss of Pofut1 is associated with myeloid hyperplasia and impaired lymphopoiesis.
Regulation of Notch signaling during T- and B-cell development by O-fucose glycans.
Guidos et al., New York City, United States. In Immunol Rev, 2009
These glycans are initiated by protein O-fucosyltransferase 1 (Pofut1), and elongated by the transfer of N-acetylglucosamine (GlcNAc) to the fucose by beta1,3GlcNAc-transferases termed lunatic, manic, or radical fringe.
Notch signalling in the paraxial mesoderm is most sensitive to reduced Pofut1 levels during early mouse development.
Gossler et al., Hannover, Germany. In Bmc Dev Biol, 2008
Reduced POFUT1 levels might affect Notch trafficking or overall O-fucosylation.
O-fucosylation of muscle agrin determines its ability to cluster acetylcholine receptors.
Martin et al., Columbus, United States. In Mol Cell Neurosci, 2008
These data are consistent with a role for Pofut1 in AChR aggregation during synaptogenesis via the regulation of the synaptogenic activity of muscle agrin.
[Regulation of notch signaling by O-linked glycosylations].
Matsuno et al., In Tanpakushitsu Kakusan Koso, 2008
It regulates notch signaling by glycosylation.(review)
Pofut1 is required for the proper localization of the Notch receptor during mouse development.
Saga et al., Mishima, Japan. In Mech Dev, 2008
Pofut1 is required for Notch signaling upstream of NICD1.
Evolutionary origins of Notch signaling in early development.
Stanley et al., New York City, United States. In Cell Cycle, 2006
Thus it is surprising that the removal of maternal and zygotic protein O-fucosyltransferase 1 (Pofut1), an essential component of the canonical Notch signaling pathway, does not affect early embryogenesis in the mouse.
Chaperone activity of protein O-fucosyltransferase 1 promotes notch receptor folding.
Irvine et al., United States. In Science, 2005
OFUT1 has a distinct Notch chaperone activity; binds to Notch; required for the trafficking of wild-type Notch out of the endoplasmic reticulum; ability to facilitate folding of Notch
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