Literature summary for 2.4.1.221 extracted from

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 (2015), Mol. Cell. Biol., 35, 391-405.

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Cloned(Commentary)

Cloned (Comment)	Organism
gene Pofut1, semiquantitative real-time RT-PCR enzyme expression analysis	Mus musculus

Protein Variants

Protein Variants	Comment	Organism
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	Mus musculus

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
endoplasmic reticulum	Pofut1 mainly colocalizes with GRP94, an endoplasmic reticulum chaperone	Mus musculus	5783	-

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
additional information	Mus musculus	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	?	-	?

Organism

Organism	UniProt	Comment	Textmining
Mus musculus	Q91ZW2	gene POFUT1	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
embryo	-	Mus musculus	-
myoblast	-	Mus musculus	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	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	Mus musculus	?	-	?

Synonyms

Synonyms	Comment	Organism
Pofut1	-	Mus musculus
protein O-fucosyltransferase 1	-	Mus musculus

General Information

General Information	Comment	Organism
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	Mus musculus
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	Mus musculus

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Release 2023.1 (January 2023)