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Gene Review

Pofut1  -  protein O-fucosyltransferase 1

Mus musculus

Synonyms: GDP-fucose protein O-fucosyltransferase 1, O-FucT-1, Peptide-O-fucosyltransferase 1, mKIAA0180
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High impact information on Pofut1

  • Homozygous mutant embryos derived from eggs lacking Pofut1 gene transcripts developed indistinguishably from the wild type until approximately embryonic day 8.0, a postgastrulation stage after the formation of the three germ layers [1].
  • To test this directly, we used conditional deletion in oocytes carrying a ZP3Cre recombinase transgene to generate mouse embryos lacking both maternal and zygotic protein O-fucosyltransferase 1, a cell-autonomous and essential component of canonical Notch receptor signaling [1].
  • These domains are also the target of sequential complex O-linked glycosylation mediated by protein O-fucosyltransferase 1 and Fringe [2].
  • The mouse gene (Pofut1) maps near Plagl2 on a homologous region of mouse chromosome 2 [3].
  • The enzyme that adds O-fucose to epidermal growth factor-like repeats, GDP-fucose protein O-fucosyltransferase (O-FucT-1), was purified previously from Chinese hamster ovary (CHO) cells [3].

Biological context of Pofut1

  • 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 [4].
  • The identification of the gene encoding protein O-fucosyltransferase I now makes possible mutational strategies to examine the functions of the unusual O-fucose post-translational modification [3].
  • The last common ancestor of all analyzed bilaterian species would be predicted to possess polyexonic Pofut genes in their genome [5].
  • Molecular evolution of protein O-fucosyltransferase genes and splice variants [5].

Anatomical context of Pofut1


Other interactions of Pofut1

  • To date, Pofut1 genes have only been characterized in human, mouse, and fly, and Pofut2 in mouse, fly, and partially in the nematode Caenorhabditis elegans [5].

Analytical, diagnostic and therapeutic context of Pofut1


  1. Canonical Notch signaling is dispensable for early cell fate specifications in mammals. Shi, S., Stahl, M., Lu, L., Stanley, P. Mol. Cell. Biol. (2005) [Pubmed]
  2. CADASIL mutations impair Notch3 glycosylation by Fringe. Arboleda-Velasquez, J.F., Rampal, R., Fung, E., Darland, D.C., Liu, M., Martinez, M.C., Donahue, C.P., Navarro-Gonzalez, M.F., Libby, P., D'Amore, P.A., Aikawa, M., Haltiwanger, R.S., Kosik, K.S. Hum. Mol. Genet. (2005) [Pubmed]
  3. Modification of epidermal growth factor-like repeats with O-fucose. Molecular cloning and expression of a novel GDP-fucose protein O-fucosyltransferase. Wang, Y., Shao, L., Shi, S., Harris, R.J., Spellman, M.W., Stanley, P., Haltiwanger, R.S. J. Biol. Chem. (2001) [Pubmed]
  4. Evolutionary origins of Notch signaling in early development. Shi, S., Stanley, P. Cell Cycle (2006) [Pubmed]
  5. Molecular evolution of protein O-fucosyltransferase genes and splice variants. Loriol, C., Dupuy, F., Rampal, R., Dlugosz, M.A., Haltiwanger, R.S., Maftah, A., Germot, A. Glycobiology (2006) [Pubmed]
  6. The canonical Notch/RBP-J signaling pathway controls the balance of cell lineages in mammary epithelium during pregnancy. Buono, K.D., Robinson, G.W., Martin, C., Shi, S., Stanley, P., Tanigaki, K., Honjo, T., Hennighausen, L. Dev. Biol. (2006) [Pubmed]
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