Beta-1,3-N-acetylglucosaminyltransferase manic fringe (MFNG)

Beta-1,3-N-acetylglucosaminyltransferase manic fringe (MFNG) is an evolutionarily conserved glycosyltransferase that catalyzes the transfer of N-acetylglucosamine to O-linked fucose residues on EGF-like repeats of the Notch receptor extracellular domain, leading to the formation of GlcNAc-β1,3-Fuc disaccharides[1][3][4]. By modifying these O-fucose residues, MFNG regulates Notch pathway signaling, influencing developmental processes and boundary formation during embryogenesis[3][4]. This enzymatic modification has disease relevance, including possible roles in tumor progression and specific skin and infectious diseases[4]. MFNG operates as part of a conserved gene family with LFNG and RFNG, and demonstrates particular substrate and acceptor specificity in its catalytic mechanism[1][4].

Other names

MFNGO-fucosylpeptide 3-beta-N-acetylglucosaminyltransferaseBeta-1,3-N-acetylglucosaminyltransferaseManic fringeGlycosyltransferase manic fringeO-fucosylpeptide 3-beta-N-acetylglucosaminyltransferase (MFNG)

Elongates O-linked fucose residues on the Notch receptor, altering downstream Notch signaling