Beta-1,3-N-acetylglucosaminyltransferase lunatic fringe (LFNG)

Beta-1,3-N-acetylglucosaminyltransferase lunatic fringe (LFNG) is an enzyme encoded by the LFNG gene in humans. It is a single-pass type II Golgi membrane protein and a key member of the glycosyltransferase superfamily, functioning as a fucose-specific glycosyltransferase. LFNG modifies Notch family receptors by adding N-acetylglucosamine to O-linked fucose residues on their epidermal growth factor-like repeats, affecting the affinity and activation response to various Notch ligands. This modulation is essential for regulating cell fate decisions during development, especially for establishing boundaries in somitogenesis—segmental organization that leads to formation of vertebrae, ribs, and related tissues. Mutations in LFNG lead to autosomal recessive spondylocostal dysostosis 3, characterized by severe vertebral and rib malformations. LFNG plays a pivotal role in the segmentation clock, crucial for normal vertebrate axial patterning, and its loss or malfunction disrupts Notch signaling dynamics, yielding developmental disorders[1][2][3][4][5].

Other names

Lunatic FringeO-fucosylpeptide 3-beta-N-acetylglucosaminyltransferaseSCDO3beta-1,3-N-acetylglucosaminyltransferase lunatic fringe

Drugs or inhibitors would modulate Notch pathway signaling by altering glycosylation on Notch receptors.