Glucoside xylosyltransferase 1 (GXYLT1)

Glucoside xylosyltransferase 1 (GXYLT1) is an enzyme classified within the glycosyltransferase 8 family and functions as a UDP-xylose:β-glucoside α1,3-xylosyltransferase[1][3][4][7][12]. It catalyzes the transfer of a xylose residue onto O-glucosylated serine residues within the EGF-like repeats of substrate proteins, including the Notch receptor, which is critical for assembling the proper trisaccharide structure needed for modulating Notch signaling[1][4][7][12]. Through this modification, GXYLT1 influences Notch receptor activation, ligand binding, receptor trafficking, and downstream cell signaling[1][3]. Pathologically, GXYLT1 is often altered in cancers such as colorectal cancer, where its upregulation may enhance migration, invasion, and metastasis[1]. It is also upregulated in acute myeloid leukemia cells upon Notch activation[1]. GXYLT1 is associated with a range of genetic diseases implicating its importance in development and homeostasis[3][12].

Other names

GLT8D3Glycosyltransferase 8 domain-containing protein 3FLJ43151glycosyltransferase 8 domain containing 3glucoside xylosyltransferase 1GXYLT1

none known (no approved or experimental drugs directly target this enzyme as of current knowledge)