POFUT1 Human

Protein O-Fucosyltransferase 1 (POFUT1) is an enzyme that plays a crucial role in the post-translational modification of proteins. It specifically catalyzes the transfer of fucose, a sugar molecule, to serine or threonine residues on target proteins. This modification is known as O-fucosylation and is essential for the proper functioning of several proteins, including those involved in Notch signaling pathways .

POFUT1 is a type II membrane protein located in the endoplasmic reticulum. It has a short N-terminal cytoplasmic domain, a single transmembrane domain, and a large C-terminal catalytic domain that faces the lumen of the endoplasmic reticulum . The enzyme recognizes specific consensus sequences on target proteins and attaches fucose to them, which can further be modified by other enzymes to form more complex glycan structures .

O-fucosylation mediated by POFUT1 is critical for the proper functioning of the Notch signaling pathway, which is involved in cell differentiation, proliferation, and apoptosis. Notch receptors, which are modified by POFUT1, interact with ligands to initiate signaling cascades that regulate gene expression . Disruptions in O-fucosylation can lead to various developmental disorders and diseases, including cancer .

Recombinant human POFUT1 is produced using advanced biotechnological methods. Typically, the gene encoding POFUT1 is cloned into an expression vector and introduced into a suitable host cell line, such as a mouse myeloma cell line (NS0). The host cells are cultured under conditions that promote the expression of the recombinant protein, which is then purified using techniques like affinity chromatography .

Recombinant POFUT1 is used in various research applications to study the mechanisms of O-fucosylation and its role in cellular processes. It is also employed in the development of therapeutic strategies targeting diseases associated with aberrant Notch signaling .