MGAT5 Protein, Human (HEK293, His)

MGAT5 protein is a key enzyme that catalyzes the addition of N-acetylglucosamine (GlcNAc) in beta 1-6 linkage to the alpha-linked mannose of biantennary N-linked oligosaccharides. This catalytic activity is crucial for the biosynthesis of branched, complex-type N-glycans found on various proteins, including EGFR, TGFR (TGF-beta receptor), and CDH2. Through its involvement in complex N-glycan biosynthesis, MGAT5 plays a pivotal role in cellular signaling pathways, actin cytoskeleton reorganization, cell-cell adhesion, and cell migration. Notably, MGAT5-dependent EGFR N-glycosylation prolongs EGFR signaling by preventing rapid endocytosis. MGAT5 is also essential for efficient interactions between TGFB1 and its receptor, enhancing intracellular signaling pathways activated by growth factors like FGF2, PDGF, IGF, TGFB1, and EGF. Additionally, MGAT5-mediated CDH2 N-glycosylation inhibits homotypic cell-cell adhesion, influencing downstream signaling pathways and promoting cell migration. In the immune response, MGAT5-dependent TCR N-glycosylation limits TCR clustering and dampens TCR-mediated responses to antigens, contributing to normal leukocyte evasion and accumulation at inflammatory sites. Moreover, MGAT5 inhibits monocyte attachment to vascular endothelium and subsequent diapedesis, while also promoting proliferation of endothelial cells and angiogenesis by facilitating the release of FGF2 from the extracellular matrix. In summary, MGAT5 emerges as a multifaceted regulator with significant implications in cellular processes, immune responses, and angiogenesis.