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Fucosyltransferase 8 (FUT8)-mediated core fucosylation is a critical post-translational
modification that regulates diverse physiological and pathological processes. In oncology, FUT8 drives breast cancer cell invasiveness and metastasis by
fucosynthesizing TGF-β receptors to amplify growth signaling. Quantitative glycoproteomics reveals 140 core-fucosylated target glycoproteins—including those in IL-6 and integrin networks—that facilitate tumor cell migration and cell-matrix adhesion. Disabling the FUT8 gene successfully suppresses this metastatic behavior.
In vascular biology, FUT8-dependent core fucosylation is essential for platelet function, dramatically enhancing platelet binding to collagen and fibrinogen.
Consequently, genetic deletion or pharmacological inhibition of FUT8 prevents dangerous blood lotting, establishing it as a promising therapeutic target for thrombosis. Finally, structural analyses of the mushroom-derived lectin PhoSL show that its high-precision recognition of core-fucosylated glycans relies on its N-terminal integrity, which stabilizes the fucose-binding pocket. Altering this structure reduces PhoSL's cytotoxicity against breast cancer cells, highlighting its value in developing new diagnostic and therapeutic strategies. Together, these studies highlight the FUT8 axis as a highly viable therapeutic target across thromboinflammatory and metastatic diseases.