Glycosyltransferase 8 domain-containing protein 2 (GLT8D2)

Glycosyltransferase 8 domain-containing protein 2 (GLT8D2) is an enzyme in the glycosyltransferase 8 (GT8) family, responsible for catalyzing the addition of sugar groups to proteins and other molecules. It is a type II membrane-associated glycoprotein broadly expressed in tissues such as gall bladder and ovary[4][6]. GLT8D2 regulates key cell processes, including cell adhesion and signaling, and has strong links to oncogenesis; its overexpression is associated with tumor progression, poor prognosis, and chemotherapy resistance in several cancers, notably ovarian and gastric cancer[2][4][5]. Mechanistically, GLT8D2 interacts with fibroblast growth factor receptor 1 (FGFR1), thereby modulating the FGFR/PI3K/Akt signaling axis to enhance cell survival and drug resistance[4][5]. Additionally, it influences immune cell infiltration and macrophage polarization, suggesting roles in immune evasion and tumor microenvironment modulation[2]. Inhibition or targeting of GLT8D2 (or its downstream pathways) can potentially restore sensitivity to platinum-based chemotherapy, making it a promising therapeutic target in drug-resistant malignancies[4][5].

Other names

GLT8D2GALA4AUNQ1901/PRO4347FLJ31494

Drugs targeting GLT8D2 (e.g., FGFR inhibitors) act by inhibiting the FGFR/PI3K/Akt signaling cascade that is upregulated by GLT8D2 overexpression in cancer cells, reversing chemoresistance. Pharmacological targeting of GLT8D2 may sensitize cancer cells to platinum drugs by affecting glycosylation-related cell signaling and survival pathways.