Glycobiology and Extracellular Matrices
- Aberrant N-glycan sialylation of glycoproteins is closely associated with malignant phenotypes of cancer cells and metastatic potential, which includes cell adhesion, migration, and growth. Recently, phosphatidylinositol 4-kinase IIα (PI4KIIα), which is localized to the trans-Golgi network, was identified as a regulator of Golgi phosphoprotein 3 (GOLPH3) and of vesicle transport in the Golgi apparatus. GOLPH3 is a target of PI4KIIα and helps anchor sialyltransferases and thereby regulates sialylation of cell surface receptors.
- N-Acetylglucosaminyltransferase III (GnT-III), which catalyzes the addition of the bisecting GlcNAc branch on N-glycans, is usually described as a metastasis suppressor. Overexpression of GnT-III inhibited migration in multiple types of tumor cells. However, these results seem controversial to the clinical observations for the increased expression of GnT-III in human hepatomas, glioma, and ovarian cancers. Here, we present evidence that these inconsistencies are mainly attributed to the different expression pattern of cell sialylation.
- Background: The functions of integrin α5 on cell proliferation and the underlying mechanisms remain unclear.Results: Loss of N-glycosylation on α5 increased the phosphorylation and internalization of EGFR and abolished its inhibitory effects on cell proliferation.Conclusion: Integrin α5 regulates EGFR-mediated signaling through N-glycosylation.Significance: N-Glycosylation plays important roles in the cross-talk between integrins and growth factor receptors.