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Glycobiology and Extracellular Matrices
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- Glycobiology and Extracellular MatricesOpen Access
A complex between phosphatidylinositol 4-kinase IIα and integrin α3β1 is required for N-glycan sialylation in cancer cells
Journal of Biological ChemistryVol. 294Issue 12p4425–4436Published online: January 18, 2019- Tomoya Isaji
- Sanghun Im
- Akihiko Kameyama
- Yuqin Wang
- Tomohiko Fukuda
- Jianguo Gu
Cited in Scopus: 16Aberrant 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.