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RSS FeedsA complex between phosphatidylinositol 4-kinase II{alpha} and integrin {alpha}3{beta}1 is required for N-glycan sialylation in cancer cells [Glycobiology and Extracellular Matrices] (Journal of Biological Chemistry)

 
 

22 march 2019 09:00:41

 
A complex between phosphatidylinositol 4-kinase II{alpha} and integrin {alpha}3{beta}1 is required for N-glycan sialylation in cancer cells [Glycobiology and Extracellular Matrices] (Journal of Biological Chemistry)
 


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 II? (PI4KII?), 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 PI4KII? and helps anchor sialyltransferases and thereby regulates sialylation of cell surface receptors. However, how PI4KII?-mediated sialyation of cell surface proteins is regulated remains unclear. In this study, using several cell lines, CRISPR/Cas9-based gene knockout and short hairpin RNA-mediated silencing, RT-PCR, lentivirus-mediated overexpression, and immunoblotting methods, we confirmed that PI4KII? knockdown suppresses the sialylation of N-glycans on the cell surface, in Akt phosphorylation and activation, and integrin ?3-mediated cell migration of MDA-MB-231 breast cancer cells. Interestingly, both integrin ?3?1 and PI4KII? co-localized to the trans-Golgi network, where they physically interacted with each other, and PI4KII? specifically associated with integrin ?3 but not ?5. Furthermore, overexpression of both integrin ?3?1 and PI4KII? induced hypersialylation. Conversely, integrin ?3 knockout significantly inhibited the sialylation of membrane proteins, such as the epidermal growth factor receptor, as well as in total cell lysates. These findings suggest that the malignant phenotype of cancer cells is affected by a sialylation mechanism that is regulated by a complex between PI4KII? and integrin ?3?1.


 
58 viewsCategory: Biochemistry
 
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