Integrins are cell surface transmembrane glycoproteins that function as adhesion receptors in cell-ECM interactions and link matrix proteins to the cytoskeleton. Integrins play an important role in cytoskeleton organization and in the transduction of intracellular signals, regulating various processes such as proliferation, differentiation, apoptosis, and cell migration. Although integrin-mediated adhesion is based on the binding of α and β subunits to a defined peptide sequence, the strength of this binding is modulated by various factors including the status of glycosylation of integrin. Glycosylation reactions are catalyzed by the catalytic action of glycosyltransferases, such as N-acetylglucosaminyltransferase III, V and α1,6 fucosyltransferase, etc., which catalyze the formation of glycosidic bonds. In this talk we will briefly overview the N-glycan structures of integrins, such as α3β1 and α5β1, and their related functions arising from recent studies, which provide insight into some long-standing questions concerning N-glycosylation functions.