The insulin-like growth factor-I receptor (IGF-IR) is an ubiquitous multifunctional tyrosine kinase growth factor receptor that has been implicated in a wide variety of cellular functions including cell proliferation, cell differentiation, cell migration and apoptosis. Recent studies have shown that IGF-IR can promote cell motility by regulating both cell-cell adhesion and cell-extracellular matrix interactions. Thus, evidence is emerging that there may be molecular crosstalk between cell adhesion molecules such as E-cadherin and integrins and IGF-IR. The goal of this review is to introduce recent data concerning the physical and functional interactions between IGF-IR, integrins and E-cadherin. The existence of a supramolecular complex containing at least E-cadherin, IGF-IR and some integrins is discussed.