Abstract
Integrin-mediated cell-matrix adhesion plays an important role in control of cell behavior. We report here that MIG-2, a widely expressed focal adhesion protein, interacts with beta1 and beta3 integrin cytoplasmic domains. Integrin binding is mediated by a single site within the MIG-2 FERM domain. Functionally, the MIG-2/integrin interaction recruits MIG-2 to focal adhesions. Furthermore, using alphaIIbbeta3 integrin-expressing Chinese hamster ovary cells, a well described model system for integrin activation, we show that MIG-2 promotes integrin activation and enhances cell-extracellular matrix adhesion. Although MIG-2 is expressed in many cell types, it is deficient in certain colon cancer cells. Expression of MIG-2, but not of an integrin binding-defective MIG-2 mutant, in MIG-2-null colon cancer cells strengthened cell-matrix adhesion, promoted focal adhesion formation, and reduced cell motility. These results suggest that the MIG-2/integrin interaction is an important element in the cellular control of integrin-mediated cell-matrix adhesion and that loss of this interaction likely contributes to high motility of colon cancer cells.
Highlights
Cell-extracellular matrix (ECM)3 adhesion is a fundamental process that is mediated by transmembrane receptors such as integrins [1,2,3,4,5,6]
The experiments presented in this study have demonstrated a specific interaction between MIG-2 and the 1 and 3 integrin cytoplasmic domains
We have shown that the MIG-2/integrin interaction is essential for recruiting MIG-2 to FAs
Summary
Cell-extracellular matrix (ECM)3 adhesion is a fundamental process that is mediated by transmembrane receptors such as integrins [1,2,3,4,5,6]. To assess FA formation, SK-LMS-1 or RKO cells infected with the control -galactosidase adenovirus or adenoviruses encoding wild-type or mutant MIG-2 were plated on coverslips and cultured as specified in each experiment. To test whether integrin binding plays a role in this process, we transfected cells with vectors encoding GFP-tagged wild-type MIG-2 or integrin binding-defective mutant ⌬FERM or Q614A/W615A.
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