The extracellular matrix (ECM) activates signalling pathways that control cell behaviour by binding to cell-surface integrin receptors and inducing the formation of focal adhesion complexes (FACs) [1,2]. In addition to clustered integrins, FACs contain proteins that mechanically couple the integrins to the cytoskeleton  and to immobilized signal-transducing molecules [1,2]. Cell adhesion to the ECM also induces a rapid increase in the translation of pre-existing messenger RNAs [4,5]. Gene expression can be controlled locally by targeting mRNAs to specialized cytoskeletal domains . Here we investigate whether cell binding to the ECM promotes formation of a cytoskeletal microcompartment specialized for translational control at the site of integrin binding. High-resolution in situ hybridization revealed that mRNA and ribosomes rapidly and specifically localized to FACs that form when cells bind to ECM-coated microbeads. Relocations of these protein synthesis components to the FAC depended on the ability of integrins to mechanically couple the ECM to the contractile cytoskeleton and on associated tension-moulding of the actin lattice. Our results suggest a new type of gene regulation by integrins and by mechanical stress which may involve translation of mRNAs into proteins near the site of signal reception.