Multicellular life requires the formation of extracellular matrices and the sensing of the cell environment through regulated adhesive interactions. By coupling the binding of extracellular adhesion proteins to the assembly of intracellular cytoskeletal and signalling complexes, integrin receptors mediate the bidirectional transmission of mechanical force and biochemical signals across the plasma membrane. Integrin-based adhesion is highly dynamic, as cells must rapidly respond to changes in their environment by altering their migratory properties, gene expression profile and proliferation state. A detailed, integrative view of the dynamics of adhesion complexes would provide insight into the molecular mechanisms that control cell morphology, movement, survival and differentiation, but, as with other membrane receptor-associated signalling complexes, integrin adhesion complexes have been refractory to isolation due to their instability and inaccessibility. A literature-curated model for the composition of adhesion complexes has revealed massive complexity (1), but despite decades of work, the global composition and mechanisms of regulation of integrin-associated protein complexes are relatively poorly understood. We reasoned that there was a need for technologies that enable systematic, proteomic analysis, and accordingly we have developed a methodology for the affinity isolation and mass spectrometric analysis of integrin adhesion complexes (2). In follow-up studies to this original publication, the isolation of stabilised complexes associated with multiple integrin receptor-ligand pairs, and detailed quantitative analyses of their composition at multiple time points and in different receptor activation states, have been carried out. Our analyses have defined temporal profiles of integrin-associated protein complexes during the initial stages of cell adhesion, and compared the complexes that are assembled by integrins occupied either by ligands or by monoclonal antibodies that freeze receptor conformation in different states of activation. Hierarchical clustering and protein interaction network analyses reveals distinct dynamics of protein modules relevant to cell adhesion processes. Although we should not underestimate the scale of the task, the development of this workflow now permits the molecular dynamics of adhesion complexes to be measured directly and presents an entry point for quantitative, systems-level analyses of adhesion signalling in health and disease.