Byron, AdamAskari, Janet A.Humphries, Jonathan D.Jacquemet, GuillaumeKoper, Ewa J.Warwood, StaceyChoi, Colin K.Stroud, Matthew J.Chen, ChristopherKnight, DavidHumphries, Martin J.2015-03-022015Byron, A., J. A. Askari, J. D. Humphries, G. Jacquemet, E. J. Koper, S. Warwood, C. K. Choi, et al. 2015. “A proteomic approach reveals integrin activation state-dependent control of microtubule cortical targeting.” Nature Communications 6 (1): 6135. doi:10.1038/ncomms7135. http://dx.doi.org/10.1038/ncomms7135.2041-1723http://nrs.harvard.edu/urn-3:HUL.InstRepos:14065520Integrin activation, which is regulated by allosteric changes in receptor conformation, enables cellular responses to the chemical, mechanical and topological features of the extracellular microenvironment. A global view of how activation state converts the molecular composition of the region proximal to integrins into functional readouts is, however, lacking. Here, using conformation-specific monoclonal antibodies, we report the isolation of integrin activation state-dependent complexes and their characterization by mass spectrometry. Quantitative comparisons, integrating network, clustering, pathway and image analyses, define multiple functional protein modules enriched in a conformation-specific manner. Notably, active integrin complexes are specifically enriched for proteins associated with microtubule-based functions. Visualization of microtubules on micropatterned surfaces and live cell imaging demonstrate that active integrins establish an environment that stabilizes microtubules at the cell periphery. These data provide a resource for the interrogation of the global molecular connections that link integrin activation to adhesion signalling.en-USJournal Article2015-03-0210.1038/ncomms7135