A proteomic approach reveals integrin activation state-dependent control of microtubule cortical targeting.

ABSTRACT: Integrin 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

SUBMITTER: Byron A 

PROVIDER: S-EPMC4317495 | biostudies-literature | 2015 Jan

REPOSITORIES: biostudies-literature