Proteomic analysis of integrin adhesion complexes

Adam Byron, Jonathan D. Humphries, Mark D. Bass, David Knight, Martin J. Humphries

    Research output: Contribution to journalArticlepeer-review


    Integrin receptors regulate cell fate by coupling the binding of extracellular adhesion proteins to the assembly of intracellular cytoskeletal and signaling complexes. A detailed, integrative view of adhesion complexes will provide insight into the molecular mechanisms that control cell morphology, survival, movement, and differentiation. To date, membrane receptor-associated signaling complexes have been refractory to proteomic analysis because of their inherent lability and inaccessibility. We developed a methodology to isolate ligand-induced integrin adhesion complexes, and we used this technique to analyze the composition of complexes associated with multiple receptor-ligand pairs and define core and receptor-specific subnetworks. In particular, we identified regulator of chromosome condensation-2 (RCC2) as a component of fibronectin-activated signaling pathways that regulate directional cell movement. The development of this proteomics pipeline provides the means to investigate the molecular composition and function of various adhesion complexes. © 2011 American Association for the Advancement of Science. All Rights Reserved.
    Original languageEnglish
    Article numberpt2
    JournalScience Signaling
    Issue number167
    Publication statusPublished - 5 Apr 2011


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