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Sci. Signal., 5 April 2011 PRESENTATIONSProteomic Analysis of Integrin Adhesion Complexes
Adam Byron1,2,*,
Jonathan D. Humphries1,2,
Mark D. Bass1,2,
1 Wellcome Trust Centre for Cell-Matrix Research, University of Manchester, Manchester M13 9PT, UK. Abstract: 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.
Citation: A. Byron, J. D. Humphries, M. D. Bass, D. Knight, M. J. Humphries, Proteomic Analysis of Integrin Adhesion Complexes. Sci. Signal. 4, pt2 (2011). The editors suggest the following Related Resources on Science sites:In Science Signaling
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Science Signaling. ISSN 1937-9145 (online), 1945-0877 (print). Pre-2008: Science's STKE. ISSN 1525-8882