PresentationCell Biology

Proteomic Analysis of Integrin Adhesion Complexes

Sci. Signal.  05 Apr 2011:
Vol. 4, Issue 167, pp. pt2
DOI: 10.1126/scisignal.2001827

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A presentation from the 6th British Society for Proteome Research (BSPR)–European Bioinformatics Institute (EBI) Meeting “Multiscale Proteomics: From Cells to Organisms” at the Wellcome Trust Conference Centre, Cambridge, UK, 14 to 16 July 2009. The Presentation also complements the Science Signaling Research Article by Humphries et al. published 8 September 2009.


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.

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