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Sci. Signal., 8 September 2009
Vol. 2, Issue 87, p. ra51
[DOI: 10.1126/scisignal.2000396]

RESEARCH ARTICLES

Editor's Summary

Integrin Interactors
Integrins mediate cell-cell adhesion, as well as cell adhesion to the extracellular matrix. Identification of the intracellular signaling networks associated with integrins is of interest because integrins are involved in processes such as invasion of tumor cells during metastasis and leukocyte infiltration during inflammation. Humphries et al. developed a method of isolating protein complexes associated with {alpha}5β1 integrin, which binds to fibronectin, and with {alpha}4β1 integrin, which binds to vascular cell adhesion molecule–1. Although a subset of proteins was detected in both the {alpha}5β1 and {alpha}4β1 networks, there were several receptor-specific proteins. In particular, regulator of chromosome condensation–2 (RCC2) was identified as a component of the {alpha}5β1 integrin–associated signaling network. RCC2 promoted fibronectin-dependent migration by inhibiting two different subnetworks (Rac1 and Arf6). These techniques provide the means to investigate the composition and function of adhesion complexes under different physiological conditions.

Citation: J. D. Humphries, A. Byron, M. D. Bass, S. E. Craig, J. W. Pinney, D. Knight, M. J. Humphries, Proteomic Analysis of Integrin-Associated Complexes Identifies RCC2 as a Dual Regulator of Rac1 and Arf6. Sci. Signal. 2, ra51 (2009).

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