Research ArticleCell Biology

Proteomic Analysis of Integrin-Associated Complexes Identifies RCC2 as a Dual Regulator of Rac1 and Arf6

Sci. Signal.  08 Sep 2009:
Vol. 2, Issue 87, pp. ra51
DOI: 10.1126/scisignal.2000396

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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 α5β1 integrin, which binds to fibronectin, and with α4β1 integrin, which binds to vascular cell adhesion molecule–1. Although a subset of proteins was detected in both the α5β1 and α4β1 networks, there were several receptor-specific proteins. In particular, regulator of chromosome condensation–2 (RCC2) was identified as a component of the α5β1 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.

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