The ability of a cell to migrate in response to a stimulus is dependent on constant reorganization of the actin cytoskeleton. The dynamic assembly and disassembly of the cytoskeleton is essential for normal growth, development and repair of an organism. The remodelling of actin filaments is guided by several factors, of which the Rho-family of small GTPases is central. VAV2 is a guanine nucleotide exchange factor (GEF) for the Rho family GTPases, specifically for Rac1 (Marignani and Carpenter, J Cell Biology 2001) and is one of three VAV-family members. Vav2 is a modular protein since it contains numerous signalling domains, suggesting that the function of Vav2 is not limited to GEF activity (Arora et al, Am J Physiol Cell Physiol 2008).

We recently identified novel binding partners for VAV2 by gel-free mass spectrometry. Our goal is to characterize these new interacting partners in an effort to better understand how VAV2 is involved in cytoskeletal reorganization that leads to cell migration.