Zyxin is a low abundance phosphoprotein localized to focal adhesion plaques and is thought to perform regulatory functions at these regions. The protein contains a number of proline-rich sequences as well as three LIM domains, zinc finger domains involved in protein binding. Zyxin interacts with several other proteins at cell adhesion sites, including members of the CRP (cysteine-rich protein) LIM domain containing protein family. The proline-rich domain of Zyxin associates with an SH3 domain of p95 Vav, but not with similar SH3 domains containing proteins such as GRB2 or PLCg. Zyxin has also been shown to interact with the focal adhesion protein VASP and may assist in the targeting of VASP to focal adhesions, microfilaments and membrane regions of high dynamic activity. Zyxin may contribute to the organization of the Actin cytoskeleton in mammalian cells.