WB-Western Blot IP-Immunoprecipitation IHC-Immunohistochemistry IF-Immunofluorescence ICC-Immunocytochemistry FC-Flow Cytometry

Zyxin is a low abundance phosphoprotein primarily localized to focal adhesion plaques, where Zyxin plays a crucial role in regulating cellular adhesion and signaling processes. Zyxin′s structure includes multiple proline-rich sequences and three LIM domains, which are zinc finger domains that facilitate protein-protein interactions. These structural features are essential for Zyxin′s function, enabling interactions with various proteins at cell adhesion sites, including members of the cysteine-rich protein LIM domain-containing family. Notably, Zyxin′s proline-rich domain associates with the SH3 domain of p95 Vav, while showing no interaction with similar SH3 domains found in proteins like GRB2 or PLCg. Additionally, Zyxin interacts with the focal adhesion protein VASP, potentially aiding in VASP localization to focal adhesions and regions of high dynamic activity within the cell.