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Zyxin is an evolutionarily conserved LIM domain protein encoded by the ZYX gene and functions as an adapter protein at focal adhesions and along actin filaments[1][2][4]. It plays a key role in signal transduction, linking mechanical or extracellular stimuli to changes in the cytoskeleton and gene expression. Zyxin is composed of an N-terminal proline-rich region and three C-terminal LIM domains, facilitating numerous protein-protein interactions and enabling movement between the cytoplasm and nucleus[1][2]. Its primary biological functions include regulation of actin dynamics, cell adhesion, migration, and the transmission of mechanical signals from the cellular environment into intracellular responses. Zyxin interacts with key cytoskeletal and signaling proteins (such as alpha-actinin, ENAH, LASP1, LATS1, and VASP), modulating processes central to cell structure and communication[1][2][4]. Aberrant zyxin function or expression is implicated in cancer development and progression, cardiovascular pathologies, and inflammatory responses[1]. No approved drugs directly target zyxin; its modulation is primarily a subject of basic cellular and mechanobiology research[2][4].
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