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Liprin-alpha-1 (encoded by the PPFIA1 gene) is a cytoplasmic scaffold protein of the liprin family, highly conserved and broadly expressed in human tissues[1][4]. It plays a crucial role in organizing and stabilizing protein complexes at plasma membrane sites that regulate cell adhesion, migration, and focal adhesion turnover, due to its ability to interact with LAR family transmembrane protein tyrosine phosphatases and multiple structural and signaling proteins[1][2][3][4][5]. In the nervous system, liprin-alpha-1 is essential for presynaptic active zone assembly, synaptic vesicle trafficking, and synaptic protein compartmentalization, while outside the nervous system, it modulates integrin dynamics, cell-matrix adhesion, cytoskeletal arrangement (notably the intermediate filament vimentin network), and thus cell proliferation and invasion[3][4][5]. Aberrant amplification or overexpression of PPFIA1 is associated with several cancers, including head and neck, breast, and esophageal carcinomas, affecting tumor cell invasiveness and metastatic behavior[2][3][4]. Despite its central biological importance and disease association, it is not a classical drug target (such as a receptor or enzyme), and no direct small-molecule drugs are known to target it[4][5].
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