Paxillin (PXN)

Paxillin is a multifunctional cytoskeletal adaptor protein encoded by the PXN gene, primarily localized to focal adhesions in non-muscle cells and costameres in striated muscle cells[1][2]. Its structure includes N-terminal LD motifs (facilitating protein-protein interactions with kinases, structural proteins, and SH2/SH3 domain proteins) and C-terminal LIM domains (zinc-finger structures mediating localization and additional interactions)[1][3][4]. Paxillin acts as a signaling hub coordinating integrin-mediated cell adhesion, actin cytoskeleton organization, and motility by assembling and regulating diverse signaling protein complexes. Abnormal PXN expression, mutations, or post-translational modifications are implicated in the pathogenesis of several cancers, including lung, colorectal, prostate, and breast cancers, where paxillin supports oncogenic signaling, tumor cell migration, invasion, and resistance to chemotherapeutics[2][3]. PXN also plays vital roles in inflammatory responses, cardiac muscle structure, and non-tumorigenic cell migration and adhesion. Despite its functional importance, paxillin is not directly targeted by current therapeutics but remains a key signaling intermediate in drug-resistance and metastatic pathways, making it an attractive candidate for therapeutic development and biomarker research[2][3].

Other names

PXNTesticular tissue protein Li 134paxillinPaxillin, testicular tissue protein Li 134

Indirect: Inhibitors of focal adhesion kinase (FAK) or Src can inhibit phosphorylation and downstream signaling through paxillin, affecting cell adhesion and migration[2][3].