{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nPaxillin (PXN) is a multifunctional focal‐adhesion adaptor protein that coordinates the assembly and turnover of integrin–based adhesions, thereby regulating cytoskeletal organization and cell migration in diverse physiologic contexts. Its dynamic activity is controlled by site‐specific phosphorylation by kinases such as JNK, ERK and Src that modulate its ability to recruit signaling and structural proteins (e.g., focal adhesion kinase, vinculin, Pyk2) and to regulate processes ranging from neurite extension to invadopodia disassembly and preadipocyte motility. In nontransformed systems, phosphorylation of PXN on specific serine and tyrosine residues has been shown to regulate focal adhesion formation and rapid cell movement, demonstrating its essential role in mechanosensitive adhesion dynamics and actin reorganization."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "10"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn a cancer context, aberrant expression and/or post‐translational modification of PXN is frequently observed and is strongly associated with tumor progression, invasion and chemoresistance. In several malignancies—including lung, colorectal, prostate, breast, and virus‐associated cancers—PXN is upregulated or mutated, often as a consequence of disrupted microRNA or splicing factor regulation, leading to enhanced migratory and invasive phenotypes. Studies have revealed that signaling cascades initiated by receptor tyrosine kinases (such as IGF‐IR, EGFR, and androgen receptor) or by integrin engagement converge on PXN phosphorylation, which in turn promotes focal adhesion remodeling, nuclear translocation and the transcriptional regulation of genes involved in proliferation and survival. Collectively, these findings establish the PXN signaling axis as a critical mediator of oncogenic processes and a potential therapeutic target in solid tumors."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "11", "end_ref": "33"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its roles in adhesion remodeling and cancer cell dissemination, PXN serves as a central hub in integrin‐mediated signal transduction. Direct interactions between PXN and integrin cytoplasmic domains—as well as with other adaptor proteins such as kindlins, 14–3–3, and β–catenin—mediate its participation in diverse signaling networks that control not only focal adhesion dynamics but also microtubule acetylation, Golgi polarization and even inflammasome activation. In addition, regulated proteolysis (e.g. by calpain) and the shuttling of PXN between the cytoplasm and nucleus further extend its impact on transcriptional programs that influence cell proliferation. These integrated mechanisms enable PXN to function as a versatile signal transducer linking extracellular cues to intracellular responses in both normal and pathological contexts."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "34", "end_ref": "40"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "S Liu, M Slepak, M H Ginsberg "}, {"type": "b", "children": [{"type": "t", "text": "Binding of Paxillin to the alpha 9 Integrin Cytoplasmic Domain Inhibits Cell Spreading."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2001)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M105114200"}], "href": "https://doi.org/10.1074/jbc.M105114200"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "11477105"}], "href": "https://pubmed.ncbi.nlm.nih.gov/11477105"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Tracee S Panetti "}, {"type": "b", "children": [{"type": "t", "text": "Tyrosine phosphorylation of paxillin, FAK, and p130CAS: effects on cell spreading and migration."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Front Biosci (2002)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.2741/A771"}], "href": "https://doi.org/10.2741/A771"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "11779709"}], "href": "https://pubmed.ncbi.nlm.nih.gov/11779709"}]}, {"type": "r", "ref": 3, "children": [{"type": "t", "text": "Cai Huang, Zenon Rajfur, Christoph Borchers, et al. 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