{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nZyxin is emerging as a central mechanosensor that orchestrates cytoskeletal dynamics and focal adhesion (FA) remodeling in response to both externally‐applied and internally‐generated forces. In fibroblasts and endothelial as well as vascular smooth muscle cells, mechanical stimulation (either by cell stretch, contractility inhibition, or integrin engagement) triggers zyxin recruitment to FAs and related adhesion sites, where it coordinates actin polymerization and stress fiber reorganization. Zyxin’s accumulation at these sites facilitates dynamic protein turnover and stabilizes cell–matrix and cell–cell junctions, as seen in studies where its mechanosensitive recruitment (via its LIM domain) supports force‐dependent actin assembly, modulates FA protein dissociation/rebinding kinetics, and even restricts the size and number of peripheral cell processes during endothelial sprouting. This mechanotransduction function is further underscored by observations in which zyxin redistribution or phosphorylation (by, for example, PKG and CDK1) influences junction remodeling and contractile force recovery under stretch conditions."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "12"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn diverse cancer and developmental contexts, zyxin plays multifaceted roles by modulating key signal transduction pathways that regulate cell proliferation, migration, differentiation, and survival. In some tumor models (e.g. Ewing sarcoma), reduced zyxin expression correlates with disrupted stress fiber formation and increased tumor cell motility, suggesting a tumor‐suppressive function; conversely, in colon, lung, glioblastoma and oral cancers, zyxin contributes to oncogenic processes by interacting with partners such as endoglin, LIM–nebulette, ZNF384, PTOV1, and by influencing pathways including HIPK2–p53, TGF‑β–mediated EMT, retinoic acid signaling and CDK8/YAP activation. Zyxin also modulates key developmental signaling cascades such as Hedgehog, via its interaction with Patched receptors, thereby impacting central nervous system patterning. Collectively, these studies identify zyxin as a versatile adaptor whose altered expression or regulation can either promote or restrain cancer cell invasiveness and developmental patterning."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "13", "end_ref": "30"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nMoreover, zyxin exerts critical functions in specialized physiological and immunological processes. In endothelial cells, zyxin regulates exocytosis events—such as the release of von Willebrand factor—and participates in thrombin-induced signaling via binding to PAR‑1, thereby influencing cytoskeletal remodeling and barrier recovery. In innate immunity, zyxin serves as a scaffold facilitating interactions between viral RNA sensors and adaptor molecules, and in cell–cell adhesion it docks via nectin interactions. Its regulatory roles extend to platelet biogenesis, where zyxin governs actin organization and the surface expression of key glycoproteins during proplatelet formation, as well as to podocyte maintenance where its upregulation upon stretch preserves actin integrity. In addition, proteolytic processing of zyxin generates fragments with anti-apoptotic properties that may contribute to wound repair, and altered zyxin expression has been implicated in aging-related conditions such as osteoporosis. These findings highlight zyxin’s broad spectrum of functions that underpin cellular adaptation to mechanical stress and contribute to tissue homeostasis."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "31", "end_ref": "39"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Hiroaki Hirata, Hitoshi Tatsumi, Masahiro Sokabe "}, {"type": "b", "children": [{"type": "t", "text": "Mechanical forces facilitate actin polymerization at focal adhesions in a zyxin-dependent manner."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Cell Sci (2008)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1242/jcs.030320"}], "href": "https://doi.org/10.1242/jcs.030320"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "18682496"}], "href": "https://pubmed.ncbi.nlm.nih.gov/18682496"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Haguy Wolfenson, Alexander Bershadsky, Yoav I Henis, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Actomyosin-generated tension controls the molecular kinetics of focal adhesions."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Cell Sci (2011)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1242/jcs.077388"}], "href": "https://doi.org/10.1242/jcs.077388"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "21486952"}], "href": "https://pubmed.ncbi.nlm.nih.gov/21486952"}]}, {"type": "r", "ref": 3, "children": [{"type": "t", "text": "Arisa Uemura, Thuc-Nghi Nguyen, Amanda N Steele, et al. "}, {"type": "b", "children": [{"type": "t", "text": "The LIM domain of zyxin is sufficient for force-induced accumulation of zyxin during cell migration."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Biophys J (2011)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.bpj.2011.08.001"}], "href": "https://doi.org/10.1016/j.bpj.2011.08.001"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "21889443"}], "href": "https://pubmed.ncbi.nlm.nih.gov/21889443"}]}, {"type": "r", "ref": 4, "children": [{"type": "t", "text": "Stephanie I Fraley, Yunfeng Feng, Anjil Giri, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Dimensional and temporal controls of three-dimensional cell migration by zyxin and binding partners."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Nat Commun (2012)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/ncomms1711"}], "href": "https://doi.org/10.1038/ncomms1711"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "22395610"}], "href": "https://pubmed.ncbi.nlm.nih.gov/22395610"}]}, {"type": "r", "ref": 5, "children": [{"type": "t", "text": "Joppe Oldenburg, Gerard van der Krogt, Floor Twiss, et al. "}, {"type": "b", "children": [{"type": "t", "text": "VASP, zyxin and TES are tension-dependent members of Focal Adherens Junctions independent of the α-catenin-vinculin module."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Sci Rep (2015)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/srep17225"}], "href": "https://doi.org/10.1038/srep17225"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "26611125"}], "href": "https://pubmed.ncbi.nlm.nih.gov/26611125"}]}, {"type": "r", "ref": 6, "children": [{"type": "t", "text": "Sahana Suresh Babu, Agnieszka Wojtowicz, Marc Freichel, et al. 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"}, {"type": "b", "children": [{"type": "t", "text": "The actin cytoskeleton-associated protein zyxin acts as a tumor suppressor in Ewing tumor cells."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Exp Cell Res (2005)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.yexcr.2004.10.035"}], "href": "https://doi.org/10.1016/j.yexcr.2004.10.035"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "15748890"}], "href": "https://pubmed.ncbi.nlm.nih.gov/15748890"}]}, {"type": "r", "ref": 16, "children": [{"type": "t", "text": "Hilde Janssen, Peter Marynen "}, {"type": "b", "children": [{"type": "t", "text": "Interaction partners for human ZNF384/CIZ/NMP4--zyxin as a mediator for p130CAS signaling?"}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Exp Cell Res (2006)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.yexcr.2006.02.001"}], "href": "https://doi.org/10.1016/j.yexcr.2006.02.001"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "16510139"}], "href": "https://pubmed.ncbi.nlm.nih.gov/16510139"}]}, {"type": "r", "ref": 17, "children": [{"type": "t", "text": "Johanna Crone, Carolina Glas, Kathrin Schultheiss, et al. 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"}, {"type": "b", "children": [{"type": "t", "text": "MicroRNA-16 targets zyxin and promotes cell motility in human laryngeal carcinoma cell line HEp-2."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "IUBMB Life (2011)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1002/iub.417"}], "href": "https://doi.org/10.1002/iub.417"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "21360639"}], "href": "https://pubmed.ncbi.nlm.nih.gov/21360639"}]}, {"type": "r", "ref": 19, "children": [{"type": "t", "text": "Hye-Sung Moon, Sharona Even-Ram, Hynda K Kleinman, et al. 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"}, {"type": "b", "children": [{"type": "t", "text": "Synemin interacts with the LIM domain protein zyxin and is essential for cell adhesion and migration."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Exp Cell Res (2010)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.yexcr.2009.10.015"}], "href": "https://doi.org/10.1016/j.yexcr.2009.10.015"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "19853601"}], "href": "https://pubmed.ncbi.nlm.nih.gov/19853601"}]}, {"type": "r", "ref": 21, "children": [{"type": "t", "text": "Nikica Mise, Rajkumar Savai, Haiying Yu, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Zyxin is a transforming growth factor-β (TGF-β)/Smad3 target gene that regulates lung cancer cell motility via integrin α5β1."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2012)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M112.357624"}], "href": "https://doi.org/10.1074/jbc.M112.357624"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "22778267"}], "href": "https://pubmed.ncbi.nlm.nih.gov/22778267"}]}, {"type": "r", "ref": 22, "children": [{"type": "t", "text": "Jiuli Zhou, Yongji Zeng, Lian Cui, et al. 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