{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nTalin‐1 (TLN1) is a large, multidomain cytoskeletal protein that functions as a central adaptor at cell–extracellular matrix adhesions by linking integrins to the actin cytoskeleton. Structural studies have unveiled that its globular head domain engages integrin β‐tails and membranes—often in a phosphatidylinositol‐4,5‐bisphosphate–dependent manner—while its extended rod domains harbor cryptic binding sites for actin and other focal adhesion proteins. These coordinated interactions not only promote integrin clustering and activation but also underlie the rapid and reversible conformational changes that regulate focal adhesion assembly and mechanotransduction."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "9"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its structural role, TLN1 is a dynamic mechanosensor central to the regulation of focal adhesion turnover and cell migration. In various adhesion‐dependent contexts—including the rapid migratory responses of T lymphocytes and other motile cells—TLN1 couples integrin activation to force‐dependent recruitment of binding partners such as vinculin, kindlin, and associated signaling proteins. Through its ability to undergo force‐induced unfolding and to present cryptic binding sites, TLN1 participates in modulating cytoskeletal linkage, actomyosin contractility, and the stabilization of adhesive contacts, thereby contributing to processes as diverse as immune synapse stabilization and adhesion strengthening under fluid shear."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "10", "end_ref": "25"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nTLN1 also plays pivotal roles in cancer progression and metastasis. Elevated or post‐translationally modified TLN1 can enhance integrin‐mediated adhesion, survival, and invasive signaling in tumor cells. For instance, up‐regulation or aberrant phosphorylation of TLN1 is correlated with increased cell migration and resistance to anoikis in prostate and other carcinomas, while TLN1 levels are emerging as potential biomarkers in hepatocellular and nasopharyngeal cancers. Collectively, these studies underscore TLN1’s capacity to orchestrate the integrin–cytoskeletal linkage that drives both tumor cell aggressiveness and chemoresistance."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "26", "end_ref": "33"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn addition to its roles in adhesion and cancer, TLN1 is critical for the mechanical integrity and specialized functions of cardiac and vascular tissues. In cardiomyocytes, isoform switching between TLN1 and TLN2—as well as alterations in TLN1 expression under stress—contribute to costamere organization, force transmission, and, ultimately, cardiac remodeling and function. Moreover, genetic and simulation‐based studies implicate TLN1 in vascular pathologies such as aortic dissection and spontaneous coronary artery dissection, emphasizing its importance in maintaining tissue homeostasis under mechanical load."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "34", "end_ref": "41"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Kun Ling, Renee L Doughman, Ari J Firestone, et al. 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