{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nRadixin (RDX) is a core member of the ezrin–radixin–moesin (ERM) family that links the actin cytoskeleton to the plasma membrane, thereby contributing to the organization and stabilization of specialized cell surface domains. In neurons, RDX participates in structuring filopodia and regulating neurite outgrowth through modulation of ERM phosphorylation, while in several immune cell types it helps organize microvillar platforms that concentrate receptors (such as T‑cell receptor and L‐selectin) and associated signaling molecules, ultimately shaping cell adhesion, migration, and survival. In polarized epithelial cells (for example, hepatocytes or intestinal cells), RDX is critical for the apical localization of transmembrane transporters, ensuring efficient barrier and secretory functions."}, {"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 disease contexts, changes in RDX expression, localization, and post‐translational modifications have been linked to pathological processes. In cancer, for example, RDX functions as a pro‐metastatic factor in gastric, pancreatic, and glioblastoma cells—with microRNAs such as miR‑409‑3p and miR‑196a/196b directly targeting its mRNA to suppress invasion and metastasis. Similarly, human genetic studies have associated mutant or null RDX alleles with sensorineural hearing loss, while in liver diseases its altered expression has been implicated in perturbed transporter localization and cholestasis. Furthermore, RDX and other ERM family proteins participate in the organization of signaling complexes that govern endothelial barrier properties and contribute to multidrug resistance when associated with membrane transporters."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "11", "end_ref": "30"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nAt the signaling and regulatory level, RDX is dynamically controlled through phosphorylation and interaction with numerous kinases, phosphatases, and adaptor molecules. Its phosphorylation status is modulated by upstream effectors—including Rho‐kinase, protein kinase C isoforms, and sphingolipid‐mediated pathways—and such modifications dictate its association with partner proteins that regulate cAMP microdomains, non‑amyloidogenic processing of the amyloid precursor protein, and even host–pathogen interactions during bacterial and viral infections. In natural killer cells and other leukocytes, for instance, tetraspanin‐induced phosphorylation of RDX contributes to cell polarization and efficient cellular trafficking. Together, these findings reveal that RDX functions not merely as a static linker but as a versatile molecular scaffold integrating mechanical cues with biochemical signals to regulate cell polarity, adhesion, transporter localization, and signal transduction across a wide spectrum of physiological and pathophysiological states."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "31", "end_ref": "42"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Hideyuki Kojima, Anne T Nies, Jörg König, et al. 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