{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nRPS19 is a highly conserved component of the small (40S) ribosomal subunit that plays an essential role in ribosome biogenesis. Multiple studies have shown that RPS19 is required for the proper processing and maturation of 18S ribosomal RNA, a critical step in assembling a functional 40S subunit. Deficiency of RPS19—whether through haploinsufficiency, large gene deletions, or missense mutations—leads to impaired pre‐rRNA processing, aberrant accumulation of immature pre‑40S particles, and nucleolar stress. Such defects disrupt protein synthesis and trigger activation of cell cycle inhibitors (for example, p53 and p21) and apoptotic cascades that selectively affect rapidly proliferating erythroid progenitors, thereby contributing to the pathogenesis of Diamond–Blackfan anemia (DBA). Genetic studies in both yeast and human hematopoietic cells—as well as analysis of patient samples—have confirmed that RPS19 mutations, including both loss‐of‐function and dominant negative alterations, impair ribosome assembly and reduce erythroid colony formation and maturation."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "26"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its canonical function in ribosome assembly, emerging evidence indicates that RPS19 is also intimately involved in regulating the translational machinery and the cellular response to ribosomal stress. Detailed biochemical and structural studies have demonstrated that altered levels of RPS19 not only impair rRNA synthesis and subunit formation but also affect downstream translational control. In experimental gene therapy models correcting RPS19 insufficiency, restoration of RPS19 expression re-establishes normal proliferative capacity in hematopoietic progenitors. Furthermore, analyses of ribosomal profiles and cryo-electron microscopy underscore a coordinated link between RPS19 levels, ribosome integrity, and cellular growth programs."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "27", "end_ref": "30"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn addition to its critical intracellular roles, RPS19 has been found to possess extraribosomal functions that impact immune regulation and cell–cell communication. Under certain pathological conditions, RPS19 can be released extracellularly from apoptotic or stressed cells and, in its dimerized form, acts as a modulator of chemotactic responses by binding to receptors such as CD74, CXCR2, or the complement C5a receptor. This interaction can alter cytokine production, suppress inflammatory responses, and even influence tumor microenvironments by promoting an immunosuppressive milieu. Moreover, viral proteins (e.g. from hantaviruses) have been shown to hijack the RPS19 interaction network to preferentially enhance translation of viral transcripts. Collectively, these extraribosomal actions of RPS19 expand its functional repertoire beyond protein synthesis, highlighting its potential as a therapeutic target in inflammatory disorders, cancers, and viral infections."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "31", "end_ref": "40"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Johan Flygare, Thomas Kiefer, Koichi Miyake, et al. 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"}, {"type": "b", "children": [{"type": "t", "text": "An RNA interference model of RPS19 deficiency in Diamond-Blackfan anemia recapitulates defective hematopoiesis and rescue by dexamethasone: identification of dexamethasone-responsive genes by microarray."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Blood (2005)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1182/blood-2004-08-3313"}], "href": "https://doi.org/10.1182/blood-2004-08-3313"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "15755903"}], "href": "https://pubmed.ncbi.nlm.nih.gov/15755903"}]}, {"type": "r", "ref": 3, "children": [{"type": "t", "text": "Isabelle Léger-Silvestre, Jacqueline Marie Caffrey, Rosy Dawaliby, et al. 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