{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nRPSA, also known as the 37/67‐kDa laminin receptor, is a multifunctional protein whose roles span both “housekeeping” and specialized cell‐surface functions. In its canonical capacity as a ribosomal protein, RPSA is a component of the 40S subunit, contributing to ribosome assembly, protein synthesis, and even nuclear processes, while its eukaryote‐specific C‑terminal region is crucial for promoting cell viability and proper organ development (for example, spleen formation). In addition, the same polypeptide serves as the precursor to its mature cell‑surface form that binds laminin, thereby mediating cell adhesion and extracellular matrix interactions essential for tissue architecture and homeostasis."}, {"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": "\nIn addition to its fundamental cellular roles, RPSA operates as a versatile cell‐surface receptor that is exploited by various pathogens and bioactive ligands. For instance, it mediates efficient transduction by certain adeno‐associated viruses and serves as a key entry port during Escherichia coli K1 invasion, illustrating its importance in infection biology. Moreover, natural ligands such as the green tea polyphenol (–)-epigallocatechin‑3‑gallate (EGCG) and pigment epithelium–derived factor (PEDF) engage RPSA to trigger anticancer and anti‑angiogenic signaling. The receptor also functions in microbial pathogenesis by binding adhesin proteins (for example, Tp0751 from Treponema pallidum), highlighting its broad role in mediating host–pathogen interactions."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "10", "end_ref": "16"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nRPSA also plays a pivotal role in oncogenesis and cancer progression. Its up‑regulation in a wide range of tumors—including gastric, pancreatic, bile duct, colon, lung, melanoma, and glioma—is frequently associated with enhanced cell adhesion, invasion, metastasis, and resistance to chemotherapeutic agents. RPSA fosters these processes by interacting with other surface molecules (for example, integrin α6) and by modulating key intracellular pathways such as PI3K/AKT, MAPK/ERK, and PP2A‐mediated signaling, ultimately promoting cell survival and impeding apoptosis. This multifunctionality has spurred interest in targeting RPSA using RNA interference, monoclonal antibodies, or small‐molecule inhibitors to overcome drug resistance and to suppress metastatic spread. Notably, its involvement extends even to the regulation of telomerase activity and contributes to the internalization of neurotoxic amyloid‑β species implicated in Alzheimer’s disease—all underscoring the receptor’s wide-ranging pathophysiological impact."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "17", "end_ref": "40"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Alexandre Bolze, Nizar Mahlaoui, Minji Byun, et al. 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