{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nNeuropilin‐1 (NRP1) is a multifunctional transmembrane receptor expressed by diverse cell types—including endothelial, neuronal, immune, and tumor cells—that binds an array of ligands, such as vascular endothelial growth factor (VEGF) isoforms, class 3 semaphorins, Galectin‑1, tuftsin, and C‑end rule (CendR) peptides. Structural and biochemical studies have delineated key features of its extracellular b1 domain, the importance of its C‑terminal binding motifs, and the impact of post‐translational modifications (e.g. glycosylation) on its ligand affinity. Such interactions enable NRP1 to serve as a co‐receptor with other tyrosine kinase receptors (like VEGFR2) and integrins, thereby modulating cell adhesion, migration, vascular permeability, and angiogenic signaling."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "11"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its roles in vascular and neural development, NRP1 critically influences immune cell interactions. It facilitates contacts between dendritic cells and resting T cells and is dynamically regulated during thymocyte differentiation—although in humans its expression does not uniquely mark regulatory T cells."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "12"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nRecent studies have unveiled a pivotal function for NRP1 in mediating viral entry. By directly binding specific proteolytically generated motifs—such as those revealed in the furin‐processed spike protein of SARS‑CoV‑2—it potentiates virus infectivity. Similar interactions have been described for the envelope proteins of human T‑cell lymphotropic virus type‑1 (HTLV‑1) and Epstein–Barr virus (EBV), underscoring NRP1 as an emerging host factor in pathogen entry."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "14", "end_ref": "18"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn the tumor microenvironment, NRP1 is a key regulator of cancer progression and angiogenesis across a variety of malignancies—including glioblastoma, medulloblastoma, colorectal, breast, and pancreatic cancers. Tumor‐derived NRP1 can potentiate pro‐survival, migratory, and invasive signaling pathways by partnering with receptors for VEGF, placental growth factor (PlGF), hepatocyte growth factor (HGF/c‑Met), transforming growth factor‑β (TGF‑β), and platelet‑derived growth factor (PDGF). Moreover, its expression and activity are modulated by microRNAs (for example, miR‑320a) and post‑translational modifications, which further impact epithelial–mesenchymal transition, chemoresistance, and neovascularization."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "19", "end_ref": "33"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn addition to serving as a ligand‐binding hub, NRP1 regulates receptor complex assembly and intracellular trafficking. It orchestrates VEGFR2 recycling via Rab GTPase–dependent pathways and mediates a distinct, macropinocytosis‐like endocytic route for CendR peptides—processes that fine‑tune VEGF signaling and endothelial permeability. Its partnership with integrins, PDGF receptors, and EBV glycoproteins further illustrates its versatile role in modulating cellular responses."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "34", "end_ref": "39"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nTherapeutic strategies targeting NRP1—via specific peptide antagonists that mimic critical C‑terminal sequences or compete with natural ligands—have shown promise in disrupting its pro‑angiogenic, pro‑tumorigenic, and viral entry functions, thereby providing novel avenues for intervention in cancer, infectious diseases, and aberrant angiogenesis."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "40"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Rafaèle Tordjman, Yves Lepelletier, Valérie Lemarchandel, et al. 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