{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nNucleophosmin 1 (NPM1) is a highly conserved, multifunctional nucleolar phosphoprotein that shuttles continuously between the nucleus and cytoplasm. In its normal state, NPM1 plays pivotal roles in ribosome biogenesis, chaperoning ribonucleoprotein complexes, regulating chromatin structure, and mediating the proper folding and assembly of ribosomal proteins. It also contributes to the regulation of cell growth and stress responses through modulation of the ARF–p53 tumor‐suppressor pathway, with its oligomerization and liquid–liquid phase separation properties helping to organize the nucleolar structure and control rRNA transcription. Post‐translational modifications, such as phosphorylation and desumoylation, further fine‐tune these functions by dynamically altering its conformation and interactions."}, {"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": "\nClinically, mutations of NPM1 are among the most common genetic alterations in acute myeloid leukemia (AML), especially in cases with a normal karyotype. These mutations typically alter the C-terminal domain to generate a novel nuclear export signal, resulting in the aberrant cytoplasmic dislocation of the mutant protein (often referred to as NPM1c+) and a distinct gene expression profile that includes deregulation of HOX genes. As such, mutant NPM1 not only acts as a founding lesion in leukemogenesis but also serves as a valuable biomarker for risk stratification, minimal residual disease monitoring, and therapeutic decision making in both adult and pediatric AML. In addition, in some hematologic malignancies NPM1 functions as a fusion partner (e.g., in NPM–ALK), further underscoring its diverse oncogenic mechanisms."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "11", "end_ref": "28"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its nucleolar and oncogenic roles, NPM1 is crucial for the maintenance of proper cellular architecture through regulation of centrosome duplication and genomic stability. Its tightly controlled nucleocytoplasmic trafficking—mediated by functional nuclear export signals and modulated by specific protein–protein interactions—ensures that NPM1 is localized to the appropriate subcellular compartments for ribosome assembly and efficient RNA processing. This multifaceted regulation highlights the importance of NPM1 in both normal cellular homeostasis and in the pathological context of malignant transformation."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "29", "end_ref": "31"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Emanuela Colombo, Jean-Christophe Marine, Davide Danovi, et al. 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