| First Author | Falini B | Year | 2025 |
| Journal | Leukemia | Volume | 39 |
| Issue | 2 | Pages | 276-290 |
| PubMed ID | 39690184 | Mgi Jnum | J:361611 |
| Mgi Id | MGI:7861330 | Doi | 10.1038/s41375-024-02476-4 |
| Citation | Falini B, et al. (2025) Functions of the native NPM1 protein and its leukemic mutant. Leukemia 39(2):276-290 |
| abstractText | The nucleophosmin (NPM1) gene encodes for the most abundant nucleolar protein. Thanks to its property to act as histone chaperone and to shuttle between the nucleus and cytoplasm, the NPM1 protein is involved in multiple cellular function that are here extensively reviewed and include the formation of the nucleolus through liquid-liquid phase separation, regulation of ribosome biogenesis and transport, control of DNA repair and centrosome duplication as well as response to nucleolar stress. NPM1 is mutated in about 30-35% of adult acute myeloid leukemia (AML). Due to its unique biological and clinical features, NPM1-mutated AML is regarded as a distinct leukemia entity in the WHO 5th edition and ICC classifications of myeloid malignancies. The NPM1 mutant undergoes changes at the C-terminus of the protein that leads to its delocalization in the cytoplasm of the leukemic cells. Here, we focus also on its biological functions discussing the murine models of NPM1 mutations and the various mechanisms that occur at cytoplasmic and nuclear levels to promote and maintain NPM1-mutated AML. |
