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Nucleophosmin (NPM1) was identified as a binding partner of DDX27 which increased NPM1 protein nuclear translocation. Its knockdown abrogated DDX27-mediated NF-kappaB signaling and colorectal cancer cell growth.
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The NPM1 gene was the most frequently mutated gene in both white blood cells and cell-free DNA in healthy individuals.
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NPM1 protein could promote more cells to enter S phase
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A novel NPM1-interacting motif occurs in the C-terminal region of p14arf, which corresponds to its predicted nucleolar localization signal. This motif recognizes a specific region of the NPM1 N-terminal domain and, upon binding, the 2 proteins form soluble high molecular weight complexes.
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NPM1 and SURF6 form heterotypic liquid-like droplets in the nucleolus.
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High NPM1 expression is associated with tongue neoplasms.
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his meta-analysis indicated that NPM may act as a valuable prognosis biomarker and a potential therapeutic target in human solid tumors.
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this paper shows that viral nucleocapsid interacts with NPM1 and protects it from proteolytic cleavage, enhancing Cell survival, and is involved in porcine epidemic diarrhea virus growth
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DNMT3A R882 mutation plays an important role in CN-AML patients' prognosis and clinical outcomes in the presence and absence of NPM1 and FLT3 mutations.
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Mutation in NPM1 gene is associated with Acute Myeloid Leukemia.
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Nucleoplasmic translocation of NPM1 is a prerequisite for stress-induced activation of p53.
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NPM1 gene B type mutation enhanced the proliferation and invasion of THP-1 AML cells through the regulation of TIMP-2, MMP-2, Ang-1, c-myc and CCND1
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In this study, FLT3 and NPM1 mutations were evaluated in adult Iranian patients with de novo cytogenetically normal acute myeloid leukemia and its correlations with clinical and laboratory parameters were also assessed.
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These observations demonstrated that the expression and localization of NPM affected the homeostatic balance of oxidative stress in tumor cells via PRDX6 protein. The regulation axis of NPM/PRDX/ROS may provide a novel therapeutic target for cancer treatment.
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In the Title.
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ese results enhance our understanding of the molecular mechanisms that govern nucleoli formation by demonstrating that PPM1D regulates nucleolar formation by regulating NPM phosphorylation status through a novel signalling pathway, PPM1D-CDC25C-CDK1-PLK1
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Data suggest that the direct interaction of several regions of nucleophosmin 1 (NPM1) C-terminal domain (CTD) with cellular membranes could be implicated in diseases where NPM1 is mutated and/or where its overexpression is cytoxic.
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Mechanically, mutant NPM1 interacted with PML and mediated its delocalization as well as stabilization contributing to elevated autophagic activity and leukemic cell survival in vitro.
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Mutation analysis in NPM1 in acute myeloid leukemia.
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We conclude that the degradation of NPM1 and HEXIM1 through autophagy in certain AML subsets contributes to the activation of the BET pathway in these cells.
