ArticleNucleic acids research2014
Intrinsically disordered regions of nucleophosmin/B23 regulate its RNA binding activity through their inter- and intra-molecular association.
Article in Nucleic acids research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 60 citations in OpenAlex.
- Nucleophosmin 1 inhibits the replication of influenza A virus by competitively binding viral RNA with viral proteins.Virologica Sinica · 2025Article
- Nuclear reorganization by NPM1-mediated phase separation triggered by adenovirus core protein VII.Microbiology spectrum · 2024Article
- Could Targeting NPM1c+ Misfolding Be a Promising Strategy for Combating Acute Myeloid Leukemia?International journal of molecular sciences · 2024Review
- Advances in the structure and function of the nucleolar protein fibrillarin.Frontiers in cell and developmental biology · 2024Review
- Nucleophosmin Plays a Role in Repairing DNA Damage and Is a Target for Cancer Treatment.Cancer research · 2023Review
- Targeting and Monitoring Acute Myeloid Leukaemia with Nucleophosmin-1 (International journal of molecular sciences · 2023Review
- A "grappling hook" interaction connects self-assembly and chaperone activity of Nucleophosmin 1.PNAS nexus · 2023Article
- ERK signaling controls productive HIF-1 binding to chromatin and cancer cell adaptation to hypoxia through HIF-1α interaction with NPM1.Molecular oncology · 2021Article
- A KRAS-responsive long non-coding RNA controls microRNA processing.Nature communications · 2021Article
- USP15 Deubiquitinates TUT1 Associated with RNA Metabolism and Maintains Cerebellar Homeostasis.Molecular and cellular biology · 2020Article
- Nucleophosmin in Its Interaction with Ligands.International journal of molecular sciences · 2020Review
- Dipeptide repeat proteins inhibit homology-directed DNA double strand break repair in C9ORF72 ALS/FTD.Molecular neurodegeneration · 2020Article
- Germline NPM1 mutations lead to altered rRNA 2'-O-methylation and cause dyskeratosis congenita.Nature genetics · 2019Article
- C9orf72 Poly(PR) Dipeptide Repeats Disturb Biomolecular Phase Separation and Disrupt Nucleolar Function.Molecular cell · 2019Article
- Phosphoproteome Profiling Reveals Multifunctional Protein NPM1 as part of the Irradiation Response of Tumor Cells.Translational oncology · 2019Article
- NPM1 alternative transcripts are upregulated in acute myeloid and lymphoblastic leukemia and their expression level affects patient outcome.Journal of translational medicine · 2018Article
- Analysis of the oligomeric states of nucleophosmin using size exclusion chromatography.Scientific reports · 2018Article
- Self-interaction of NPM1 modulates multiple mechanisms of liquid-liquid phase separation.Nature communications · 2018Article
- Dynamic intramolecular regulation of the histone chaperone nucleoplasmin controls histone binding and release.Nature communications · 2017Article
- Fly Fishing for Histones: Catch and Release by Histone Chaperone Intrinsically Disordered Regions and Acidic Stretches.Journal of molecular biology · 2017Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Nucleophosmin (NPM1/B23) is a nucleolar protein implicated in growth-associated functions, in which the RNA binding activity of B23 plays essential roles in ribosome biogenesis. The C-terminal globular domain (CTD) of B23 has been believed to be the RNA binding domain because the splicing variant B23.2 lacking the CTD binds considerably less efficiently to RNA. However, the recognition of target RNAs by B23 remains poorly understood. Herein, we report a novel mechanism by which B23 recognizes specific RNA targets. We observed that the nucleolar retention of B23.3 lacking the basic region of B23.1 was lower than that of B23.1 because of its low RNA binding activity. Circular dichroism measurements indicated that the basic region and adjacent acidic regions of B23 are intrinsically disordered regions (IDRs). Biochemical analyses revealed that the basic IDR alone strongly binds to RNA with low specificity. The excessive RNA binding activity of the basic IDR was restrained by intra-molecular interaction with the acidic IDR of B23. Chemical cross-linking experiments and fluorescent labeling of bipartite tetracysteine-tagged proteins suggested that the inter- and intra-molecular interactions between the two IDRs contribute to the regulation of the RNA binding activity of CTD to control the cellular localization and functions of B23.
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