- EMDB-15606: CryoEM structure of the human Nucleophosmin 1 core -
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Database: EMDB / ID: EMD-15606
Title
CryoEM structure of the human Nucleophosmin 1 core
Map data
Sample
Complex: Nucleophosmin 1
Protein or peptide: Nucleophosmin
Keywords
Phase separation / CHAPERONE
Function / homology
Function and homology information
regulation of eIF2 alpha phosphorylation by dsRNA / regulation of mRNA stability involved in cellular response to UV / regulation of endoribonuclease activity / negative regulation of centrosome duplication / regulation of endodeoxyribonuclease activity / positive regulation of cell cycle G2/M phase transition / regulation of centriole replication / granular component / TFAP2A acts as a transcriptional repressor during retinoic acid induced cell differentiation / negative regulation of protein kinase activity by regulation of protein phosphorylation ...regulation of eIF2 alpha phosphorylation by dsRNA / regulation of mRNA stability involved in cellular response to UV / regulation of endoribonuclease activity / negative regulation of centrosome duplication / regulation of endodeoxyribonuclease activity / positive regulation of cell cycle G2/M phase transition / regulation of centriole replication / granular component / TFAP2A acts as a transcriptional repressor during retinoic acid induced cell differentiation / negative regulation of protein kinase activity by regulation of protein phosphorylation / SARS-CoV-1-host interactions / regulation of centrosome duplication / Tat protein binding / ALK mutants bind TKIs / spindle pole centrosome / Nuclear import of Rev protein / centrosome cycle / nucleocytoplasmic transport / TP53 regulates transcription of additional cell cycle genes whose exact role in the p53 pathway remain uncertain / protein kinase inhibitor activity / ribosomal large subunit binding / ribosomal small subunit binding / NF-kappaB binding / ribosomal large subunit export from nucleus / Nuclear events stimulated by ALK signaling in cancer / ribosomal small subunit export from nucleus / Deposition of new CENPA-containing nucleosomes at the centromere / core promoter sequence-specific DNA binding / ribosome assembly / SUMOylation of transcription cofactors / ribosomal large subunit biogenesis / positive regulation of translation / protein-DNA complex / intracellular protein transport / PKR-mediated signaling / cellular senescence / cellular response to UV / protein localization / unfolded protein binding / Signaling by ALK fusions and activated point mutants / nucleosome assembly / positive regulation of NF-kappaB transcription factor activity / ribosomal small subunit biogenesis / histone binding / DNA-binding transcription factor binding / transcription coactivator activity / chromatin remodeling / rRNA binding / ribonucleoprotein complex / negative regulation of cell population proliferation / DNA repair / focal adhesion / chromatin binding / centrosome / positive regulation of cell population proliferation / positive regulation of DNA-templated transcription / negative regulation of apoptotic process / nucleolus / protein kinase binding / signal transduction / positive regulation of transcription by RNA polymerase II / protein homodimerization activity / protein-containing complex / RNA binding / nucleoplasm / membrane / nucleus / cytoplasm / cytosol Similarity search - Function
Journal: PNAS Nexus / Year: 2023 Title: A "grappling hook" interaction connects self-assembly and chaperone activity of Nucleophosmin 1. Authors: Mihkel Saluri / Axel Leppert / Genis Valentin Gese / Cagla Sahin / Dilraj Lama / Margit Kaldmäe / Gefei Chen / Arne Elofsson / Timothy M Allison / Marie Arsenian-Henriksson / Jan Johansson ...Authors: Mihkel Saluri / Axel Leppert / Genis Valentin Gese / Cagla Sahin / Dilraj Lama / Margit Kaldmäe / Gefei Chen / Arne Elofsson / Timothy M Allison / Marie Arsenian-Henriksson / Jan Johansson / David P Lane / B Martin Hällberg / Michael Landreh / Abstract: How the self-assembly of partially disordered proteins generates functional compartments in the cytoplasm and particularly in the nucleus is poorly understood. Nucleophosmin 1 (NPM1) is an abundant ...How the self-assembly of partially disordered proteins generates functional compartments in the cytoplasm and particularly in the nucleus is poorly understood. Nucleophosmin 1 (NPM1) is an abundant nucleolar protein that forms large oligomers and undergoes liquid-liquid phase separation by binding RNA or ribosomal proteins. It provides the scaffold for ribosome assembly but also prevents protein aggregation as part of the cellular stress response. Here, we use aggregation assays and native mass spectrometry (MS) to examine the relationship between the self-assembly and chaperone activity of NPM1. We find that oligomerization of full-length NPM1 modulates its ability to retard amyloid formation in vitro. Machine learning-based structure prediction and cryo-electron microscopy reveal fuzzy interactions between the acidic disordered region and the C-terminal nucleotide-binding domain, which cross-link NPM1 pentamers into partially disordered oligomers. The addition of basic peptides results in a tighter association within the oligomers, reducing their capacity to prevent amyloid formation. Together, our findings show that NPM1 uses a "grappling hook" mechanism to form a network-like structure that traps aggregation-prone proteins. Nucleolar proteins and RNAs simultaneously modulate the association strength and chaperone activity, suggesting a mechanism by which nucleolar composition regulates the chaperone activity of NPM1.
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