ArticleNucleic acids research2022
CryoEM of RUVBL1-RUVBL2-ZNHIT2, a complex that interacts with pre-mRNA-processing-splicing factor 8.
Article in Nucleic acids research, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 21 citations in OpenAlex.
- Nanoplastic Particle Exposure Induces Toxicity and Amplifies Cellular Stress in THP-1 Macrophages: Insights on Molecular Pathways and Circulating Proteome Interaction.Journal of biochemical and molecular toxicology · 2026Article
- A novel RNA-binding activity of ECD contributes to U5 snRNP stability and pre-mRNA splicing.Nucleic acids research · 2026Article
- Neurochondrin promotes U5 snRNP maturation by regulating AAR2 release from PRPF8.Nucleic acids research · 2026Article
- Insights into the function and structure of the R2TP (RUVBL1-RUVBL2-RPAP3-PIH1D1) chaperone complex.Cell stress & chaperones · 2026Review
- RPAP3: Structural evolution, chaperone networks, and disease implications of a transcriptional Co-chaperone.The Journal of biological chemistry · 2026Review
- An integrative structural biology approach reveals the dynamic organization of the R2SP quaternary chaperone complex.Nature communications · 2026Article
- Co-translational determination of quaternary structures in chaperone factories.Nature communications · 2026Article
- Roodmus: a toolkit for benchmarking heterogeneous electron cryo-microscopy reconstructions.IUCrJ · 2024Article
- Differential roles of putative arginine fingers of AAAbioRxiv : the preprint server for biology · 2024Article
- Structure of the human 20S U5 snRNP.Nature structural & molecular biology · 2024Article
- Maturation and Assembly of mTOR Complexes by the HSP90-R2TP-TTT Chaperone System: Molecular Insights and Mechanisms.Sub-cellular biochemistry · 2024Review
- The Role of Hsp90-R2TP in Macromolecular Complex Assembly and Stabilization.Biomolecules · 2022Review
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Authors and funding
9 authors at 2 institutions in 2 countries.
Funding
Abstract
Biogenesis of the U5 small nuclear ribonucleoprotein (snRNP) is an essential and highly regulated process. In particular, PRPF8, one of U5 snRNP main components, requires HSP90 working in concert with R2TP, a cochaperone complex containing RUVBL1 and RUVBL2 AAA-ATPases, and additional factors that are still poorly characterized. Here, we use biochemistry, interaction mapping, mass spectrometry and cryoEM to study the role of ZNHIT2 in the regulation of the R2TP chaperone during the biogenesis of PRPF8. ZNHIT2 forms a complex with R2TP which depends exclusively on the direct interaction of ZNHIT2 with the RUVBL1-RUVBL2 ATPases. The cryoEM analysis of this complex reveals that ZNHIT2 alters the conformation and nucleotide state of RUVBL1-RUVBL2, affecting its ATPase activity. We characterized the interactions between R2TP, PRPF8, ZNHIT2, ECD and AAR2 proteins. Interestingly, PRPF8 makes a direct interaction with R2TP and this complex can incorporate ZNHIT2 and other proteins involved in the biogenesis of PRPF8 such as ECD and AAR2. Together, these results show that ZNHIT2 participates in the assembly of the U5 snRNP as part of a network of contacts between assembly factors required for PRPF8 biogenesis and the R2TP-HSP90 chaperone, while concomitantly regulating the structure and nucleotide state of R2TP.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.