ArticleNature structural & molecular biology2025
Condensation of ZFP207 and U1 snRNP promotes spliceosome assembly.
Article in Nature structural & molecular biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
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Who cites it
11 citing papers in PubMed.
- Hierarchical Nuclear Architecture in Pre-mRNA Splicing: From IDRs to Speckles and Meshworks.International journal of molecular sciences · 2026Review
- LENG8 mediates RNA nuclear retention and degradation in eukaryotes.Molecular cell · 2026Article
- MCVAE-based multi-omic anomaly detection in Fragile X Syndrome.NAR molecular medicine · 2026Article
- Zinc finger proteins (ZFPs) in health and disease.Molecular biomedicine · 2026Review
- RNA-coupled CRISPR screens reveal ZNF207 as a regulator of LMNA aberrant splicing in progeria.Molecular cell · 2026Article
- Protein codes and mobility together shape cellular function and disease.Trends in biochemical sciences · 2026Review
- Alternative Splicing: Molecular Mechanisms, Biological Functions, Diseases, and Potential Therapeutic Targets.MedComm · 2025Review
- Swt21p Is Required for Nam8p-U1 snRNP Association and Efficient Pre-mRNA Splicing inInternational journal of molecular sciences · 2025Article
- Cholesterol finds its pocket in LYCHOS.Nature structural & molecular biology · 2025Article
- Controlled and orthogonal partitioning of large particles into biomolecular condensates.Nature communications · 2025Article
- Emerging Roles of Biomolecular Condensates in Pre-mRNA 3' End Processing.Wiley interdisciplinary reviews. RNAReview
Corrections and comments
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Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The U1 small nuclear ribonucleoprotein (snRNP) has an essential role in initiating spliceosome assembly, yet the mechanism underlying its synergy with other splicing regulators for efficient spliceosome assembly remains elusive. Here we identify zinc finger protein 207 (ZFP207) as a key regulator of U1 snRNP function that substantially promotes spliceosome assembly. Acute depletion of ZFP207 results in a series of molecular phenotypes indicative of U1 snRNP dysregulation. Mechanistically, the N-terminal zinc finger domains of ZFP207 directly bind to stem-loop 3 of U1 snRNA, while its C-terminal intrinsically disordered regions undergo phase separation to form biomolecular condensates with U1 snRNP. These condensates create a crowded molecular environment that increases the local concentration of splicing snRNPs and regulators, thereby accelerating the speed of spliceosome assembly by facilitating interactions between U1 snRNP and other snRNPs. Collectively, our study demonstrates the critical role of phase separation in ensuring effective U1 snRNP function and promoting efficient spliceosome assembly.
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Registered trials
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 OpenQuestion graph.