ArticleMolecular and cellular biology2004
snRNAs contain specific SMN-binding domains that are essential for snRNP assembly.
Article in Molecular and cellular biology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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Who cites it
42 citing papers in PubMed, 86 citations in OpenAlex.
- RNA export through the nuclear pore complex: pathways, mechanisms, and imaging strategies.RNA biology · 2026Review
- Experimentally Tuned Protein-RNA Rosetta Score Function using Bayesian Optimization.bioRxiv : the preprint server for biology · 2026Article
- Sm-site containing mRNAs can accept Sm-rings and are downregulated in Spinal Muscular Atrophy.Nucleic acids research · 2025Article
- RNA-binding proteins in disease etiology: fragile X syndrome and spinal muscular atrophy.RNA (New York, N.Y.) · 2025Review
- SMN regulates GEMIN5 expression and acts as a modifier of GEMIN5-mediated neurodegeneration.Acta neuropathologica · 2023Article
- DIS3L2 and LSm proteins are involved in the surveillance of Sm ring-deficient snRNAs.Nucleic acids research · 2020Article
- Negative cooperativity between Gemin2 and RNA provides insights into RNA selection and the SMN complex's release in snRNP assembly.Nucleic acids research · 2020Article
- U1 snRNP Telescripting: Suppression of Premature Transcription Termination in Introns as a New Layer of Gene Regulation.Cold Spring Harbor perspectives in biology · 2019Review
- The Integrator complex regulates differential snRNA processing and fate of adult stem cells in the highly regenerative planarian Schmidtea mediterranea.PLoS genetics · 2018Article
- The role of survival motor neuron protein (SMN) in protein homeostasis.Cellular and molecular life sciences : CMLS · 2018Review
- The Sm-core mediates the retention of partially-assembled spliceosomal snRNPs in Cajal bodies until their full maturation.Nucleic acids research · 2018Article
- Structural basis for snRNA recognition by the double-WD40 repeat domain of Gemin5.Genes & development · 2016Article
- Structural insights into Gemin5-guided selection of pre-snRNAs for snRNP assembly.Genes & development · 2016Article
- A U1 snRNP-specific assembly pathway reveals the SMN complex as a versatile hub for RNP exchange.Nature structural & molecular biology · 2016Article
- Spatial regulation of cytoplasmic snRNP assembly at the cellular level.Journal of experimental botany · 2015Article
- Intracellular Bacterial Pathogens Trigger the Formation of U Small Nuclear RNA Bodies (U Bodies) through Metabolic Stress Induction.The Journal of biological chemistry · 2015Article
- SMN control of RNP assembly: from post-transcriptional gene regulation to motor neuron disease.Seminars in cell & developmental biology · 2014Review
- Identification and characterization of Drosophila Snurportin reveals a role for the import receptor Moleskin/importin-7 in snRNP biogenesis.Molecular biology of the cell · 2013Article
- Implication of the SMN complex in the biogenesis and steady state level of the signal recognition particle.Nucleic acids research · 2013Article
- Interplay between polyadenylate-binding protein 1 and Kaposi's sarcoma-associated herpesvirus ORF57 in accumulation of polyadenylated nuclear RNA, a viral long noncoding RNA.Journal of virology · 2013Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
To serve in its function as an assembly machine for spliceosomal small nuclear ribonucleoprotein particles (snRNPs), the survival of motor neurons (SMN) protein complex binds directly to the Sm proteins and the U snRNAs. A specific domain unique to U1 snRNA, stem-loop 1 (SL1), is required for SMN complex binding and U1 snRNP Sm core assembly. Here, we show that each of the major spliceosomal U snRNAs (U2, U4, and U5), as well as the minor splicing pathway U11 snRNA, contains a domain to which the SMN complex binds directly and with remarkable affinity (low nanomolar concentration). The SMN-binding domains of the U snRNAs do not have any significant nucleotide sequence similarity yet they compete for binding to the SMN complex in a manner that suggests the presence of at least two binding sites. Furthermore, the SMN complex-binding domain and the Sm site are both necessary and sufficient for Sm core assembly and their relative positions are critical for snRNP assembly. These findings indicate that the SMN complex stringently scrutinizes RNAs for specific structural features that are not obvious from the sequence of the RNAs but are required for their identification as bona fide snRNAs. It is likely that this surveillance capacity of the SMN complex ensures assembly of Sm cores on the correct RNAs only and prevents illicit, potentially deleterious, assembly of Sm cores on random RNAs.
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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 OpenQuestion graph.