ArticleChromosoma2005
The C-terminal domain of coilin interacts with Sm proteins and U snRNPs.
Article in Chromosoma, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
39 citing papers in PubMed, 59 citations in OpenAlex.
- Dynamic interaction of spliceosomal snRNPs with coilin explains Cajal body characteristics.The Journal of cell biology · 2025Article
- Coilin and Cajal bodies.Nucleus (Austin, Tex.) · 2023Review
- A GFP splicing reporter in a coilin mutant background reveals links between alternative splicing, siRNAs, and coilin function in Arabidopsis thaliana.G3 (Bethesda, Md.) · 2023Article
- The Cajal body marker protein coilin is SUMOylated and possesses SUMO E3 ligase-like activity.Frontiers in RNA research · 2023Article
- The coilin N-terminus mediates multivalent interactions between coilin and Nopp140 to form and maintain Cajal bodies.Nature communications · 2022Article
- A point mutation in human coilin prevents Cajal body formation.Journal of cell science · 2022Article
- Early rRNA processing is a stress-dependent regulatory event whose inhibition maintains nucleolar integrity.Nucleic acids research · 2022Article
- Shaping the Innate Immune Response Through Post-Transcriptional Regulation of Gene Expression Mediated by RNA-Binding Proteins.Frontiers in immunology · 2021Review
- Functional Analysis of Coilin in Virus Resistance and Stress Tolerance of Potato Solanum tuberosum using CRISPR-Cas9 Editing.Doklady. Biochemistry and biophysics · 2019Article
- The Sm-core mediates the retention of partially-assembled spliceosomal snRNPs in Cajal bodies until their full maturation.Nucleic acids research · 2018Article
- The life of U6 small nuclear RNA, from cradle to grave.RNA (New York, N.Y.) · 2018Review
- The prognostic potential of coilin in association with p27 expression in pediatric acute lymphoblastic leukemia for disease relapse.Cancer cell international · 2018Article
- SMN - A chaperone for nuclear RNP social occasions?RNA biology · 2017Review
- Activation of transcription enforces the formation of distinct nuclear bodies in zebrafish embryos.RNA biology · 2017Review
- Towards an understanding of regulating Cajal body activity by protein modification.RNA biology · 2017Review
- Cajal bodies and snRNPs - friends with benefits.RNA biology · 2017Review
- Article
- Coilin: The first 25 years.RNA biology · 2015Review
- Whole-genome screening identifies proteins localized to distinct nuclear bodies.The Journal of cell biology · 2013Article
- Article
Corrections and comments
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Authors and funding
8 authors at 5 institutions in 2 countries.
Funding
Abstract
Coilin is the signature protein of the Cajal body (CB), a nuclear suborganelle involved in the biogenesis of small nuclear ribonucleoproteins (snRNPs). Newly imported Sm-class snRNPs are thought to traffic through CBs before proceeding to their final nuclear destinations. Loss of coilin function in mice leads to significant viability and fertility problems. Coilin interacts directly with the spinal muscular atrophy (SMA) protein via dimethylarginine residues in its C-terminal domain. Although coilin hypomethylation results in delocalization of survival of motor neurons (SMN) from CBs, high concentrations of snRNPs remain within these structures. Thus, CBs appear to be involved in snRNP maturation, but factors that tether snRNPs to CBs have not been described. In this report, we demonstrate that the coilin C-terminal domain binds directly to various Sm and Lsm proteins via their Sm motifs. We show that the region of coilin responsible for this binding activity is separable from that which binds to SMN. Interestingly, U2, U4, U5, and U6 snRNPs interact with the coilin C-terminal domain in a glutathione S-transferase (GST)-pulldown assay, whereas U1 and U7 snRNPs do not. Thus, the ability to interact with free Sm (and Lsm) proteins as well as with intact snRNPs, indicates that coilin and CBs may facilitate the modification of newly formed snRNPs, the regeneration of 'mature' snRNPs, or the reclamation of unassembled snRNP components.
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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.