ArticleNucleic acids research2004
RNA recognition motif 2 directs the recruitment of SF2/ASF to nuclear stress bodies.
Article in Nucleic acids research, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
30 citing papers in PubMed, 54 citations in OpenAlex.
- SRSF1 modulates the dark nucleolar cap pH to restore nucleolar integrity and function.Nature chemical biology · 2026Article
- Embryo-scale Visual Cell Sorting reveals a conserved transcriptomic signature of nucleolar size linked to proteostasis.bioRxiv : the preprint server for biology · 2026Article
- Answering the Cell Stress Call: Satellite Non-Coding Transcription as a Response Mechanism.Biomolecules · 2024Review
- Review
- Mechanistic and Therapeutic Insights into Ataxic Disorders with Pentanucleotide Expansions.Cells · 2022Review
- Review
- Review
- Inhibition of HSF1 and SAFB Granule Formation Enhances Apoptosis Induced by Heat Stress.International journal of molecular sciences · 2021Article
- Heat Shock Affects Mitotic Segregation of Human Chromosomes Bound to Stress-Induced Satellite III RNAs.International journal of molecular sciences · 2020Article
- Centromere and Pericentromere Transcription: Roles and Regulation … in Sickness and in Health.Frontiers in genetics · 2018Review
- Bromodomain factors of BET family are new essential actors of pericentric heterochromatin transcriptional activation in response to heat shock.Scientific reports · 2017Article
- The bromodomain protein BRD4 regulates splicing during heat shock.Nucleic acids research · 2017Article
- Stressing out over long noncoding RNA.Biochimica et biophysica acta · 2016Review
- Transcription of tandemly repetitive DNA: functional roles.Chromosome research : an international journal on the molecular, supramolecular and evolutionary aspects of chromosome biology · 2015Review
- Constitutive heterochromatin formation and transcription in mammals.Epigenetics & chromatin · 2015Review
- Isolated pseudo-RNA-recognition motifs of SR proteins can regulate splicing using a noncanonical mode of RNA recognition.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- The landscape of DNA repeat elements in human heart failure.Genome biology · 2012Article
- Phosphorylation of SRSF1 is modulated by replicational stress.Nucleic acids research · 2012Article
- The serine/arginine-rich protein SF2/ASF regulates protein sumoylation.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Heat shock factors: integrators of cell stress, development and lifespan.Nature reviews. Molecular cell biology · 2010Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Heat shock induces the transcriptional activation of large heterochromatic regions of the human genome composed of arrays of satellite III DNA repeats. A number of RNA-processing factors, among them splicing factor SF2/ASF, associate with these transcription factors giving rise to nuclear stress bodies (nSBs). Here, we show that the recruitment of SF2/ASF to these structures is mediated by its second RNA recognition motif. Amino acid substitutions in the first alpha-helix of this domain, but not in the beta-strand regions, abrogate the association with nSBs. The same mutations drastically affect the in vivo activity of SF2/ASF in the alternative splicing of adenoviral E1A transcripts. Sequence analysis identifies four putative high-affinity binding sites for SF2/ASF in the transcribed strand of the satellite III DNA. We have verified by gel mobility shift assays that the second RNA-binding domain of SF2/ASF binds at least one of these sites. Our analysis suggests that the recruitment of SF2/ASF to nSBs is mediated by a direct interaction with satellite III transcripts and points to the second RNA-binding domain of the protein as the major determinant of this interaction.
Indexed as
Identifiers
What OpenQuestion holds
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.