ArticleJournal of molecular biology2012
Three RNA recognition motifs participate in RNA recognition and structural organization by the pro-apoptotic factor TIA-1.
Article in Journal of molecular biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 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
26 citing papers in PubMed, 37 citations in OpenAlex.
- Role of Stress Granules in Suppressing Viral Replication by the Infectious Bronchitis Virus Endoribonuclease.Journal of virology · 2022Article
- Tandem RNA binding sites induce self-association of the stress granule marker protein TIA-1.Nucleic acids research · 2021Article
- Restriction of an intron size en route to endothermy.Nucleic acids research · 2021Article
- Post-translational Control of RNA-Binding Proteins and Disease-Related Dysregulation.Frontiers in molecular biosciences · 2021Review
- AU-rich element-binding proteins in colorectal cancer.World journal of gastrointestinal oncology · 2019Review
- Linking hnRNP Function to ALS and FTD Pathology.Frontiers in neuroscience · 2018Review
- KH-type splicing regulatory protein is involved in esophageal squamous cell carcinoma progression.Oncotarget · 2017Article
- CryoEM structure of Saccharomyces cerevisiae U1 snRNP offers insight into alternative splicing.Nature communications · 2017Article
- KSHV inhibits stress granule formation by viral ORF57 blocking PKR activation.PLoS pathogens · 2017Article
- TIA-1 RRM23 binding and recognition of target oligonucleotides.Nucleic acids research · 2017Article
- Topoisomerase 3β is the major topoisomerase for mRNAs and linked to neurodevelopment and mental dysfunction.Nucleic acids research · 2017Article
- Unmasking the U2AF homology motif family: a bona fide protein-protein interaction motif in disguise.RNA (New York, N.Y.) · 2016Review
- A Structure-free Method for Quantifying Conformational Flexibility in proteins.Scientific reports · 2016Article
- Selection preserves Ubiquitin Specific Protease 4 alternative exon skipping in therian mammals.Scientific reports · 2016Article
- Spatio-temporal Dynamics and Mechanisms of Stress Granule Assembly.PLoS computational biology · 2015Article
- Boric acid induces cytoplasmic stress granule formation, eIF2α phosphorylation, and ATF4 in prostate DU-145 cells.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2015Article
- Alternative splicing of TIA-1 in human colon cancer regulates VEGF isoform expression, angiogenesis, tumour growth and bevacizumab resistance.Molecular oncology · 2015Article
- T-cell intracellular antigens in health and disease.Cell cycle (Georgetown, Tex.) · 2015Review
- RNA recognition and stress granule formation by TIA proteins.International journal of molecular sciences · 2014Review
- Structure, dynamics and RNA binding of the multi-domain splicing factor TIA-1.Nucleic acids research · 2014Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
T-cell intracellular antigen-1 (TIA-1) regulates developmental and stress-responsive pathways through distinct activities at the levels of alternative pre-mRNA splicing and mRNA translation. The TIA-1 polypeptide contains three RNA recognition motifs (RRMs). The central RRM2 and C-terminal RRM3 associate with cellular mRNAs. The N-terminal RRM1 enhances interactions of a C-terminal Q-rich domain of TIA-1 with the U1-C splicing factor, despite linear separation of the domains in the TIA-1 sequence. Given the expanded functional repertoire of the RRM family, it was unknown whether TIA-1 RRM1 contributes to RNA binding as well as documented protein interactions. To address this question, we used isothermal titration calorimetry and small-angle X-ray scattering to dissect the roles of the TIA-1 RRMs in RNA recognition. Notably, the fas RNA exhibited two binding sites with indistinguishable affinities for TIA-1. Analyses of TIA-1 variants established that RRM1 was dispensable for binding AU-rich fas sites, yet all three RRMs were required to bind a polyU RNA with high affinity. Small-angle X-ray scattering analyses demonstrated a "V" shape for a TIA-1 construct comprising the three RRMs and revealed that its dimensions became more compact in the RNA-bound state. The sequence-selective involvement of TIA-1 RRM1 in RNA recognition suggests a possible role for RNA sequences in regulating the distinct functions of TIA-1. Further implications for U1-C recruitment by the adjacent TIA-1 binding sites of the fas pre-mRNA and the bent TIA-1 shape, which organizes the N- and C-termini on the same side of the protein, are discussed.
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.