ArticleRNA biology2014
The binding of TIA-1 to RNA C-rich sequences is driven by its C-terminal RRM domain.
Article in RNA biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 25 citations in OpenAlex.
- eIF5A coordinates the transcription and translation of its target genes.Cellular and molecular life sciences : CMLS · 2026Article
- Expression Patterns of T-Cell Intracellular Antigen 1 in Neurodegenerative Disorders and Stroke.International journal of molecular sciences · 2026Review
- Study of Stress Granule Core Protein AtUBP1b PhosphorylationPlants (Basel, Switzerland) · 2025Article
- Targeting the Hippo pathway in Schwann cells ameliorates peripheral nerve degeneration via a polypharmacological mechanism.Neurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics · 2024Article
- RNA structures within Venezuelan equine encephalitis virus E1 alter macrophage replication fitness and contribute to viral emergence.PLoS pathogens · 2024Article
- A New Phase of Networking: The Molecular Composition and Regulatory Dynamics of Mammalian Stress Granules.Chemical reviews · 2023Review
- Regulation of TIA-1 Condensates: ZnFrontiers in molecular biosciences · 2022Article
- Tandem RNA binding sites induce self-association of the stress granule marker protein TIA-1.Nucleic acids research · 2021Article
- Post-translational Control of RNA-Binding Proteins and Disease-Related Dysregulation.Frontiers in molecular biosciences · 2021Review
- RNA-Binding Proteins in the Control of LPS-Induced Macrophage Response.Frontiers in genetics · 2019Review
- A putative RNA binding protein fromFEBS open bio · 2018Article
- TIA-1 RRM23 binding and recognition of target oligonucleotides.Nucleic acids research · 2017Article
- RNA Binding Protein Regulation and Cross-Talk in the Control of AU-rich mRNA Fate.Frontiers in molecular biosciences · 2017Review
- 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
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Authors and funding
11 authors at 8 institutions in 6 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
T-cell intracellular antigen-1 (TIA-1) is a key DNA/RNA binding protein that regulates translation by sequestering target mRNAs in stress granules (SG) in response to stress conditions. TIA-1 possesses three RNA recognition motifs (RRM) along with a glutamine-rich domain, with the central domains (RRM2 and RRM3) acting as RNA binding platforms. While the RRM2 domain, which displays high affinity for U-rich RNA sequences, is primarily responsible for interaction with RNA, the contribution of RRM3 to bind RNA as well as the target RNA sequences that it binds preferentially are still unknown. Here we combined nuclear magnetic resonance (NMR) and surface plasmon resonance (SPR) techniques to elucidate the sequence specificity of TIA-1 RRM3. With a novel approach using saturation transfer difference NMR (STD-NMR) to quantify protein-nucleic acids interactions, we demonstrate that isolated RRM3 binds to both C- and U-rich stretches with micromolar affinity. In combination with RRM2 and in the context of full-length TIA-1, RRM3 significantly enhanced the binding to RNA, particularly to cytosine-rich RNA oligos, as assessed by biotinylated RNA pull-down analysis. Our findings provide new insight into the role of RRM3 in regulating TIA-1 binding to C-rich stretches, that are abundant at the 5' TOPs (5' terminal oligopyrimidine tracts) of mRNAs whose translation is repressed under stress situations.
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