ArticleNucleic acids research2011
Different modes of interaction by TIAR and HuR with target RNA and DNA.
Article in Nucleic acids research, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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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
38 citing papers in PubMed, 72 citations in OpenAlex.
- The Regulatory Roles of RNA-Binding Proteins in Plant Salt Stress Response.Plants (Basel, Switzerland) · 2025Review
- Post-transcriptional regulation by HuR in colorectal cancer: impacts on tumor progression and therapeutic strategies.Frontiers in immunology · 2025Review
- Applications of Surface Plasmon Resonance for Advanced Studies Involving Nucleic Acids.RNA nanomed · 2024Article
- Novel, soluble 3-heteroaryl-substituted tanshinone mimics attenuate the inflammatory response in murine macrophages.Scientific reports · 2024Article
- Experimental methods to study the structure and dynamics of intrinsically disordered regions in proteins.Current research in structural biology · 2024Review
- The RNA binding proteins TIA1 and TIAL1 promote Mcl1 mRNA translation to protect germinal center responses from apoptosis.Cellular & molecular immunology · 2023Article
- T-Cell Intracellular Antigen 1-Like Protein in Physiology and Pathology.International journal of molecular sciences · 2022Review
- Tumor protein D52 is upregulated in oral squamous carcinoma cells under hypoxia in a hypoxia-inducible-factor-independent manner and is involved in cell death resistance.Cell & bioscience · 2021Article
- Article
- Approaches for measuring the dynamics of RNA-protein interactions.Wiley interdisciplinary reviews. RNA · 2020Review
- HuR controls apoptosis and activation response without effects on cytokine 3' UTRs.RNA biology · 2019Article
- HuR biological function involves RRM3-mediated dimerization and RNA binding by all three RRMs.Nucleic acids research · 2019Article
- Discovering the 3' UTR-mediated regulation of alpha-synuclein.Nucleic acids research · 2017Article
- Regulation of HuR structure and function by dihydrotanshinone-I.Nucleic acids research · 2017Article
- TIA-1 RRM23 binding and recognition of target oligonucleotides.Nucleic acids research · 2017Article
- Posttranslational control of HuR function.Wiley interdisciplinary reviews. RNA · 2017Review
- The fungal natural product azaphilone-9 binds to HuR and inhibits HuR-RNA interaction in vitro.PloS one · 2017Article
- RNA Binding Protein Regulation and Cross-Talk in the Control of AU-rich mRNA Fate.Frontiers in molecular biosciences · 2017Review
- RBM7 subunit of the NEXT complex binds U-rich sequences and targets 3'-end extended forms of snRNAs.Nucleic acids research · 2015Article
- ALS-associated mutant FUS inhibits macroautophagy which is restored by overexpression of Rab1.Cell death discovery · 2015Article
Corrections and comments
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Authors and funding
10 authors at 3 institutions in 2 countries.
Funding
Abstract
TIAR and HuR are mRNA-binding proteins that play important roles in the regulation of translation. They both possess three RNA recognition motifs (RRMs) and bind to AU-rich elements (AREs), with seemingly overlapping specificity. Here we show using SPR that TIAR and HuR bind to both U-rich and AU-rich RNA in the nanomolar range, with higher overall affinity for U-rich RNA. However, the higher affinity for U-rich sequences is mainly due to faster association with U-rich RNA, which we propose is a reflection of the higher probability of association. Differences between TIAR and HuR are observed in their modes of binding to RNA. TIAR is able to bind deoxy-oligonucleotides with nanomolar affinity, whereas HuR affinity is reduced to a micromolar level. Studies with U-rich DNA reveal that TIAR binding depends less on the 2'-hydroxyl group of RNA than HuR binding. Finally we show that SAXS data, recorded for the first two domains of TIAR in complex with RNA, are more consistent with a flexible, elongated shape and not the compact shape that the first two domains of Hu proteins adopt upon binding to RNA. We thus propose that these triple-RRM proteins, which compete for the same binding sites in cells, interact with their targets in fundamentally different ways.
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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.