ArticleNucleic acids research2008
The third RNA recognition motif of Drosophila ELAV protein has a role in multimerization.
Article in Nucleic acids research, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed, 62 citations in OpenAlex.
- Article
- Angel wing: a class of alternative splicing regulators in animals.Nucleic acids research · 2025Article
- Structural, biological, and biomedical implications of mRNA interactions with the master regulator HuR.NAR molecular medicine · 2025Review
- Phylogenomic instructed target analysis reveals ELAV complex binding to multiple optimally spaced U-rich motifs.Nucleic acids research · 2024Article
- HPF1 regulates tendon stem/progenitor cell senescence and tendon repair via PARP1-mediated poly-ADP ribosylation of HuR.Genes & genomics · 2024Article
- Identification of HuR-RNA Interfering Compounds by Dynamic Combinatorial Chemistry and Fluorescence Polarization.ACS medicinal chemistry letters · 2023Article
- Spontaneous binding of single-stranded RNAs to RRM proteins visualized by unbiased atomistic simulations with a rescaled RNA force field.Nucleic acids research · 2022Article
- A critical developmental window for ELAV/Hu-dependent mRNA signatures at the onset of neuronal differentiation.Cell reports · 2022Article
- Cell-Penetrating Peptide TAT-HuR-HNS3 Suppresses Proinflammatory Gene Expression via Competitively Blocking Interaction of HuR with Its Partners.Journal of immunology (Baltimore, Md. : 1950) · 2022Article
- The versatile role of HuR in Glioblastoma and its potential as a therapeutic target for a multi-pronged attack.Advanced drug delivery reviews · 2022Review
- Roles of Embryonic Lethal Abnormal Vision-Like RNA Binding Proteins in Cancer and Beyond.Frontiers in cell and developmental biology · 2022Review
- Poly(ADP-ribosyl)ation enhances HuR oligomerization and contributes to pro-inflammatory gene mRNA stabilization.Cellular and molecular life sciences : CMLS · 2021Article
- The ELAV family of RNA-binding proteins in synaptic plasticity and long-term memory.Neurobiology of learning and memory · 2019Review
- Molecular basis for AU-rich element recognition and dimerization by the HuR C-terminal RRM.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- HuR biological function involves RRM3-mediated dimerization and RNA binding by all three RRMs.Nucleic acids research · 2019Article
- Exploration of ligand binding modes towards the identification of compounds targeting HuR: a combined STD-NMR and Molecular Modelling approach.Scientific reports · 2018Article
- Hu antigen R (HuR) multimerization contributes to glioma disease progression.The Journal of biological chemistry · 2017Article
- Identification of HuR target circular RNAs uncovers suppression of PABPN1 translation by CircPABPN1.RNA biology · 2017Article
- LncRNA OIP5-AS1/cyrano sponges RNA-binding protein HuR.Nucleic acids research · 2016Article
- mRNA and DNA selection via protein multimerization: YB-1 as a case study.Nucleic acids research · 2015Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
ELAV is a neuron-specific RNA-binding protein in Drosophila that is required for development and maintenance of neurons. ELAV regulates alternative splicing of Neuroglian and erect wing (ewg) transcripts, and has been shown to form a multimeric complex on the last ewg intron. The protein has three RNA recognition motifs (RRM1, 2 and 3) with a hinge region between RRM2 and 3. In this study, we used the yeast two-hybrid system to determine the multimerization domain of ELAV. Using deletion constructs, we mapped an interaction activity to a region containing most of RRM3. We found three conserved short sequences in RRM3 that were essential for the interaction, and also sufficient to give the interaction activity to RRM2 when introduced into it. In our in vivo functional assay, a mutation in one of the three sequences showed reduced activity in splicing regulation, underlining the functional importance of multimerization. However, RRM2 with the three RRM3 interaction sequences did not function as RRM3 in vivo, which suggested that multimerization is not the only function of RRM3. Our results are consistent with a model in which RRM3 serves as a bi-functional domain that interacts with both RNA and protein.
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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.