ArticleThe Journal of biological chemistry2014
A conserved three-nucleotide core motif defines Musashi RNA binding specificity.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.
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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.
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Who cites it
59 citing papers in PubMed, 94 citations in OpenAlex.
- Deciphering the RNA recognition by Musashi-1 to design protein and RNA variants for in vitro and in vivo applications.Nucleic acids research · 2025Article
- RRMScorer: A web server for predicting RNA recognition motif binding preferences.Nucleic acids research · 2025Article
- Dissecting RNA selectivity mediated by tandem RNA-binding domains.The Journal of biological chemistry · 2025Article
- Regulatory Effects of RNA-Protein Interactions Revealed by Reporter Assays of Bacteria Grown on Solid Media.Biosensors · 2025Article
- Developing novel Lin28 inhibitors by computer aided drug design.Cell death discovery · 2025Article
- Progress in understanding how clock genes regulate aging and associated metabolic processes.Frontiers in physiology · 2025Review
- Unraveling the Bivalent and Rapid Interactions Between a Multivalent RNA Recognition Motif and RNA: A Kinetic Approach.Biochemistry · 2024Article
- Probing the orthogonality and robustness of the mammalian RNA-binding protein Musashi-1 in Escherichia coli.Journal of biological engineering · 2024Article
- A novel interaction between the 5' untranslated region of the Chikungunya virus genome and Musashi RNA binding protein is essential for efficient virus genome replication.Nucleic acids research · 2024Article
- The RNA-binding protein Msi2 regulates autophagy during myogenic differentiation.Life science alliance · 2024Article
- Repurposing the mammalian RNA-binding protein Musashi-1 as an allosteric translation repressor in bacteria.eLife · 2024Article
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- The Musashi RNA-binding proteins in female cancers: insights on molecular mechanisms and therapeutic relevance.Biomarker research · 2023Review
- Musashi Exerts Control of Gonadotrope Target mRNA Translation During the Mouse Estrous Cycle.Endocrinology · 2023Article
- 3'UTR of mRNA Encoding CPEB Protein Orb2 Plays an Essential Role in Intracellular Transport in Neurons.Cells · 2023Article
- Zika virus RNA structure controls its unique neurotropism by bipartite binding to Musashi-1.Nature communications · 2023Article
- (-)- Gossypol Inhibition of Musashi-Mediated Forgetting Improves Memory and Age-Dependent Memory Decline in Caenorhabditis elegans.Molecular neurobiology · 2023Article
- Deciphering the RRM-RNA recognition code: A computational analysis.PLoS computational biology · 2023Article
- TP53 mutations and RNA-binding protein MUSASHI-2 drive resistance to PRMT5-targeted therapy in B-cell lymphoma.Nature communications · 2022Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
Musashi (MSI) family proteins control cell proliferation and differentiation in many biological systems. They are overexpressed in tumors of several origins, and their expression level correlates with poor prognosis. MSI proteins control gene expression by binding RNA and regulating its translation. They contain two RNA recognition motif (RRM) domains, which recognize a defined sequence element. The relative contribution of each nucleotide to the binding affinity and specificity is unknown. We analyzed the binding specificity of three MSI family RRM domains using a quantitative fluorescence anisotropy assay. We found that the core element driving recognition is the sequence UAG. Nucleotides outside of this motif have a limited contribution to binding free energy. For mouse MSI1, recognition is determined by the first of the two RRM domains. The second RRM adds affinity but does not contribute to binding specificity. In contrast, the recognition element for Drosophila MSI is more extensive than the mouse homolog, suggesting functional divergence. The short nature of the binding determinant suggests that protein-RNA affinity alone is insufficient to drive target selection by MSI family proteins.
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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.