ArticleNature structural & molecular biology2013
Staufen1 dimerizes through a conserved motif and a degenerate dsRNA-binding domain to promote mRNA decay.
Article in Nature structural & molecular biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.
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Who cites it
47 citing papers in PubMed, 60 citations in OpenAlex.
- Fine-Tuned Regulation of mRNA Translation and Transport by STAU2 Condensate Facilitates Neuronal Development and Plasticity.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Article
- Toward unraveling molecular grammars for dsRNA-binding proteins: substrate recognition to binding mechanisms.BMB reports · 2025Review
- Dimerization of ADAR1 modulates site-specificity of RNA editing.Nature communications · 2024Article
- Noncanonical formation of SNX5 gene-derived circular RNA regulates cancer growth.Cell death & disease · 2024Article
- Excessive STAU1 condensate drives mTOR translation and autophagy dysfunction in neurodegeneration.The Journal of cell biology · 2024Article
- ADAR Family Proteins: A Structural Review.Current issues in molecular biology · 2024Review
- Identification of whole-cell dsRNA-binding proteins by phase separation.RNA biology · 2024Article
- Phosphomimicry on STAU1 Serine 20 Impairs STAU1 Posttranscriptional Functions and Induces Apoptosis in Human Transformed Cells.International journal of molecular sciences · 2022Article
- acorde unravels functionally interpretable networks of isoform co-usage from single cell data.Nature communications · 2022Article
- The multifunctional RNA-binding protein Staufen1: an emerging regulator of oncogenesis through its various roles in key cellular events.Cellular and molecular life sciences : CMLS · 2021Review
- Investigation of the effect of Staufen1 overexpression on the HIV-1 virus production.BMB reports · 2021Article
- Targeting of viral RNAs by Upf1-mediated RNA decay pathways.Current opinion in virology · 2021Review
- 3'READS + RIP defines differential Staufen1 binding to alternative 3'UTR isoforms and reveals structures and sequence motifs influencing binding and polysome association.RNA (New York, N.Y.) · 2020Article
- Short interspersed nuclear element (SINE)-mediated post-transcriptional effects on human and mouse gene expression: SINE-UP for active duty.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2020Review
- A multipronged approach to understanding the form and function of hStaufen protein.RNA (New York, N.Y.) · 2020Article
- Staufen1 reads out structure and sequence features in ARF1 dsRNA for target recognition.Nucleic acids research · 2020Article
- Insights into the assembly and architecture of a Staufen-mediated mRNA decay (SMD)-competent mRNP.Nature communications · 2019Article
- Staufen1 and UPF1 exert opposite actions on the replacement of the nuclear cap-binding complex by eIF4E at the 5' end of mRNAs.Nucleic acids research · 2019Article
- Staufen2-mediated RNA recognition and localization requires combinatorial action of multiple domains.Nature communications · 2019Article
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4 authors at 1 institution in 1 country.
Funding
Abstract
Staufen1 (STAU1)-mediated mRNA decay (SMD) degrades mammalian-cell mRNAs that bind the double-stranded RNA (dsRNA)-binding protein STAU1 in their 3' untranslated region. We report a new motif, which typifies STAU homologs from all vertebrate classes, that is responsible for human STAU1 (hSTAU1) homodimerization. Our crystal structure and mutagenesis analyses reveal that this motif, which we named the Staufen-swapping motif (SSM), and the dsRNA-binding domain 5 ('RBD'5) mediate protein dimerization: the two SSM α-helices of one molecule interact primarily through a hydrophobic patch with the two 'RBD'5 α-helices of a second molecule. 'RBD'5 adopts the canonical α-β-β-β-α fold of a functional RBD, but it lacks residues and features required to bind duplex RNA. In cells, SSM-mediated hSTAU1 dimerization increases the efficiency of SMD by augmenting hSTAU1 binding to the ATP-dependent RNA helicase hUPF1. Dimerization regulates keratinocyte-mediated wound healing and many other cellular processes.
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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.