ArticleThe Biochemical journal2002
Molecular mapping of the determinants involved in human Staufen-ribosome association.
Article in The Biochemical journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed, 58 citations in OpenAlex.
- A Degradation Motif in STAU1 Defines a Novel Family of Proteins Involved in Inflammation.International journal of molecular sciences · 2022Article
- Phosphomimicry on STAU1 Serine 20 Impairs STAU1 Posttranscriptional Functions and Induces Apoptosis in Human Transformed Cells.International journal of molecular sciences · 2022Article
- The double-stranded RNA-binding protein, Staufen1, is an IRES-transacting factor regulating HIV-1 cap-independent translation initiation.Nucleic acids research · 2022Article
- Noncanonical immune response to the inhibition of DNA methylation by Staufen1 via stabilization of endogenous retrovirus RNAs.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- 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
- Article
- The crystal structure of Staufen1 in complex with a physiological RNA sheds light on substrate selectivity.Life science alliance · 2018Article
- HIV-1 NC-induced stress granule assembly and translation arrest are inhibited by the dsRNA binding protein Staufen1.RNA (New York, N.Y.) · 2018Article
- UPF1 Governs Synaptic Plasticity through Association with a STAU2 RNA Granule.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2017Article
- The M-phase specific hyperphosphorylation of Staufen2 involved the cyclin-dependent kinase CDK1.BMC cell biology · 2017Article
- Staufen1 promotes HCV replication by inhibiting protein kinase R and transporting viral RNA to the site of translation and replication in the cells.Nucleic acids research · 2016Article
- The structural basis of Miranda-mediated Staufen localization during Drosophila neuroblast asymmetric division.Nature communications · 2015Article
- Article
- The multifunctional Staufen proteins: conserved roles from neurogenesis to synaptic plasticity.Trends in neurosciences · 2014Review
- Cell cycle-dependent regulation of the RNA-binding protein Staufen1.Nucleic acids research · 2014Article
- 'Black sheep' that don't leave the double-stranded RNA-binding domain fold.Trends in biochemical sciences · 2014Review
- Staufen1 senses overall transcript secondary structure to regulate translation.Nature structural & molecular biology · 2014Article
- Neuronal activity induces synaptic delivery of hnRNP A2/B1 by a BDNF-dependent mechanism in cultured hippocampal neurons.PloS one · 2014Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The human double-stranded (ds) RNA-binding protein Staufen (hStau) is considered to have a role in RNA transport and its localization. By using sedimentation analysis on sucrose gradients, we showed that the Staufen isoform with an apparent molecular mass of 55 kDa (Stau(55)) co-fractionated with ribosomes and associated with both the 40 and 60 S ribosomal subunits, suggesting that the Staufen isoform hStau(55) plays some role in translation. To map the determinant(s) involved in this association, we generated a series of deletion mutants and analysed their subcellular distribution by cell fractionation and fluorescent immunomicroscopy. Our results demonstrated that multiple determinants promote hStau(55)-ribosome association via both an RNA-binding-dependent mechanism and protein-protein interaction. The RNA-binding activity of the ds RNA-binding protein domain 3 (dsRBD3) but not that of dsRBD4 is the first determinant. Although necessary for stable association with ribosomes, dsRBD3 alone is not sufficient and needs other determinants as co-factors. Consistently, when expressed together, dsRBD4 and the tubulin-binding domain constitute the minimal Stau(55)/ribosome protein-protein association domain. This region of Stau(55) is sufficient to associate with ribosomes independently, but requires the RNA-binding activity of dsRBD3 for complete association. Thus the results are consistent with a putative role for Stau(55) in the regulation of translation.
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