ArticleRNA (New York, N.Y.)2010
Multimerization of Staufen1 in live cells.
Article in RNA (New York, N.Y.), 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 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
34 citing papers in PubMed, 49 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
- 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
- Staufen1 unwinds the secondary structure and facilitates the translation of fatty acid binding protein 4 mRNA during adipogenesis.Adipocyte · 2021Article
- Investigation of the effect of Staufen1 overexpression on the HIV-1 virus production.BMB reports · 2021Article
- 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
- 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
- The crystal structure of Staufen1 in complex with a physiological RNA sheds light on substrate selectivity.Life science alliance · 2018Article
- The M-phase specific hyperphosphorylation of Staufen2 involved the cyclin-dependent kinase CDK1.BMC cell biology · 2017Article
- The downregulation of the RNA-binding protein Staufen2 in response to DNA damage promotes apoptosis.Nucleic acids research · 2016Article
- Staufen1 Regulates Multiple Alternative Splicing Events either Positively or Negatively in DM1 Indicating Its Role as a Disease Modifier.PLoS genetics · 2016Article
- Selective ligand activity at Nur/retinoid X receptor complexes revealed by dimer-specific bioluminescence resonance energy transfer-based sensors.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2015Article
- 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
- Synaptic control of local translation: the plot thickens with new characters.Cellular and molecular life sciences : CMLS · 2014Review
- mRNP granules. Assembly, function, and connections with disease.RNA biology · 2014Review
- Staufen1 senses overall transcript secondary structure to regulate translation.Nature structural & molecular biology · 2014Article
Corrections and comments
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Authors and funding
10 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Transport of mRNA is an efficient mechanism to target proteins to specific regions of a cell. Although it is well documented that mRNAs are transported in ribonucleoprotein (RNP) complexes, several of the mechanisms involved in complex formation and localization are poorly understood. Staufen (Stau) 1, a double-stranded RNA-binding protein, is a well accepted marker of mRNA transport complexes. In this manuscript, we provide evidence that Stau1 self-associates in live cells using immunoprecipitation and bioluminescence resonance energy transfer (BRET) assays. The double-stranded RNA-binding domains dsRBD3 and dsRBD4 contributed about half of the signal, suggesting that Stau1 RNA-binding activity is involved in Stau1 self-association. Protein-protein interaction also occurred, via dsRBD5 and dsRBD2, as shown by in vitro pull-down, yeast two-hybrid, and BRET assays in live cells. Interestingly, Stau1 self-association contributes to the formation of oligomeric complexes as evidenced by the coexpression of split Renilla luciferase halves covalently linked to Stau1 in a protein complementation assay (PCA) combined with a BRET assay with Stau1-YFP. Moreover, we showed that these higher-order Stau1-containing complexes carry RNAs when the RNA stain SYTO 14 was used as the energy acceptor in the PCA/BRET assay. The oligomeric composition of Stau1-containing complexes and the presence of specific mRNAs have been confirmed by biochemical approaches involving two successive immunoprecipitations of Stau1-tagged molecules followed by qRT-PCR amplification. Altogether, these results indicate that Stau1 self-associates in mRNPs via its multiple functional domains that can select mRNAs to be transported and establish protein-protein interaction.
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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.