ArticleThe Biochemical journal2004
Characterization of Staufen 1 ribonucleoprotein complexes.
Article in The Biochemical journal, 2004. 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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Who cites it
34 citing papers in PubMed, 71 citations in OpenAlex.
- The double-stranded RNA-binding protein, Staufen1, is an IRES-transacting factor regulating HIV-1 cap-independent translation initiation.Nucleic acids research · 2022Article
- Intracellular and intercellular transport of RNA organelles in CXG repeat disorders: The strength of weak ties.Frontiers in molecular biosciences · 2022Review
- A kinesin adapter directly mediates dendritic mRNA localization during neural development in mice.The Journal of biological chemistry · 2020Article
- Sorting mRNA Molecules for Cytoplasmic Transport and Localization.Frontiers in genetics · 2018Review
- Proteomic analysis of FUS interacting proteins provides insights into FUS function and its role in ALS.Biochimica et biophysica acta · 2016Article
- A ribonucleoprotein complex protects the interleukin-6 mRNA from degradation by distinct herpesviral endonucleases.PLoS pathogens · 2015Article
- The RNA-binding protein Staufen1 impairs myogenic differentiation via a c-myc-dependent mechanism.Molecular biology of the cell · 2014Article
- Functional signature for the recognition of specific target mRNAs by human Staufen1 protein.Nucleic acids research · 2014Article
- Article
- A non-canonical initiation site is required for efficient translation of the dendritically localized Shank1 mRNA.PloS one · 2014Article
- Subcellular sorting of the G-protein coupled mouse somatostatin receptor 5 by a network of PDZ-domain containing proteins.PloS one · 2014Article
- Staufen-1 interacts with the human endogenous retrovirus family HERV-K(HML-2) rec and gag proteins and increases virion production.Journal of virology · 2013Article
- SHANK3 gene mutations associated with autism facilitate ligand binding to the Shank3 ankyrin repeat region.The Journal of biological chemistry · 2013Article
- Ribosomal protein P0 promotes Potato virus A infection and functions in viral translation together with VPg and eIF(iso)4E.Journal of virology · 2013Article
- Makorin ring zinc finger protein 1 (MKRN1), a novel poly(A)-binding protein-interacting protein, stimulates translation in nerve cells.The Journal of biological chemistry · 2012Article
- Molecular and genetic analysis of the Drosophila model of fragile X syndrome.Results and problems in cell differentiation · 2012Article
- Characterization of staufen1 ribonucleoproteins by mass spectrometry and biochemical analyses reveal the presence of diverse host proteins associated with human immunodeficiency virus type 1.Frontiers in microbiology · 2012Article
- Molecular composition of staufen2-containing ribonucleoproteins in embryonic rat brain.PloS one · 2010Article
- Multimerization of Staufen1 in live cells.RNA (New York, N.Y.) · 2010Article
- Fragile X mental retardation protein regulates the levels of scaffold proteins and glutamate receptors in postsynaptic densities.The Journal of biological chemistry · 2009Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In Drosophila oocytes and neuroblasts, the double-stranded RNA binding protein Staufen assembles into ribonucleoprotein particles, which mediate cytoplasmic mRNA trafficking and translation. Two different mammalian orthologues also appear to reside in distinct RNA-containing particles. To date, relatively little is known about the molecular composition of Staufen-containing ribonucleoprotein complexes. Here, we have used a novel one-step affinity purification protocol to identify components of Staufen 1-containing particles. Whereas the nucleocytoplasmic RNA-binding protein nucleolin is linked to Staufen in an RNA-dependent manner, the association of protein phosphatase 1, the microtubule-dependent motor protein kinesin and several components of the large and small ribosomal subunits with Staufen ribonucleoprotein complexes is RNA-independent. Notably, all these components do not co-purify with a second RNA-binding protein, hnRNPK (heterogeneous ribonucleoprotein K), demonstrating the high specificity of the purification protocol. Furthermore, pull-down and immunoprecipitation experiments suggest a direct interaction between Staufen 1 and the ribosomal protein P0 in vitro as well as in cells. In cell fractionation and sucrose gradient assays, Staufen co-fractionates with intact ribosomes and polysomes, but not with the isolated 40 S ribosomal subunit. Taken together, these findings imply that, in the cytoplasm of mammalian cells, an association with the ribosomal P-stalk protein P0 recruits Staufen 1 into ribosome-containing ribonucleoprotein particles, which also contain kinesin, protein phosphatase 1 and nucleolin.
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