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Staufen, RNA binding protein, homolog 1

Staufen, Stau, Stau1
Staufen is a member of the family of double-stranded RNA (dsRNA)-binding proteins involved in the transport and/or localization of mRNAs to different subcellular compartments and/or organelles. These proteins are characterized by the presence of multiple dsRNA-binding domains which are required to bind RNAs having double-stranded secondary structures. The human homologue of staufen encoded by STAU, in addition contains a microtubule- binding domain similar to that of microtubule-associated protein 1B, and binds tubulin. The STAU gene product has been shown to be present in the cytoplasm in association with the rough endoplasmic reticulum (RER), implicating this protein in the transport of mRNA via the microtubule network to the RER, the site of translation. Five transcript variants resulting from alternative splicing of STAU gene and encoding three isoforms have been described. Three of these variants encode the same isoform, however, differ in their 5'UTR. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: CAN, caspase-3, V1a, UPF1, STEP
Papers using Staufen antibodies
The use of non-permeating pigments for testing the survival of cells.
Supplier
Yang Ching-Hong, In PLoS ONE, 1970
... ml Erlenmeyer flasks and then incubated at on an orbital shaker (KS250 basic, IKA150 Labortechnik, Staufen, Germany) at 150 rpm, 25°C, in the dark.The bacterial peptide flg22 was synthesised by GenScript and diluted in sterile ...
Papers on Staufen
CLIPing Staufen to secondary RNA structures: size and location matter!
New
Kiebler et al., München, Germany. In Bioessays, Oct 2015
The authors chose a notoriously difficult to study double-stranded RNA-binding protein (dsRBP) termed Staufen1, a mammalian homolog of Drosophila Staufen involved in mRNA localization and translational control.
Dynamic profiling of double-stranded RNA binding proteins.
New
Myong et al., Urbana, United States. In Nucleic Acids Res, Oct 2015
Here we examined four human dsRBPs, ADAD2, TRBP, Staufen 1 and ADAR1 on six dsRNA substrates that vary in length and secondary structure.
hiCLIP reveals the in vivo atlas of mRNA secondary structures recognized by Staufen 1.
New
Impact
Ule et al., London, United Kingdom. In Nature, Apr 2015
Using this technique to investigate RNA structures bound by Staufen 1 (STAU1) in human cells, we uncover a dominance of intra-molecular RNA duplexes, a depletion of duplexes from coding regions of highly translated mRNAs, an unexpected prevalence of long-range duplexes in 3' untranslated regions (UTRs), and a decreased incidence of single nucleotide polymorphisms in duplex-forming regions.
Screening of APP interaction proteins by DUALmembrane yeast two-hybrid system.
Zhang et al., Beijing, China. In Int J Clin Exp Pathol, 2014
APP functions through protein-protein interactions, and in this report staufen 1 (STAU1) is demonstrated to have interaction with APP, using yeast two-hybrid screening and co-immunoprecipitation in mammalian system.
Analysis of RNA decay factor mediated RNA stability contributions on RNA abundance.
Akimitsu et al., Kashiwa, Japan. In Bmc Genomics, 2014
We identified UPF1, EXOSC5 and STAU1, well-studied RNA degradation factors, as controlling factors for 8% of cases.
The structural basis of Miranda-mediated Staufen localization during Drosophila neuroblast asymmetric division.
Wang et al., Shanghai, China. In Nat Commun, 2014
During the asymmetric division of Drosophila neuroblasts (NBs), the scaffold Miranda (Mira) coordinates the subcellular distribution of cell-fate determinants including Staufen (Stau) and segregates them into the ganglion mother cells (GMCs).
The multifunctional Staufen proteins: conserved roles from neurogenesis to synaptic plasticity.
Review
Kiebler et al., Vienna, Austria. In Trends Neurosci, 2014
Staufen (Stau) proteins belong to a family of RNA-binding proteins (RBPs) that are important for RNA localisation in many organisms.
'Black sheep' that don't leave the double-stranded RNA-binding domain fold.
Review
Maquat et al., Rochester, United States. In Trends Biochem Sci, 2014
We exemplify the growing importance of divergent dsRBDs in mRNA decay by discussing Dicer, Staufen (STAU)1 and 2, trans-activation responsive RNA-binding protein (TARBP)2, protein activator of protein kinase RNA-activated (PKR) (PACT), DiGeorge syndrome critical region (DGCR)8, DEAH box helicase proteins (DHX) 9 and 30, and dsRBD-like fold-containing proteins that have ribosome-related functions.
Staufen-mediated mRNA decay.
Review
Maquat et al., Rochester, United States. In Wiley Interdiscip Rev Rna, 2013
Staufen1 (STAU1)-mediated mRNA decay (SMD) is an mRNA degradation process in mammalian cells that is mediated by the binding of STAU1 to a STAU1-binding site (SBS) within the 3'-untranslated region (3'-UTR) of target mRNAs.
Control of somatic tissue differentiation by the long non-coding RNA TINCR.
Impact
Khavari et al., Stanford, United States. In Nature, 2013
A high-throughput screen to analyse TINCR binding capacity to approximately 9,400 human recombinant proteins revealed direct binding of TINCR RNA to the staufen1 (STAU1) protein.
Myotonic dystrophy: is a narrow focus obscuring the rest of the field?
Review
Mahadevan, Charlottesville, United States. In Curr Opin Neurol, 2012
The role of other RNA-binding proteins beyond MBNL1 and CUGBP1, such as Staufen 1 and DDX5, are being identified and studied with respect to their role in myotonic dystrophy.
Neurodegeneration-associated TDP-43 interacts with fragile X mental retardation protein (FMRP)/Staufen (STAU1) and regulates SIRT1 expression in neuronal cells.
GeneRIF
Wang et al., Beijing, China. In J Biol Chem, 2012
TDP-43 is physically associated with fragile X mental retardation protein (FMRP) and Staufen (STAU1) to form a functional complex.
Assembly of mRNA-protein complexes for directional mRNA transport in eukaryotes--an overview.
Review
Niessing et al., Tübingen, Germany. In Curr Protein Pept Sci, 2012
The second example is Staufen-dependent localization of oskar mRNA in the Drosophila embryo, for which the importance of nuclear events for cytoplasmic localization and translational control has been clearly demonstrated.
Staufen1-mediated mRNA decay functions in adipogenesis.
GeneRIF
Kim et al., Seoul, South Korea. In Mol Cell, 2012
For Stau1-mediated mRNA decay, Stau1 binds to the 3' untranslated region of target mRNA and recruits Upf1 to elicit rapid mRNA degradation.
The RNA-binding protein Staufen1 is increased in DM1 skeletal muscle and promotes alternative pre-mRNA splicing.
GeneRIF
Jasmin et al., Ottawa, Canada. In J Cell Biol, 2012
our results unravel a novel function for Staufen1 in splicing regulation and indicate that it may positively modulate the complex DM1 phenotype
Stau1 regulates Dvl2 expression during myoblast differentiation.
GeneRIF
Irie et al., Tsukuba, Japan. In Biochem Biophys Res Commun, 2012
Dvl2 has an inhibitory role in myogenesis and Stau1 coordinates myogenesis through the regulation of Dvl2 mRNA.
Impairment of the Staufen1-NS1 interaction reduces influenza viral replication.
GeneRIF
Kim et al., Ch'ŏngju, South Korea. In Biochem Biophys Res Commun, 2011
the specific region responsible for the interaction between Stau1 and influenza A Virus NS1 was identified.
Mutations in the RNA granule component TDRD7 cause cataract and glaucoma.
Impact
Maas et al., Boston, United States. In Science, 2011
TDRD7 is a Tudor domain RNA binding protein that is expressed in lens fiber cells in distinct TDRD7-RGs that interact with STAU1-ribonucleoproteins (RNPs).
lncRNAs transactivate STAU1-mediated mRNA decay by duplexing with 3' UTRs via Alu elements.
Impact
GeneRIF
Maquat et al., Rochester, United States. In Nature, 2011
findings that the binding of STAU1 to mRNAs can be transactivated by long non-coding RNAs uncovers an unexpected strategy that cells use to recruit proteins to mRNAs and mediate the decay of these mRNAs
Assembly of endogenous oskar mRNA particles for motor-dependent transport in the Drosophila oocyte.
Impact
Ephrussi et al., Heidelberg, Germany. In Cell, 2009
Here we show at the ultrastructural level that endogenous oskar ribonucleoprotein complexes (RNPs) assemble sequentially with initial recruitment of Hrp48 and the exon junction complex (EJC) to oskar transcripts in the nurse cell nuclei, and subsequent recruitment of Staufen and microtubule motors, following transport to the cytoplasm.
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