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anti-Mouse (Murine) STAU1 Anticorps:
anti-Human STAU1 Anticorps:
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Human Polyclonal STAU1 Primary Antibody pour IP, WB - ABIN443142
Paul, Dansithong, Figueroa, Scoles, Pulst: Staufen1 links RNA stress granules and autophagy in a model of neurodegeneration. dans Nature communications 2018
Human Polyclonal STAU1 Primary Antibody pour ELISA, FM - ABIN6656386
Shiihashi, Ito, Arai, Kobayashi, Hayashi, Otsuka, Nakajima, Yuzaki, Itohara, Suzuki: Dendritic Homeostasis Disruption in a Novel Frontotemporal Dementia Mouse Model Expressing Cytoplasmic Fused in Sarcoma. dans EBioMedicine 2018
Study shows that double-stranded RNA binding domains (dsRBDs) 1 and 2 of mStau2 bind RNA with similar affinities and kinetics as dsRBDs 3 and 4. While RNA binding by these tandem domains is transient, all four dsRBDs recognize their target RNAs with high stability. Rescue experiments in Drosophila oocytes demonstrate that mStau2 partially rescues dmStau-dependent mRNA localization.
The role of Miranda in the localization of Staufen during the division of neuroblasts is described.
Staufen targets coracle mRNA to Drosophila neuromuscular junctions and regulates GluRIIA synaptic accumulation and bouton number.
the expression of Adf-1 targets Staufen and Fasciclin II (FasII), identified through larval brain ChIP-Seq for Adf-1, is negatively regulated by Adf-1, and manipulations of these genes predictably modify dendrite growth.
Data propose bicoid mRNA localization was done by Swallow indirectly organizing the cytoskeleton, whereas Staufen plays a direct role in dynein-dependent bicoid mRNA transport.
establishment of developmental precision and proportions in the early Drosophila embryo
role in long-term memory
Miranda has a role in coupling oskar mRNA/Staufen complexes to the bicoid mRNA localization pathway
haploinsufficiency partially restored behavioral, proteomic, and morphological characteristics of spinocerebellar ataxia type 2 pathology in vivo
The results highlight a novel molecular mechanism underlying stability of neurogenesis-associated mRNAs controlled by the Klf4/Ddx5/Stau1 axis during mammalian corticogenesis.
we suggest a model in which dynein's interaction with Staufen1 regulates mRNA localization along the axon and the synapses, and alterations in this process may correlate with synapse disruption and amyotrophic lateral sclerosis toxicity.
Collectively our results show that Staufen1 is highly expressed during early stages of differentiation/development and that it can impair differentiation by regulating c-myc thereby highlighting the multifunctional role of Staufen1 in skeletal muscle cell
For Stau1-mediated mRNA decay, Stau1 binds to the 3' untranslated region of target mRNA and recruits Upf1 to elicit rapid mRNA degradation.
Dvl2 has an inhibitory role in myogenesis and Stau1 coordinates myogenesis through the regulation of Dvl2 mRNA.
Expression of Stau1 in the mouse hippocampus is modulated by a sequence variant (B2 SINE indel) in the 3' UTR of Comt (catechol-O-methyltransferase).
Identification of mRNA/protein (mRNP) complexes and their association with rough endoplasmic reticulum equipeed with a kinesin motor
Results suggest that Stau1 negatively regulates myogenesis in C2C12 myoblasts through a mechanism that is different from Stau1-mediated mRNA decay.
Staufen is present in the preimplantation mouse embryo
Stau1 is crucial for synapse development in vitro but not critical for normal behavioral function
Stau1 is involved in recovery from stress by stabilizing polysomes, thus helping stress granule dissolution.
The results revealed the collaboration of two RNA-binding proteins, STAU1 and Lin28B, as a regulatory mechanism in neuronal differentiation.
HIV-1 requires Staufen1 to dissociate stress granules and to produce infectious viral particles.
Stau1 is an important host factor involved in viral translation and influential early in the EV-A71 replication cycle.
Our data indicate that STAU1 plays a critical role in Ebola virus replication by coordinating interactions between the viral genome and RNA synthesis machinery.
recruited to mutant ATXN2 aggregates in spinocerebellar ataxia type 2 fibroblasts
Staufen1 has differential roles in embryonal versus alveolar rhabdomyosarcoma through the control of proliferative and apoptotic pathways, respectively.
Mechanistically, we suggest that SNHG5 stabilizes the target transcripts by blocking their degradation by STAU1. Accordingly, depletion of STAU1 rescues the apoptosis induced after SNHG5 knockdown. Hence, we characterize SNHG5 as a lncRNA promoting tumour cell survival in colorectal cancer.
E2F1 induces TINCR transcriptional activity and accelerates gastric cancer progression via activation of TINCR/STAU1/CDKN2B signaling axis.
ADAR1p110 isoform competitively inhibits binding of Staufen1 to the 3'-untranslated-region dsRNAs and antagonizes Staufen1-mediated mRNA decay.
Stau1 is a stress response gene that remains efficiently translated during hypoxia and ER stress despite the substantial global inhibition of cap-dependent protein translation, promoting cell recovery following stress
Our findings suggest that HCV may appropriate Stau1 to its advantage to prevent PKR-mediated inhibition of eIF2alpha, which is required for the synthesis of HCV proteins for translocation of viral RNA genome to the polysomes for efficient translation and replication.
together, these data highlight the broad impact of Stau1 as a splicing regulator and suggest that Stau1 may act as a disease modifier in DM1.
expression of human Staufen1 is essential for proper dendritic arborisation during neuroblastoma cell differentiation, yet it is not necessary for maintenance of differentiated state, and suggest potential human Stauf1 mRNA targets involved in the process
The changing pattern of STAU distribution during meiotic maturation of human oocytes implicates a novel mechanism for the regulation of protein synthesis based on mRNA localization
in vivo atlas of mRNA secondary structures recognized by Staufen 1
TINCR, together with Staufen1, seems to stabilize a subset of mRNAs required for epidermal differentiation.
A common sequence signature consisting of two opposite-polarity Alu motifs was present in the hStau1-associated mRNAs and was shown to be sufficient for binding to hStau1 and hStau1-dependent stimulation of protein expression.
Staufen1 is an important factor in HCV replication and it might play a role early in the HCV replication cycle, rather than virion morphogenesis.
STAU1 binding to a 3'-UTR SBS was previously shown to trigger STAU1-mediated mRNA decay (SMD) by directly recruiting the ATP-dependent RNA helicase UPF1
These results suggest a new role for Staufen-1 as a cellular Rec and human endogenous retrovirus family HERV-K Gag cofactor.
STAU1 & STAU2 & ELAVL1 mRNAs & proteins were detected throughout cow preimplantation development from the germinal vesicle (GV) oocyte to the blastocyst stage; ELAVL2 mRNAs were detectable from the GV to the morula stage; ELAVL2 protein was in all stages
present in a ribonucleoprotein complex; associates with both a kinesin motor protein and vegetally localized RNAs Vg1 and VegT; results suggest a central role for Staufen in RNA localization in Xenopus oocytes
The findings suggest that cyclin B1 mRNA-Staufen1 protein complexes are transported toward the animal pole of zebrafish oocytes by the plus-end-directed motor protein Kinesin1 along microtubules, and that a common mRNA transport machinery functions in zebrafish and Xenopus oocytes, although its transport direction is opposite due to different organizations of microtubules.
Maternally expressed staufen is dispersed in the mature oocyte and early embryo. In the adult, staufen is expressed in specific brain nuclei, the testis, neurons and Leydig cells
stau1 is required for the survival and migration of primordial germ cells.
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.
staufen, RNA binding protein, homolog 1 (Drosophila)
, double-stranded RNA-binding protein Staufen homolog 1
, double-stranded RNA-binding protein Staufen homolog 1-like
, staufen, RNA binding protein, homolog 1
, Staufen 1
, RNA binding protein homolog
, staufen RNA binding protein homolog 1