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anti-Mouse (Murine) STAU1 Antikörper:
anti-Human STAU1 Antikörper:
anti-Rat (Rattus) STAU1 Antikörper:
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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 (zeige CFL1 Antikörper)-1 targets Staufen and Fasciclin II (zeige NCAM2 Antikörper) (FasII), identified through larval brain ChIP-Seq for Adf (zeige CFL1 Antikörper)-1, is negatively regulated by Adf (zeige CFL1 Antikörper)-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.
Miranda has a role in coupling oskar mRNA/Staufen complexes to the bicoid mRNA localization pathway
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 (zeige MYC Antikörper) 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 (zeige UPF1 Antikörper) to elicit rapid mRNA degradation.
Dvl2 (zeige DVL2 Antikörper) has an inhibitory role in myogenesis and Stau1 coordinates myogenesis through the regulation of Dvl2 (zeige DVL2 Antikörper) mRNA.
Expression of Stau1 in the mouse hippocampus is modulated by a sequence variant (B2 SINE indel) in the 3' UTR (zeige UTS2R Antikörper) of Comt (catechol-O-methyltransferase (zeige COMT Antikörper)).
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.
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 (zeige PKLR Antikörper)-mediated inhibition of eIF2alpha (zeige EIF2A Antikörper), 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 (zeige ARHGEF16 Antikörper) 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.
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 (zeige UTS2R Antikörper) SBS (zeige CYLD Antikörper) was previously shown to trigger STAU1-mediated mRNA decay (SMD) by directly recruiting the ATP-dependent RNA helicase (zeige DDX52 Antikörper) UPF1 (zeige UPF1 Antikörper)
STAU1 & STAU2 & ELAVL1 (zeige ELAVL1 Antikörper) mRNAs & proteins were detected throughout cow preimplantation development (zeige MTA2 Antikörper) from the germinal vesicle (GV) oocyte to the blastocyst stage; ELAVL2 (zeige ELAVL2 Antikörper) mRNAs were detectable from the GV to the morula stage; ELAVL2 (zeige ELAVL2 Antikörper) protein was in all stages
present in a ribonucleoprotein complex; associates with both a kinesin motor protein (zeige KIF16B Antikörper) and vegetally localized RNAs Vg1 and VegT; results suggest a central role for Staufen in RNA localization in Xenopus oocytes
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