Localization of a Human Double-Stranded RNA-Binding Protein Gene (STAU) to Band 20q13.1 by Fluorescencein SituHybridization

DesGroseillers, Luc; Lemieux, Nicole

doi:10.1006/geno.1996.0499

Cited by 13 publications

(10 citation statements)

References 7 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Recently, we showed by both Southern blot analysis of human DNA and fluorescent in situ hybridization on human chromosomes in metaphase that the human gene is present as a single copy in the human genome and is localized in the middle of the long arm of chromosome 20 (11). We now report the sequence of the hStau and mStau and show that the transcript is found in all tested tissues.…”

mentioning

confidence: 67%

Mammalian Staufen Is a Double-Stranded-RNA- and Tubulin-Binding Protein Which Localizes to the Rough Endoplasmic Reticulum

Wickham¹,

Duchaîne²,

Luo³

et al. 1999

Molecular and Cellular Biology

Self Cite

228

364

View full text Add to dashboard Cite

mentioning

confidence: 67%

Mammalian Staufen Is a Double-Stranded-RNA- and Tubulin-Binding Protein Which Localizes to the Rough Endoplasmic Reticulum

Wickham¹,

Duchaîne²,

Luo³

et al. 1999

Molecular and Cellular Biology

Self Cite

228

364

View full text Add to dashboard Cite

“…The use of a cDNA probe for in situ hybridization on mitotic spreads indicated a single-copy gene located at band 20q13.1 (11). We took advantage of the isolation of cDNAs corresponding to the thSTL clone to investigate the pattern of expression of hStaufen-like mRNAs and to study the RNA-binding properties and the intracellular localization of hStaufen-like protein.…”

Section: Discussionmentioning

confidence: 99%

A Human Sequence Homologue of Staufen Is an RNA-Binding Protein That Is Associated with Polysomes and Localizes to the Rough Endoplasmic Reticulum

Marión

Fortes

Beloso

et al. 1999

Molecular and Cellular Biology

164

184

View full text Add to dashboard Cite

In the course of a two-hybrid screen with the NS1 protein of influenza virus, a human clone capable of coding for a protein with high homology to the Staufen protein from Drosophila melanogaster (dmStaufen) was identified. With these sequences used as a probe, cDNAs were isolated from a cDNA library. The encoded protein (hStaufen-like) contained four double-stranded RNA (dsRNA)-binding domains with 55% similarity and 38% identity to those of dmStaufen, including identity at all residues involved in RNA binding. A recombinant protein containing all dsRNA-binding domains was expressed in Escherichia coli as a His-tagged polypeptide. It showed dsRNA binding activity in vitro, with an apparent K d of 10 ؊9 M. Using a specific antibody, we detected in human cells a major form of the hStaufen-like protein with an apparent molecular mass of 60 to 65 kDa. The intracellular localization of hStaufen-like protein was investigated by immunofluorescence using a series of markers for the cell compartments. Colocalization was observed with the rough endoplasmic reticulum but not with endosomes, cytoskeleton, or Golgi apparatus. Furthermore, sedimentation analyses indicated that hStaufen-like protein associates with polysomes. These results are discussed in relation to the possible functions of the protein.The establishment and maintenance of asymmetries in certain cells implies the localized expression of many proteins, a property often enhanced by the localization of the corresponding mRNAs (for reviews, see references 2 and 47). The relevance of mRNA localization at precise sites of the cell in the definition of polarity of developing embryos has been documented in both Drosophila melanogaster and Xenopus laevis. Thus, the positions of gurken and oskar mRNAs in the fly oocyte define its dorsoventral axis (36) and the location of the pole plasm at the posterior pole (15), respectively. Likewise, the localization of the bicoid and nanos mRNAs at the anterior and posterior poles of the embryo, respectively, leads to the generation of two opposing gradients of their protein products and ultimately to the definition of the head, thorax, and abdomen of the embryo (50). In the case of X. laevis, several mRNAs, such as Xcat2, Xcat3, and Xlsirt, are directed to the germ plasm (34), while others, such as Vg1 and Xwnt11, accumulate at the vegetal cortex (30). By analogy to the D. melanogaster genes, these mRNAs are thought to play a role in defining patterns in the X. laevis embryo. In fact, a region of the Xcat2 protein shows sequence homology to the zinc finger domain of nanos protein (34).The specific localization of certain mRNAs to precise sites within the cell is not an exclusive property of germ cells or developing embryos. A number of observations indicate that some of the mRNAs of somatic cells are also localized at different sites within the cell. Thus, myelin-binding protein is translated in oligodendrocytes from free ribosomes on localized mRNA (51), and the microtubule-associated protein MAP2 is translated preferentially i...

show abstract

“…Two proteins that are encoded by distinct genes, Staufen1 (Stau1) and Staufen2 (Stau2), have been identified as mammalian homologs of Staufen (DesGroseillers and Lemieux, 1996;Buchner et al, 1999 (Mallardo et al, 2003;Monshausen et al, 2004). Each isoform of Stau1 or Stau2 contains conserved dsRBDs.…”

Section: Staufenmentioning

confidence: 99%

The Role of Mammalian Staufen on mRNA Traffic: a View from Its Nucleocytoplasmic Shuttling Function

Miki

Takano

Yoneda

2005

Cell Struct. Funct.

View full text Add to dashboard Cite

ABSTRACT. The localization of mRNA in neuronal dendrites plays a role in both locally and temporally regulated protein synthesis, which is required for certain forms of synaptic plasticity. RNA granules constitute a dendritic mRNA transport machinery in neurons, which move along microtubules. RNA granules contain densely packed clusters of ribosomes, but lack some factors that are required for translation, suggesting that they are translationally incompetent. Recently some of the components of RNA granules have been identified, and their functions are in the process of being examined, in attempts to better understand the properties of RNA granules. Mammalian Staufen, a double-stranded RNA binding protein, is a component of RNA granules. Staufen is localized in the somatodendritic domain of neurons, and plays an important role in dendritic mRNA targeting. Recently, one of the mammalian homologs of Staufen, Staufen2 (Stau2), was shown to shuttle between the nucleus and the cytoplasm. This finding suggests the possibility that Stau2 binds RNA in the nucleus and that this ribonucleoprotein particle is transported from the nucleus to RNA granules in the cytoplasm. A closer study of this process might provide a clue to the mechanism by which RNA granules are formed.

show abstract

Localization of a Human Double-Stranded RNA-Binding Protein Gene (STAU) to Band 20q13.1 by Fluorescencein SituHybridization

Cited by 13 publications

References 7 publications

Mammalian Staufen Is a Double-Stranded-RNA- and Tubulin-Binding Protein Which Localizes to the Rough Endoplasmic Reticulum

Mammalian Staufen Is a Double-Stranded-RNA- and Tubulin-Binding Protein Which Localizes to the Rough Endoplasmic Reticulum

A Human Sequence Homologue of Staufen Is an RNA-Binding Protein That Is Associated with Polysomes and Localizes to the Rough Endoplasmic Reticulum

The Role of Mammalian Staufen on mRNA Traffic: a View from Its Nucleocytoplasmic Shuttling Function

Contact Info

Product

Resources

About