scholarly journals Cis-acting determinants of asymmetric, cytoplasmic RNA transport

RNA ◽  
2007 ◽  
Vol 13 (5) ◽  
pp. 625-642 ◽  
Author(s):  
A. Jambhekar ◽  
J. L. DeRisi
Keyword(s):  
Rna Transport ◽  
Cis Acting ◽  
Cytoplasmic Rna

scholarly journals PTB/hnRNP I Is Required for RNP Remodeling during RNA Localization in Xenopus Oocytes

2007 ◽  
Vol 28 (2) ◽  
pp. 678-686 ◽  
Author(s):  
Raymond A. Lewis ◽  
James A. Gagnon ◽  
Kimberly L. Mowry
Keyword(s):  
Protein Interactions ◽  
Xenopus Oocytes ◽  
Rna Binding ◽  
Rna Binding Proteins ◽  
Rna Localization ◽  
Rna Transport ◽  
Rna Sequences ◽  
Cytoplasmic Rna ◽  
Embryonic Polarity ◽  
Specific Mrnas

ABSTRACT Transport of specific mRNAs to defined regions within the cell cytoplasm is a fundamental mechanism for regulating cell and developmental polarity. In the Xenopus oocyte, Vg1 RNA is transported to the vegetal cytoplasm, where localized expression of the encoded protein is critical for embryonic polarity. The Vg1 localization pathway is directed by interactions between key motifs within Vg1 RNA and protein factors recognizing those RNA sequences. We have investigated how RNA-protein interactions could be modulated to trigger distinct steps in the localization pathway and found that the Vg1 RNP is remodeled during cytoplasmic RNA transport. Our results implicate two RNA-binding proteins with key roles in Vg1 RNA localization, PTB/hnRNP I and Vg1RBP/vera, in this process. We show that PTB/hnRNP I is required for remodeling of the interaction between Vg1 RNA and Vg1RBP/vera. Critically, mutations that block this remodeling event also eliminate vegetal localization of the RNA, suggesting that RNP remodeling is required for localization.

scholarly journals Importance of mammalian nuclear-envelope nucleoside triphosphatase in nucleo-cytoplasmic transport of ribonucleoproteins

1979 ◽  
Vol 182 (3) ◽  
pp. 811-819 ◽  
Author(s):  
P S Agutter ◽  
B McCaldin ◽  
H J McArdle
Keyword(s):  
Ionic Strength ◽  
Substrate Specificity ◽  
Nuclear Envelope ◽  
Nucleoside Triphosphate ◽  
Rna Transport ◽  
Isolated Nuclei ◽  
Cytoplasmic Rna ◽  
Cytoplasmic Transport ◽  
Nucleoside Triphosphatase

The nucleoside triphosphate-stimulated efflux of RNA from isolated nuclei was studied under a range of conditions, and the effects of these conditions on the process were compared with the properties of the nucleoside triphosphatase located in the pore complex. A marked similarity between the rate of efflux and the rate of nucleoside triphosphate hydrolysis was apparent, in terms of substrate specificity, sensitivity to treatment with insolubilized trypsin, kinetics and the effects of increased ionic strength and of many inhibitors. These results are taken, in view of earlier evidence, to suggest that the activity of the nucleoside triphosphatase is a prerequisite for nucleo-cytoplasmic RNA transport in vivo. There are some indications that the nuclear-envelope lipid is also involved in regulating the efflux process.

A cytoplasmic protein that promotes nucleo-cytoplasmic RNA transport in rat liver

1983 ◽  
Vol 11 (4) ◽  
pp. 371-371 ◽  
Author(s):  
ALEXANDER R. McDONALD ◽  
CHARLES A. STEWART ◽  
CHARLES D. GLEED ◽  
PAUL S. AGUTTER
Keyword(s):  
Rat Liver ◽  
Cytoplasmic Protein ◽  
Rna Transport ◽  
Cytoplasmic Rna

Some features of nucleo-cytoplasmic RNA transport from isolated nuclei

1981 ◽  
Vol 7 (1-3) ◽  
pp. 25-30 ◽  
Author(s):  
A. V. Peskin ◽  
Y. M. Koen ◽  
I. B. Zbarsky
Keyword(s):  
Rna Transport ◽  
Isolated Nuclei ◽  
Cytoplasmic Rna

scholarly journals Multiple Kinesin Motors Coordinate Cytoplasmic RNA Transport on a Subpopulation of Microtubules in Xenopus Oocytes

2008 ◽  
Vol 15 (3) ◽  
pp. 426-436 ◽  
Author(s):  
Timothy J. Messitt ◽  
James A. Gagnon ◽  
Jill A. Kreiling ◽  
Catherine A. Pratt ◽  
Young J. Yoon ◽  
...  
Keyword(s):  
Xenopus Oocytes ◽  
Rna Transport ◽  
Cytoplasmic Rna

scholarly journals REVERSIBLE, THERMOTROPIC ALTERATION OF NUCLEAR MEMBRANE STRUCTURE AND NUCLEOCYTOPLASMIC RNA TRANSPORT IN TETRAHYMENA

1974 ◽  
Vol 61 (3) ◽  
pp. 633-640 ◽  
Author(s):  
Frank Wunderlich ◽  
Werner Batz ◽  
Volker Speth ◽  
Donald F. H. Wallach
Keyword(s):  
Nuclear Membrane ◽  
Growth Temperature ◽  
Nuclear Pore ◽  
Lipid Phase ◽  
Rna Transport ◽  
Optimum Growth ◽  
Whole Cells ◽  
Uridine Incorporation ◽  
Optimum Growth Temperature ◽  
Cytoplasmic Rna

We examine the effect of cooling upon the freeze-etch ultrastructure of nuclear membranes, as well as upon nucleocytoplasmic RNA transport in the unicellular eukaryote Tetrahymena pyriformis. Chilling produces smooth, particle-free areas on both faces of the two freeze-fractured macronuclear membranes. Upon return to optimum growth temperature the membrane-associated particles revert to their normal uniform distribution and the smooth areas disappear. Chilling lowers the incorporation of [14C]uridine into whole cells and their cytoplasmic RNA. Cooling from the optimum growth temperature of 28° to 18°C (or above) decreases [14C]uridine incorporation into cells more than into their cytoplasmic RNA; chilling to below 18°C but above 10°C causes the reverse. [14C]Uridine incorporation into whole cells and their cytoplasmic RNA reflects overall RNA synthesis and nucleocytoplasmic RNA transport, respectively. RNA transport decreases strongly between 20° and 16°C, which is also the temperature range where morphologically detectable nuclear membrane transitions occur. This suggests that the nuclear envelope limits the rate of nucleocytoplasmic RNA transport at low temperatures. We hypothesize that a thermotropic lipid phase transition switches nuclear pore complexes from an "open" to a "closed" state with respect to nucleocytoplasmic RNA transport.

scholarly journals Flanking sequences regulate the toxicity, non-ATG translation, and aggregation of RNA with tandem CAG Repeats

2021 ◽  
Author(s):  
Michael R. Das ◽  
Yeonji Chang ◽  
Reuben Saunders ◽  
Nan Zhang ◽  
Colson Tomberlin ◽  
...  
Keyword(s):  
Nuclear Export ◽  
Binding Proteins ◽  
Rna Binding ◽  
Rna Binding Proteins ◽  
Cag Repeats ◽  
Cell Toxicity ◽  
Cis Acting ◽  
Cytoplasmic Rna ◽  
Flanking Sequences ◽  
Ran Translation

Nucleotide repeat-expansions cause several neurodegenerative disorders, including Huntington's disease and spinocerebellar ataxia. The expanded repeat-containing RNA transcribed from the affected loci agglomerate in the nucleus as pathogenic foci. Here we demonstrate that depending on their surrounding sequence context, RNAs with expanded CAG repeats can also undergo nuclear export and aggregate in the cytoplasm. Cytoplasmic aggregation of repeat-containing RNA coincides with several disease hallmarks, including repeat-associated non-AUG (RAN) translation, mislocalization of RNA binding proteins, and cell toxicity. Interestingly, the repeat-containing RNA co-aggregate with RAN translation products. Inhibition of RAN translation prevents cytoplasmic RNA aggregation and also alleviates cell toxicity. Our findings provide a cogent explanation for aberrant cytoplasmic localization of RNA binding proteins and implicate cis-acting flanking sequences in mediating RAN translation and disease.

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