Staufen recruitment into stress granules does not affect early mRNA transport in oligodendrocytes
Staufen is a conserved double-stranded RNA-binding protein required for mRNA localization in Drosophila oocytes and embryos. The mammalian homologues Staufen 1 and Staufen 2 have been implicated in dendritic RNA targeting in neurons. Here we show that in rodent oligodendrocytes, these two proteins a...
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todo:paper_10591524_v16_n1_p405_Thomas2023-10-03T16:01:01Z Staufen recruitment into stress granules does not affect early mRNA transport in oligodendrocytes Thomas, M.G. Tosar, L.J.M. Loschi, M. Pasquini, J.M. Correale, J. Kindler, S. Boccaccio, G.L. HuR protein messenger RNA myelin polyadenylic acid binding protein protein staufen 1 protein staufen 2 protein tiar RNA binding protein unclassified drug animal cell article cell granule microfilament microtubule nonhuman nucleotide sequence oligodendroglia polysome priority journal protein targeting rat RNA transport stress Alternative Splicing Animals Animals, Newborn Biological Transport Blotting, Western Brain Cloning, Molecular Computer Simulation Cytoplasm In Situ Hybridization, Fluorescence Microfilaments Microscopy, Confocal Microscopy, Fluorescence Microtubules Models, Genetic Myelin Sheath Oligodendroglia Oxidative Stress Polyribosomes Protein Structure, Tertiary Rats Rats, Sprague-Dawley Ribonucleases Ribosomes RNA RNA, Double-Stranded RNA, Messenger RNA-Binding Proteins Animalia Mammalia Rodentia Staufen is a conserved double-stranded RNA-binding protein required for mRNA localization in Drosophila oocytes and embryos. The mammalian homologues Staufen 1 and Staufen 2 have been implicated in dendritic RNA targeting in neurons. Here we show that in rodent oligodendrocytes, these two proteins are present in two independent sets of RNA granules located at the distal myelinating processes. A third kind of RNA granules lacks Staufen and contains major myelin mRNAs. Myelin Staufen granules associate with microfilaments and microtubules, and their subcellular distribution is affected by polysome-disrupting drugs. Under oxidative stress, both Staufen 1 and Staufen 2 are recruited into stress granules (SGs), which are stress-induced organelles containing transiently silenced messengers. Staufen SGs contain the poly(A)-binding protein (PABP), the RNA-binding proteins HuR and TIAR, and small but not large ribosomal subunits. Staufen recruitment into perinuclear SGs is paralleled by a similar change in the overall localization of polyadenylated RNA. Under the same conditions, the distribution of recently transcribed and exported mRNAs is not affected. Our results indicate that Staufen 1 and Staufen 2 are novel and ubiquitous SG components and suggest that Staufen RNPs are involved in repositioning of most polysomal mRNAs, but not of recently synthesized transcripts, during the stress response. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_10591524_v16_n1_p405_Thomas |
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Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
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Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
HuR protein messenger RNA myelin polyadenylic acid binding protein protein staufen 1 protein staufen 2 protein tiar RNA binding protein unclassified drug animal cell article cell granule microfilament microtubule nonhuman nucleotide sequence oligodendroglia polysome priority journal protein targeting rat RNA transport stress Alternative Splicing Animals Animals, Newborn Biological Transport Blotting, Western Brain Cloning, Molecular Computer Simulation Cytoplasm In Situ Hybridization, Fluorescence Microfilaments Microscopy, Confocal Microscopy, Fluorescence Microtubules Models, Genetic Myelin Sheath Oligodendroglia Oxidative Stress Polyribosomes Protein Structure, Tertiary Rats Rats, Sprague-Dawley Ribonucleases Ribosomes RNA RNA, Double-Stranded RNA, Messenger RNA-Binding Proteins Animalia Mammalia Rodentia |
| spellingShingle |
HuR protein messenger RNA myelin polyadenylic acid binding protein protein staufen 1 protein staufen 2 protein tiar RNA binding protein unclassified drug animal cell article cell granule microfilament microtubule nonhuman nucleotide sequence oligodendroglia polysome priority journal protein targeting rat RNA transport stress Alternative Splicing Animals Animals, Newborn Biological Transport Blotting, Western Brain Cloning, Molecular Computer Simulation Cytoplasm In Situ Hybridization, Fluorescence Microfilaments Microscopy, Confocal Microscopy, Fluorescence Microtubules Models, Genetic Myelin Sheath Oligodendroglia Oxidative Stress Polyribosomes Protein Structure, Tertiary Rats Rats, Sprague-Dawley Ribonucleases Ribosomes RNA RNA, Double-Stranded RNA, Messenger RNA-Binding Proteins Animalia Mammalia Rodentia Thomas, M.G. Tosar, L.J.M. Loschi, M. Pasquini, J.M. Correale, J. Kindler, S. Boccaccio, G.L. Staufen recruitment into stress granules does not affect early mRNA transport in oligodendrocytes |
| topic_facet |
HuR protein messenger RNA myelin polyadenylic acid binding protein protein staufen 1 protein staufen 2 protein tiar RNA binding protein unclassified drug animal cell article cell granule microfilament microtubule nonhuman nucleotide sequence oligodendroglia polysome priority journal protein targeting rat RNA transport stress Alternative Splicing Animals Animals, Newborn Biological Transport Blotting, Western Brain Cloning, Molecular Computer Simulation Cytoplasm In Situ Hybridization, Fluorescence Microfilaments Microscopy, Confocal Microscopy, Fluorescence Microtubules Models, Genetic Myelin Sheath Oligodendroglia Oxidative Stress Polyribosomes Protein Structure, Tertiary Rats Rats, Sprague-Dawley Ribonucleases Ribosomes RNA RNA, Double-Stranded RNA, Messenger RNA-Binding Proteins Animalia Mammalia Rodentia |
| description |
Staufen is a conserved double-stranded RNA-binding protein required for mRNA localization in Drosophila oocytes and embryos. The mammalian homologues Staufen 1 and Staufen 2 have been implicated in dendritic RNA targeting in neurons. Here we show that in rodent oligodendrocytes, these two proteins are present in two independent sets of RNA granules located at the distal myelinating processes. A third kind of RNA granules lacks Staufen and contains major myelin mRNAs. Myelin Staufen granules associate with microfilaments and microtubules, and their subcellular distribution is affected by polysome-disrupting drugs. Under oxidative stress, both Staufen 1 and Staufen 2 are recruited into stress granules (SGs), which are stress-induced organelles containing transiently silenced messengers. Staufen SGs contain the poly(A)-binding protein (PABP), the RNA-binding proteins HuR and TIAR, and small but not large ribosomal subunits. Staufen recruitment into perinuclear SGs is paralleled by a similar change in the overall localization of polyadenylated RNA. Under the same conditions, the distribution of recently transcribed and exported mRNAs is not affected. Our results indicate that Staufen 1 and Staufen 2 are novel and ubiquitous SG components and suggest that Staufen RNPs are involved in repositioning of most polysomal mRNAs, but not of recently synthesized transcripts, during the stress response. |
| format |
JOUR |
| author |
Thomas, M.G. Tosar, L.J.M. Loschi, M. Pasquini, J.M. Correale, J. Kindler, S. Boccaccio, G.L. |
| author_facet |
Thomas, M.G. Tosar, L.J.M. Loschi, M. Pasquini, J.M. Correale, J. Kindler, S. Boccaccio, G.L. |
| author_sort |
Thomas, M.G. |
| title |
Staufen recruitment into stress granules does not affect early mRNA transport in oligodendrocytes |
| title_short |
Staufen recruitment into stress granules does not affect early mRNA transport in oligodendrocytes |
| title_full |
Staufen recruitment into stress granules does not affect early mRNA transport in oligodendrocytes |
| title_fullStr |
Staufen recruitment into stress granules does not affect early mRNA transport in oligodendrocytes |
| title_full_unstemmed |
Staufen recruitment into stress granules does not affect early mRNA transport in oligodendrocytes |
| title_sort |
staufen recruitment into stress granules does not affect early mrna transport in oligodendrocytes |
| url |
http://hdl.handle.net/20.500.12110/paper_10591524_v16_n1_p405_Thomas |
| work_keys_str_mv |
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| _version_ |
1807315751714947072 |