The RNA-Binding Protein Rasputin/G3BP Enhances the Stability and Translation of Its Target mRNAs
Summary: G3BP RNA-binding proteins are important components of stress granules (SGs). Here, we analyze the role of the Drosophila G3BP Rasputin (RIN) in unstressed cells, where RIN is not SG associated. Immunoprecipitation followed by microarray analysis identifies over 550 mRNAs that copurify with...
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| Format: | Article |
| Language: | English |
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Elsevier
2020-03-01
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| Series: | Cell Reports |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S2211124720302345 |
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doaj-9faf1f277a61420f88079b33d872a60a |
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Article |
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DOAJ |
| language |
English |
| format |
Article |
| sources |
DOAJ |
| author |
John D. Laver Jimmy Ly Allison K. Winn Angelo Karaiskakis Sichun Lin Kun Nie Giulia Benic Nima Jaberi-Lashkari Wen Xi Cao Alireza Khademi J. Timothy Westwood Sachdev S. Sidhu Quaid Morris Stephane Angers Craig A. Smibert Howard D. Lipshitz |
| spellingShingle |
John D. Laver Jimmy Ly Allison K. Winn Angelo Karaiskakis Sichun Lin Kun Nie Giulia Benic Nima Jaberi-Lashkari Wen Xi Cao Alireza Khademi J. Timothy Westwood Sachdev S. Sidhu Quaid Morris Stephane Angers Craig A. Smibert Howard D. Lipshitz The RNA-Binding Protein Rasputin/G3BP Enhances the Stability and Translation of Its Target mRNAs Cell Reports |
| author_facet |
John D. Laver Jimmy Ly Allison K. Winn Angelo Karaiskakis Sichun Lin Kun Nie Giulia Benic Nima Jaberi-Lashkari Wen Xi Cao Alireza Khademi J. Timothy Westwood Sachdev S. Sidhu Quaid Morris Stephane Angers Craig A. Smibert Howard D. Lipshitz |
| author_sort |
John D. Laver |
| title |
The RNA-Binding Protein Rasputin/G3BP Enhances the Stability and Translation of Its Target mRNAs |
| title_short |
The RNA-Binding Protein Rasputin/G3BP Enhances the Stability and Translation of Its Target mRNAs |
| title_full |
The RNA-Binding Protein Rasputin/G3BP Enhances the Stability and Translation of Its Target mRNAs |
| title_fullStr |
The RNA-Binding Protein Rasputin/G3BP Enhances the Stability and Translation of Its Target mRNAs |
| title_full_unstemmed |
The RNA-Binding Protein Rasputin/G3BP Enhances the Stability and Translation of Its Target mRNAs |
| title_sort |
rna-binding protein rasputin/g3bp enhances the stability and translation of its target mrnas |
| publisher |
Elsevier |
| series |
Cell Reports |
| issn |
2211-1247 |
| publishDate |
2020-03-01 |
| description |
Summary: G3BP RNA-binding proteins are important components of stress granules (SGs). Here, we analyze the role of the Drosophila G3BP Rasputin (RIN) in unstressed cells, where RIN is not SG associated. Immunoprecipitation followed by microarray analysis identifies over 550 mRNAs that copurify with RIN. The mRNAs found in SGs are long and translationally silent. In contrast, we find that RIN-bound mRNAs, which encode core components of the transcription, splicing, and translation machinery, are short, stable, and highly translated. We show that RIN is associated with polysomes and provide evidence for a direct role for RIN and its human homologs in stabilizing and upregulating the translation of their target mRNAs. We propose that when cells are stressed, the resulting incorporation of RIN/G3BPs into SGs sequesters them away from their short target mRNAs. This would downregulate the expression of these transcripts, even though they are not incorporated into stress granules. : Laver et al. show that in early embryos, Rasputin, the Drosophila G3BP ortholog, binds short mRNAs and is associated with polysomes. They provide evidence for a direct role for Rasputin and its human homologs in stabilizing and upregulating the translation of their target mRNAs. Keywords: RNA-binding protein, post-transcriptional regulation, mRNA translation, mRNA stability, stress granule, Drosophila, embryo, G3BP, Rasputin |
| url |
http://www.sciencedirect.com/science/article/pii/S2211124720302345 |
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doaj-9faf1f277a61420f88079b33d872a60a2020-11-25T01:40:39ZengElsevierCell Reports2211-12472020-03-01301033533367.e7The RNA-Binding Protein Rasputin/G3BP Enhances the Stability and Translation of Its Target mRNAsJohn D. Laver0Jimmy Ly1Allison K. Winn2Angelo Karaiskakis3Sichun Lin4Kun Nie5Giulia Benic6Nima Jaberi-Lashkari7Wen Xi Cao8Alireza Khademi9J. Timothy Westwood10Sachdev S. Sidhu11Quaid Morris12Stephane Angers13Craig A. Smibert14Howard D. Lipshitz15Department of Molecular Genetics, University of Toronto, 661 University Avenue, Toronto, ON M5G 1M1, CanadaDepartment of Molecular Genetics, University of Toronto, 661 University Avenue, Toronto, ON M5G 1M1, Canada; Department of Biochemistry, University of Toronto, 661 University Avenue, Toronto, ON M5G 1M1, CanadaDepartment of Biochemistry, University of Toronto, 661 University Avenue, Toronto, ON M5G 1M1, CanadaDepartment of Molecular Genetics, University of Toronto, 661 University Avenue, Toronto, ON M5G 1M1, CanadaDepartment of Pharmaceutical Sciences, University of Toronto, 144 College Street, Toronto, ON M5S 3M2, CanadaDepartment of Molecular Genetics, University of Toronto, 661 University Avenue, Toronto, ON M5G 1M1, CanadaDepartment of Molecular Genetics, University of Toronto, 661 University Avenue, Toronto, ON M5G 1M1, CanadaDepartment of Molecular Genetics, University of Toronto, 661 University Avenue, Toronto, ON M5G 1M1, Canada; Department of Biochemistry, University of Toronto, 661 University Avenue, Toronto, ON M5G 1M1, CanadaDepartment of Molecular Genetics, University of Toronto, 661 University Avenue, Toronto, ON M5G 1M1, CanadaDepartment of Molecular Genetics, University of Toronto, 661 University Avenue, Toronto, ON M5G 1M1, CanadaDepartment of Biology, University of Toronto, 3359 Mississauga, Mississauga, ON L5L 1C6, CanadaDepartment of Molecular Genetics, University of Toronto, 661 University Avenue, Toronto, ON M5G 1M1, Canada; Donnelly Centre, University of Toronto, 160 College Street, Toronto, ON M5S 3E1, CanadaDepartment of Molecular Genetics, University of Toronto, 661 University Avenue, Toronto, ON M5G 1M1, Canada; Donnelly Centre, University of Toronto, 160 College Street, Toronto, ON M5S 3E1, Canada; Vector Institute, 661 University Ave, Toronto, Ontario, Canada, M160 College Street, Toronto, ON M5G 1M1, CanadaDepartment of Biochemistry, University of Toronto, 661 University Avenue, Toronto, ON M5G 1M1, Canada; Department of Pharmaceutical Sciences, University of Toronto, 144 College Street, Toronto, ON M5S 3M2, CanadaDepartment of Molecular Genetics, University of Toronto, 661 University Avenue, Toronto, ON M5G 1M1, Canada; Department of Biochemistry, University of Toronto, 661 University Avenue, Toronto, ON M5G 1M1, Canada; Corresponding authorDepartment of Molecular Genetics, University of Toronto, 661 University Avenue, Toronto, ON M5G 1M1, Canada; Corresponding authorSummary: G3BP RNA-binding proteins are important components of stress granules (SGs). Here, we analyze the role of the Drosophila G3BP Rasputin (RIN) in unstressed cells, where RIN is not SG associated. Immunoprecipitation followed by microarray analysis identifies over 550 mRNAs that copurify with RIN. The mRNAs found in SGs are long and translationally silent. In contrast, we find that RIN-bound mRNAs, which encode core components of the transcription, splicing, and translation machinery, are short, stable, and highly translated. We show that RIN is associated with polysomes and provide evidence for a direct role for RIN and its human homologs in stabilizing and upregulating the translation of their target mRNAs. We propose that when cells are stressed, the resulting incorporation of RIN/G3BPs into SGs sequesters them away from their short target mRNAs. This would downregulate the expression of these transcripts, even though they are not incorporated into stress granules. : Laver et al. show that in early embryos, Rasputin, the Drosophila G3BP ortholog, binds short mRNAs and is associated with polysomes. They provide evidence for a direct role for Rasputin and its human homologs in stabilizing and upregulating the translation of their target mRNAs. Keywords: RNA-binding protein, post-transcriptional regulation, mRNA translation, mRNA stability, stress granule, Drosophila, embryo, G3BP, Rasputinhttp://www.sciencedirect.com/science/article/pii/S2211124720302345 |