Cell Reports
Volume 30, Issue 10, 10 March 2020, Pages 3353-3367.e7
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Article
The RNA-Binding Protein Rasputin/G3BP Enhances the Stability and Translation of Its Target mRNAs

https://doi.org/10.1016/j.celrep.2020.02.066Get rights and content
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Highlights

  • In early embryos, the Drosophila G3BP Rasputin (RIN) is polysome associated

  • RIN binds over 550 mRNAs, which are short, stable, and highly translated

  • In rin mutants, steady-state levels of its target mRNAs are reduced

  • Tethering RIN or human G3BPs enhances the expression of a luciferase reporter mRNA

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.

Keywords

RNA-binding protein
post-transcriptional regulation
mRNA translation
mRNA stability
stress granule
Drosophila
embryo
G3BP
Rasputin

Cited by (0)

7

Present address: Department of Cell and Systems Biology, University of Toronto, 25 Harbord Street, Toronto, ON M5S 3G5, Canada

8

Present address: Department of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139, USA

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