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Elife. 2018 Oct 3;7. pii: e37663. doi: 10.7554/eLife.37663.

Changes in mRNA abundance drive shuttling of RNA binding proteins, linking cytoplasmic RNA degradation to transcription.

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Department of Molecular and Cell Biology, University of California, Berkeley, United States.
Department of Molecular Biology, Princeton University, Princeton, United States.
Department of Plant & Microbial Biology, University of California, Berkeley, United States.
Howard Hughes Medical Institute, United States.


Alterations in global mRNA decay broadly impact multiple stages of gene expression, although signals that connect these processes are incompletely defined. Here, we used tandem mass tag labeling coupled with mass spectrometry to reveal that changing the mRNA decay landscape, as frequently occurs during viral infection, results in subcellular redistribution of RNA binding proteins (RBPs) in human cells. Accelerating Xrn1-dependent mRNA decay through expression of a gammaherpesviral endonuclease drove nuclear translocation of many RBPs, including poly(A) tail-associated proteins. Conversely, cells lacking Xrn1 exhibited changes in the localization or abundance of numerous factors linked to mRNA turnover. Using these data, we uncovered a new role for relocalized cytoplasmic poly(A) binding protein in repressing recruitment of TATA binding protein and RNA polymerase II to promoters. Collectively, our results show that changes in cytoplasmic mRNA decay can directly impact protein localization, providing a mechanism to connect seemingly distal stages of gene expression.


RNA Polymerase II; RNA binding proteins; RNA decay; chromosomes; gene expression; human; infectious disease; microbiology; mouse; viruses

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