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Transcriptome reprogramming via Tob2-promoted global mRNA turnover

ABSTRACT: We found that multilayered phosphorylation of human Tob2 modulates its PABP-binding ability to change global deadenylation and mRNA turnover, which in turn reprograms transcriptome to influence cell proliferation.

ORGANISM(S): Homo sapiens

PROVIDER: GSE149684 | GEO | 2020/08/26

REPOSITORIES: GEO

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Transcriptome reprogramming via Tob2-promoted global mRNA turnover

Project description:We found that multilayered phosphorylation of human Tob2 modulates its PABP-binding ability to change global deadenylation and mRNA turnover, which in turn reprograms transcriptome to influence cell proliferation.

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Transcriptome reprogramming via Tob2-promoted global mRNA turnover

Project description:Transcriptome reprogramming via Tob2-promoted global mRNA turnover

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Transcriptome reprogramming via Tob2-promoted global mRNA turnover

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Spt6 association with RNAPII directs mRNA turnover during transcription

Project description:Spt6 is an essential histone chaperone that mediates nucleosome reassembly during gene transcription. Spt6 interacts with elongating RNA polymerase II (RNAPII) via a tandem Src2 homology (tSH2) domain, but it is not known whether this particular interaction is required for the nucleosome reassembly activity of Spt6. Here, we show that Spt6 recruitment to genes and its nucleosome reassembly functions are largely independent of association with RNAPII. Instead, the Spt6-RNAPII association is required for post-transcriptional mRNA turnover. Mechanistically, association of Spt6 with RNAPII couples the Ccr4-Not complex to the transcribed regions of genes, which we show regulates the timely deadenylation and degradation of a broad range of mRNAs including those required for cell cycle progression. Thus, our findings reveal an unexpected control mechanism for mRNA turnover facilitated by a histone chaperone during transcription.

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Project description:Gene expression is tightly regulated at the levels of both mRNA translation and stability. The poly(A) binding protein (PABP) plays a role in regulating these processes by binding the mRNA 3´ poly(A) tail and interfacing with both the translation initiation and mRNA deadenylation machineries. Here we directly investigate the impact of PABP on the translation and stability of endogenous mRNAs in human cell lines. Remarkably, our transcriptome-wide analysis does not generally detect changes to mRNA translation in PABP-depleted cells. In contrast, rapidly depleting PABP alters transcriptome abundance and stability, albeit non-uniformly. Transcripts with long half-lives and short 3’UTRs are preferentially depleted in PABP-depleted cells. PABP depletion induces cell death; however, disrupting the mRNA decapping and 5’-3’ decay machinery can partially suppress this lethality. Finally, we show that disrupting the LSM1-7 complex prevents the premature decay of mRNAs that are destabilized in PABP-depleted cells. Taken together, these findings suggest that PABP plays an important role in preventing the untimely decay of select mRNA populations in human cells.

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NF-kB regulator Bcl3 modulates bone density and turnover

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Rnase L reprograms translation by widespread mRNA turnover escaped by antiviral mRNAs

Project description:In response to foreign and endogenous double-stranded RNA (dsRNA), protein kinase R (PKR) and ribonuclease L (RNase L) reprogram translation in mammalian cells. PKR inhibits translation initiation through eIF2 phosphorylation, which triggers stress granule (SG) formation and promotes translation of stress responsive mRNAs. The mechanisms of RNase L-driven translation repression, its contribution to SG assembly, and its regulation of dsRNA stress-induced mRNAs are unknown. We demonstrate that RNase L drives translational shut-off in response to dsRNA by promoting widespread turnover of mRNAs. This alters stress granule assembly and reprograms translation by only allowing for the translation of mRNAs resistant to RNase L degradation, including numerous antiviral mRNAs such as IFN- . Individual cells differentially activate dsRNA responses revealing variation that can affect cellular outcomes. This identifies bulk mRNA degradation and the resistance of antiviral mRNAs as the mechanism by which RNaseL reprograms translation in response to dsRNA.

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Rnase L reprograms translation by widespread mRNA turnover escaped by antiviral mRNAs

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MITOCHONDRIAL Akt REGULATION OF HYPOXIC METABOLIC REPROGRAMMING

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