The eukaryotic RNA exosome: Same scaffold but variable catalytic subunits

Lykke‐Andersen, Søren; Tomecki, Rafał; Jensen, Torben Heick; Dziembowski, Andrzej

doi:10.4161/rna.8.1.14237

Cited by 95 publications

(78 citation statements)

References 46 publications

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“…53 For example, the RNase exosome complex, which exists in both the nucleus and the cytoplasm, is involved in many types of RNA processing associated with nuclear-transcribed proteins, including mRNA decay. 54,55 The nine core proteins of this complex were observed exclusively in the nuclear fraction (Supporting Information Table 3). For the 13 proteins that are transcribed inas TSFM, TACO1, SLIRP and PUS1, 53 which we observed exclusively in the mitochondrial fraction (Supporting Information Table 3).…”

Section: Separation Of the Nuclear And Mitochondrial Fractionsmentioning

confidence: 99%

Spatial Distribution of Cellular Function: The Partitioning of Proteins between Mitochondria and the Nucleus in MCF7 Breast Cancer Cells

et al. 2012

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Section: Separation Of the Nuclear And Mitochondrial Fractionsmentioning

confidence: 99%

Spatial Distribution of Cellular Function: The Partitioning of Proteins between Mitochondria and the Nucleus in MCF7 Breast Cancer Cells

et al. 2012

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“…The eukaryotic exosome is composed of a core that is catalytically inactive (reviewed in Lorentzen et al, 2008;Januszyk and Lima, 2014). The RNases RRP6 (also known as EXOSC10 in mammals) and DIS3 (also known as RRP44) associate with this core and provide catalytic activity (reviewed by Lykke-Andersen et al, 2011). RRP6 and DIS3, however, have other interaction partners than the exosome core and can act independently of the exosome (Synowsky et al, 2009;Graham et al, 2009;Kiss and Andrulis, 2011).…”

Section: Introductionmentioning

confidence: 99%

RRP6/EXOSC10 is required for the repair of DNA double-strand breaks by homologous recombination

Marín-Vicente

Domingo-Prim

Eberle

et al. 2015

Journal of Cell Science

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The exosome acts on different RNA substrates and plays important roles in RNA metabolism. The fact that short non-coding RNAs are involved in the DNA damage response led us to investigate whether the exosome factor RRP6 of Drosophila melanogaster and its human ortholog EXOSC10 play a role in DNA repair. Here, we show that RRP6 and EXOSC10 are recruited to DNA double-strand breaks (DSBs) in S2 cells and HeLa cells, respectively. Depletion of RRP6/ EXOSC10 does not interfere with the phosphorylation of the histone variant H2Av (Drosophila) or H2AX (humans), but impairs the recruitment of the homologous recombination factor RAD51 to the damaged sites, without affecting RAD51 levels. The recruitment of RAD51 to DSBs in S2 cells is also inhibited by overexpression of RRP6-Y361A-V5, a catalytically inactive RRP6 mutant. Furthermore, cells depleted of RRP6 or EXOSC10 are more sensitive to radiation, which is consistent with RRP6/EXOSC10 playing a role in DNA repair. RRP6/EXOSC10 can be co-immunoprecipitated with RAD51, which links RRP6/EXOSC10 to the homologous recombination pathway. Taken together, our results suggest that the ribonucleolytic activity of RRP6/EXOSC10 is required for the recruitment of RAD51 to DSBs.

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“…This generates a transcript bearing a 59 monophosphate that is rapidly and processively degraded by the 59-to-39 exoribo-nuclease XRN1 (Chang et al 2011;Jinek et al 2011). Alternatively, proteins associated with the exosome complex attack the transcript exonucleolytically from the 39-to-59 direction (Lykke-Andersen et al 2011;Astuti et al 2012). XRN1-mediated decay is considered in many current models to be the major pathway of mRNA decay in cells (Stoecklin et al 2006), although it is clear that exosome-mediated 39-to-59 decay may also make a significant contribution (Murray and Schoenberg 2007).…”

Section: Introductionmentioning

confidence: 99%

A noncoding RNA produced by arthropod-borne flaviviruses inhibits the cellular exoribonuclease XRN1 and alters host mRNA stability

Moon

Anderson

Kumagai

et al. 2012

RNA

184

251

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All arthropod-borne flaviviruses generate a short noncoding RNA (sfRNA) from the viral 39 untranslated region during infection due to stalling of the cellular 59-to-39 exonuclease XRN1. We show here that formation of sfRNA also inhibits XRN1 activity. Cells infected with Dengue or Kunjin viruses accumulate uncapped mRNAs, decay intermediates normally targeted by XRN1. XRN1 repression also resulted in the increased overall stability of cellular mRNAs in flavivirus-infected cells. Importantly, a mutant Kunjin virus that cannot form sfRNA but replicates to normal levels failed to affect host mRNA stability or XRN1 activity. Expression of sfRNA in the absence of viral infection demonstrated that sfRNA formation was directly responsible for the stabilization of cellular mRNAs. Finally, numerous cellular mRNAs were differentially expressed in an sfRNA-dependent fashion in a Kunjin virus infection. We conclude that flaviviruses incapacitate XRN1 during infection and dysregulate host mRNA stability as a result of sfRNA formation.

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The eukaryotic RNA exosome: Same scaffold but variable catalytic subunits

Cited by 95 publications

References 46 publications

Spatial Distribution of Cellular Function: The Partitioning of Proteins between Mitochondria and the Nucleus in MCF7 Breast Cancer Cells

Spatial Distribution of Cellular Function: The Partitioning of Proteins between Mitochondria and the Nucleus in MCF7 Breast Cancer Cells

RRP6/EXOSC10 is required for the repair of DNA double-strand breaks by homologous recombination

A noncoding RNA produced by arthropod-borne flaviviruses inhibits the cellular exoribonuclease XRN1 and alters host mRNA stability

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