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The RNA Exosome Adaptor ZFC3H1 Functionally Competes with Nuclear Export Activity to Retain Target Transcripts

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The RNA Exosome Adaptor ZFC3H1 Functionally Competes with Nuclear Export Activity to Retain Target Transcripts. / Silla, Toomas; Karadoulama, Evdoxia; Mąkosa, Dawid; Lubas, Michal; Jensen, Torben Heick.

In: Cell Reports, Vol. 23, No. 7, 15.05.2018, p. 2199-2210.

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

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Silla, Toomas ; Karadoulama, Evdoxia ; Mąkosa, Dawid ; Lubas, Michal ; Jensen, Torben Heick. / The RNA Exosome Adaptor ZFC3H1 Functionally Competes with Nuclear Export Activity to Retain Target Transcripts. In: Cell Reports. 2018 ; Vol. 23, No. 7. pp. 2199-2210.

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@article{d6b700882c8a40b2b35eb3582a9815c7,
title = "The RNA Exosome Adaptor ZFC3H1 Functionally Competes with Nuclear Export Activity to Retain Target Transcripts",
abstract = "Mammalian genomes are promiscuously transcribed, yielding protein-coding and non-coding products. Many transcripts are short lived due to their nuclear degradation by the ribonucleolytic RNA exosome. Here, we show that abolished nuclear exosome function causes the formation of distinct nuclear foci, containing polyadenylated (pA + ) RNA secluded from nucleocytoplasmic export. We asked whether exosome co-factors could serve such nuclear retention. Co-localization studies revealed the enrichment of pA + RNA foci with “pA-tail exosome targeting (PAXT) connection” components MTR4, ZFC3H1, and PABPN1 but no overlap with known nuclear structures such as Cajal bodies, speckles, paraspeckles, or nucleoli. Interestingly, ZFC3H1 is required for foci formation, and in its absence, selected pA + RNAs, including coding and non-coding transcripts, are exported to the cytoplasm in a process dependent on the mRNA export factor AlyREF. Our results establish ZFC3H1 as a central nuclear pA + RNA retention factor, counteracting nuclear export activity. Silla et al. report that the RNA exosome adaptor protein ZFC3H1 acts as a nuclear RNA retention factor. In the absence of ZFC3H1, exosome targets are exported to the cytoplasm in a AlyREF-dependent manner. The discovery establishes ZFC3H1 as a central factor in the retention and degradation of polyadenylated RNA.",
keywords = "AlyREF, MTR4, RNA aggregates, RNA exosome, ZFC3H1, nuclear RNA decay, nuclear RNA retention, nuclear export",
author = "Toomas Silla and Evdoxia Karadoulama and Dawid Mąkosa and Michal Lubas and Jensen, {Torben Heick}",
note = "Copyright {\circledC} 2018 The Author(s). Published by Elsevier Inc. All rights reserved.",
year = "2018",
month = "5",
day = "15",
doi = "10.1016/j.celrep.2018.04.061",
language = "English",
volume = "23",
pages = "2199--2210",
journal = "Cell Reports",
issn = "2211-1247",
publisher = "Cell Press",
number = "7",

}

RIS

TY - JOUR

T1 - The RNA Exosome Adaptor ZFC3H1 Functionally Competes with Nuclear Export Activity to Retain Target Transcripts

AU - Silla, Toomas

AU - Karadoulama, Evdoxia

AU - Mąkosa, Dawid

AU - Lubas, Michal

AU - Jensen, Torben Heick

N1 - Copyright © 2018 The Author(s). Published by Elsevier Inc. All rights reserved.

PY - 2018/5/15

Y1 - 2018/5/15

N2 - Mammalian genomes are promiscuously transcribed, yielding protein-coding and non-coding products. Many transcripts are short lived due to their nuclear degradation by the ribonucleolytic RNA exosome. Here, we show that abolished nuclear exosome function causes the formation of distinct nuclear foci, containing polyadenylated (pA + ) RNA secluded from nucleocytoplasmic export. We asked whether exosome co-factors could serve such nuclear retention. Co-localization studies revealed the enrichment of pA + RNA foci with “pA-tail exosome targeting (PAXT) connection” components MTR4, ZFC3H1, and PABPN1 but no overlap with known nuclear structures such as Cajal bodies, speckles, paraspeckles, or nucleoli. Interestingly, ZFC3H1 is required for foci formation, and in its absence, selected pA + RNAs, including coding and non-coding transcripts, are exported to the cytoplasm in a process dependent on the mRNA export factor AlyREF. Our results establish ZFC3H1 as a central nuclear pA + RNA retention factor, counteracting nuclear export activity. Silla et al. report that the RNA exosome adaptor protein ZFC3H1 acts as a nuclear RNA retention factor. In the absence of ZFC3H1, exosome targets are exported to the cytoplasm in a AlyREF-dependent manner. The discovery establishes ZFC3H1 as a central factor in the retention and degradation of polyadenylated RNA.

AB - Mammalian genomes are promiscuously transcribed, yielding protein-coding and non-coding products. Many transcripts are short lived due to their nuclear degradation by the ribonucleolytic RNA exosome. Here, we show that abolished nuclear exosome function causes the formation of distinct nuclear foci, containing polyadenylated (pA + ) RNA secluded from nucleocytoplasmic export. We asked whether exosome co-factors could serve such nuclear retention. Co-localization studies revealed the enrichment of pA + RNA foci with “pA-tail exosome targeting (PAXT) connection” components MTR4, ZFC3H1, and PABPN1 but no overlap with known nuclear structures such as Cajal bodies, speckles, paraspeckles, or nucleoli. Interestingly, ZFC3H1 is required for foci formation, and in its absence, selected pA + RNAs, including coding and non-coding transcripts, are exported to the cytoplasm in a process dependent on the mRNA export factor AlyREF. Our results establish ZFC3H1 as a central nuclear pA + RNA retention factor, counteracting nuclear export activity. Silla et al. report that the RNA exosome adaptor protein ZFC3H1 acts as a nuclear RNA retention factor. In the absence of ZFC3H1, exosome targets are exported to the cytoplasm in a AlyREF-dependent manner. The discovery establishes ZFC3H1 as a central factor in the retention and degradation of polyadenylated RNA.

KW - AlyREF

KW - MTR4

KW - RNA aggregates

KW - RNA exosome

KW - ZFC3H1

KW - nuclear RNA decay

KW - nuclear RNA retention

KW - nuclear export

UR - http://www.scopus.com/inward/record.url?scp=85046620862&partnerID=8YFLogxK

U2 - 10.1016/j.celrep.2018.04.061

DO - 10.1016/j.celrep.2018.04.061

M3 - Journal article

C2 - 29768216

VL - 23

SP - 2199

EP - 2210

JO - Cell Reports

JF - Cell Reports

SN - 2211-1247

IS - 7

ER -