The human cap-binding complex is functionally connected to the nuclear RNA exosome

Andersen, Peder; Domanski, Michal; Kristiansen, Maiken Søndergaard; Storvall, Helena; Ntini, Evgenia; Verheggen, Céline; Schein, Aleks; Bunkenborg, Jakob; Poser, Ina; Hallais, Marie; Sandberg, Rickard; Hyman, Anthony; LaCava, John; Rout, Michael P.; Andersen, Jens S.; Bertrand, Édouard; Jensen, Torben Heick

doi:10.1038/nsmb.2703

Cited by 210 publications

(374 citation statements)

References 55 publications

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“…This was demonstrated through proteomic analysis using immunoprecipitations of the machinery involved in these processes, and knockdown experiments of ARS2 or CBP20/80, which increases 3'-read-through transcripts for each of these RNA classes [10,11] . Interestingly, transcripts longer than ~1 kb were largely unaffected by ARS2 depletion with regards to 3'-read-through [10] , suggesting CBCA or a CBCA-interacting factor have a mechanism to limit their activity to promoter proximal areas.…”

Section: Ars2 and Transcription Terminationmentioning

confidence: 99%

“…interacts with SLBP and negative elongation factor (NELF) [6,11] . Meanwhile, mammalian ARS2 interacts with RDH RNA and FLICE-associated huge protein (FLASH) [9,54,61] .…”

Section: Ars2 and Replication-dependent Histone Rnamentioning

confidence: 99%

“…Immunoprecipitation of either ARS2 or CBP20/80 pulls down a substantially overlapping set of proteins, implying a strong functional overlap [10,11] . This is supported by loss-of-function experiments demonstrating ARS2 and CBP20/80 regulate similar transcripts, and phenotypically resemble one another [10,11] . This review will emphasize the interactions mediated by ARS2, for additional reviews on the CBC please see [24,25] .…”

Section: Introductionmentioning

confidence: 99%

“…Each of these RNA classes possess unique processing requirements. The interaction between the CBC and processing machinery is necessary for transcription termination, 3'-end formation, exosomal degradation, intranuclear transport, and export into the cytoplasm [2][3][4][5][6][7][8][9][10][11] . Precisely how the cap facilitates these disparate processes and discriminates between transcripts is not known.…”

Section: Introductionmentioning

confidence: 99%

“…Precisely how the cap facilitates these disparate processes and discriminates between transcripts is not known. The cap-binding protein, ARS2, is a scaffold that interacts constitutively with CBP20/80 and the 5'-end cap to form a complex called CBCA [8,10,11] , which mediates interactions between the cap complex and RNA 3'-end processing, shuttling, exosome, and export machinery. Thus, ARS2 is emerging as a critical factor, physically coupling multiple steps in the life of RNAP II transcripts.…”

Section: Introductionmentioning

confidence: 99%

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The Diverse Requirements of ARS2 in nuclear cap-binding complex-dependent RNA Processing

O’Sullivan

Howard

2016

RNA Dis

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ARS2 is a stable component of the nuclear cap-binding complex (CBC) and is critical for RNA Polymerase II transcript processing. Moreover, ARS2, and its orthologue SERRATE in plants, has been implicated in having a role in most established CBC-dependent functions. This review will provide insight into the functions of ARS2/SERRATE in numerous RNA Polymerase II transcript processing events, which happen co-transcriptionally from initiation to termination, and post-transcriptionally during maturation and export into the cytoplasm. Additionally, we will discuss what is known regarding ARS2/SERRATE structure in plants and in mammals.

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Section: Ars2 and Transcription Terminationmentioning

confidence: 99%

“…interacts with SLBP and negative elongation factor (NELF) [6,11] . Meanwhile, mammalian ARS2 interacts with RDH RNA and FLICE-associated huge protein (FLASH) [9,54,61] .…”

Section: Ars2 and Replication-dependent Histone Rnamentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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The Diverse Requirements of ARS2 in nuclear cap-binding complex-dependent RNA Processing

O’Sullivan

Howard

2016

RNA Dis

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Rrp6: Integrated roles in nuclear RNA metabolism and transcription termination

Fox

Mosley

2015

WIREs RNA

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The yeast RNA exosome is a eukaryotic ribonuclease complex essential for RNA processing, surveillance and turnover. It is comprised of a barrel-shaped core and cap as well as a 3’–5’ ribonuclease known as Dis3 which contains both endo- and exonuclease domains. A second exonuclease, Rrp6, is added in the nucleus. Dis3 and Rrp6 have both shared and distinct roles in RNA metabolism, and this review will focus primarily on Rrp6 and the roles of the RNA exosome in the nucleus. The functions of the nuclear exosome are modulated by cofactors and interacting partners specific to each type of substrate. Generally, the cofactor TRAMP (Trf4/5-Air2/1-Mtr4 polyadenylation) complex helps unwind unstable RNAs, RNAs requiring processing such as rRNAs, tRNAs, or snRNAs or improperly processed RNAs and direct it toward the exosome. In yeast, Rrp6 interacts with Nrd1, the cap binding complex (CBC), and RNA Polymerase II to aid in nascent RNA processing, termination, and polyA tail length regulation. Recent studies have shown that proper termination and processing of short, non-coding RNAs by Rrp6 is particularly important for transcription regulation across the genome and has important implications for regulation of diverse processes at the cellular level. Loss of proper Rrp6 and exosome activity may contribute to various pathologies such as autoimmune disease, neurological disorders, and cancer.

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Writing a wrong: Coupled RNA polymerase II transcription and RNA quality control

et al. 2019

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Processing and maturation of precursor RNA species is coupled to RNA polymerase II transcription. Co‐transcriptional RNA processing helps to ensure efficient and proper capping, splicing, and 3′ end processing of different RNA species to help ensure quality control of the transcriptome. Many improperly processed transcripts are not exported from the nucleus, are restricted to the site of transcription, and are in some cases degraded, which helps to limit any possibility of aberrant RNA causing harm to cellular health. These critical quality control pathways are regulated by the highly dynamic protein–protein interaction network at the site of transcription. Recent work has further revealed the extent to which the processes of transcription and RNA processing and quality control are integrated, and how critically their coupling relies upon the dynamic protein interactions that take place co‐transcriptionally. This review focuses specifically on the intricate balance between 3′ end processing and RNA decay during transcription termination. This article is categorized under: RNA Turnover and Surveillance > Turnover/Surveillance Mechanisms RNA Processing > 3' End Processing RNA Processing > Splicing Mechanisms RNA Processing > Capping and 5' End Modifications

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The human cap-binding complex is functionally connected to the nuclear RNA exosome

Cited by 210 publications

References 55 publications

The Diverse Requirements of ARS2 in nuclear cap-binding complex-dependent RNA Processing

The Diverse Requirements of ARS2 in nuclear cap-binding complex-dependent RNA Processing

Rrp6: Integrated roles in nuclear RNA metabolism and transcription termination

Writing a wrong: Coupled RNA polymerase II transcription and RNA quality control

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