Evidence map›Paper›PMID 31363146›Full record

ArticleScientific reports2019

A protein-RNA interaction atlas of the ribosome biogenesis factor AATF.

Rainer W J Kaiser, Michael Ignarski, Eric L Van Nostrand, Christian K Frese, Manaswita Jain, Sadrija Cukoski, Heide Heinen, Melanie Schaechter, Lisa Seufert, Konstantin Bunte and 12 more

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.4field-weighted citation impact, top 19% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

14 citing papers in PubMed, 27 citations in OpenAlex.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

22 authors at 5 institutions in 2 countries.

Rainer W J KaiserDepartment II of Internal Medicine and Center for Molecular Medicine Cologne, University of Cologne, Faculty of Medicine and University Hospital of Cologne, 50937, Cologne, Germany.ORCID http://orcid.org/0000-0003-1750-3395
Michael IgnarskiDepartment II of Internal Medicine and Center for Molecular Medicine Cologne, University of Cologne, Faculty of Medicine and University Hospital of Cologne, 50937, Cologne, Germany.ORCID http://orcid.org/0000-0001-6057-7694
Eric L Van NostrandDepartment of Cellular and Molecular Medicine, University of California at San Diego, La Jolla, CA, USA.
Christian K FreseProteomics Core Facility, Cologne Excellence Cluster on Cellular Stress Responses in Aging-associated Diseases (CECAD), University of Cologne, 50931, Cologne, Germany.
Manaswita JainDepartment II of Internal Medicine and Center for Molecular Medicine Cologne, University of Cologne, Faculty of Medicine and University Hospital of Cologne, 50937, Cologne, Germany.
Sadrija CukoskiDepartment II of Internal Medicine and Center for Molecular Medicine Cologne, University of Cologne, Faculty of Medicine and University Hospital of Cologne, 50937, Cologne, Germany.
Heide HeinenDepartment II of Internal Medicine and Center for Molecular Medicine Cologne, University of Cologne, Faculty of Medicine and University Hospital of Cologne, 50937, Cologne, Germany.
Melanie SchaechterDepartment II of Internal Medicine and Center for Molecular Medicine Cologne, University of Cologne, Faculty of Medicine and University Hospital of Cologne, 50937, Cologne, Germany.
Lisa SeufertDepartment II of Internal Medicine and Center for Molecular Medicine Cologne, University of Cologne, Faculty of Medicine and University Hospital of Cologne, 50937, Cologne, Germany.
Konstantin BunteDepartment II of Internal Medicine and Center for Molecular Medicine Cologne, University of Cologne, Faculty of Medicine and University Hospital of Cologne, 50937, Cologne, Germany.
Peter FrommoltBioinformatics Core Facility, Cologne Excellence Cluster on Cellular Stress Responses in Aging-associated Diseases (CECAD), University of Cologne, 50931, Cologne, Germany.
Patrick KellerInstitute of Pharmacy and Biochemistry, Johannes Gutenberg-University Mainz, Staudingerweg 5, 55128, Mainz, Germany.
Mark HelmInstitute of Pharmacy and Biochemistry, Johannes Gutenberg-University Mainz, Staudingerweg 5, 55128, Mainz, Germany.
Katrin BohlDepartment II of Internal Medicine and Center for Molecular Medicine Cologne, University of Cologne, Faculty of Medicine and University Hospital of Cologne, 50937, Cologne, Germany.
Martin HöhneDepartment II of Internal Medicine and Center for Molecular Medicine Cologne, University of Cologne, Faculty of Medicine and University Hospital of Cologne, 50937, Cologne, Germany.
Bernhard SchermerDepartment II of Internal Medicine and Center for Molecular Medicine Cologne, University of Cologne, Faculty of Medicine and University Hospital of Cologne, 50937, Cologne, Germany.ORCID http://orcid.org/0000-0002-5194-9000
Thomas BenzingDepartment II of Internal Medicine and Center for Molecular Medicine Cologne, University of Cologne, Faculty of Medicine and University Hospital of Cologne, 50937, Cologne, Germany.
Katja HöpkerDepartment II of Internal Medicine and Center for Molecular Medicine Cologne, University of Cologne, Faculty of Medicine and University Hospital of Cologne, 50937, Cologne, Germany.
Christoph DieterichGerman Center for Cardiovascular Research (DZHK), Partner site Heidelberg/Mannheim, Im Neuenheimer Feld 669, 69120, Heidelberg, Germany.
Gene W YeoDepartment of Cellular and Molecular Medicine, University of California at San Diego, La Jolla, CA, USA.
Roman-Ulrich MüllerDepartment II of Internal Medicine and Center for Molecular Medicine Cologne, University of Cologne, Faculty of Medicine and University Hospital of Cologne, 50937, Cologne, Germany. roman-ulrich.mueller@uk-koeln.de.ORCID http://orcid.org/0000-0001-6910-0745
Francesca FabrettiDepartment II of Internal Medicine and Center for Molecular Medicine Cologne, University of Cologne, Faculty of Medicine and University Hospital of Cologne, 50937, Cologne, Germany.
University of Cologne · DEJohannes Gutenberg University Mainz · DEUniversity of California San Diego · USInstitute of Bioinformatics and Systems Biology · DETH Köln - University of Applied Sciences · DE

Funding

Comprhensive analysis of functional RNA elements encoded in the human genomeU54HG007005 · NHGRI · UNIVERSITY OF CONNECTICUT SCH OF MED/DNT · PI GRAVELEY, BRENTON R. · 2012 to 2017
$12.5M
Defining the messenger RNP code in the brainR01NS075449 · NINDS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI YEO, EUGENE WEI-MING · 2012 to 2016
$3.0M
Robust, high-throughput identification of RNA processing regulators and regulatory networks genome-wideR00HG009530 · NHGRI · BAYLOR COLLEGE OF MEDICINE · PI VAN NOSTRAND, ERIC LYMAN · 2020 to 2022
$747k
Robust, high-throughput identification of RNA processing regulators and regulatory networks genome-wideK99HG009530 · NHGRI · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI VAN NOSTRAND, ERIC LYMAN · 2017 to 2018
$250k
NHGRI NIH HHS K99 HG009530NHGRI NIH HHS R00 HG009530NHGRI NIH HHS U54 HG007005NINDS NIH HHS R01 NS075449
6 · The paper itself

Abstract

AATF is a central regulator of the cellular outcome upon p53 activation, a finding that has primarily been attributed to its function as a transcription factor. Recent data showed that AATF is essential for ribosome biogenesis and plays a role in rRNA maturation. AATF has been implicated to fulfil this role through direct interaction with rRNA and was identified in several RNA-interactome capture experiments. Here, we provide a first comprehensive analysis of the RNA bound by AATF using CLIP-sequencing. Interestingly, this approach shows predominant binding of the 45S pre-ribosomal RNA precursor molecules. Furthermore, AATF binds to mRNAs encoding for ribosome biogenesis factors as well as snoRNAs. These findings are complemented by an in-depth analysis of the protein interactome of AATF containing a large set of proteins known to play a role in rRNA maturation with an emphasis on the protein-RNA-complexes known to be required for the generation of the small ribosomal subunit (SSU). In line with this finding, the binding sites of AATF within the 45S rRNA precursor localize in close proximity to the SSU cleavage sites. Consequently, our multilayer analysis of the protein-RNA interactome of AATF reveals this protein to be an important hub for protein and RNA interactions involved in ribosome biogenesis.

Indexed as

AnimalsApoptosis Regulatory ProteinsBinding SitesCell LineHEK293 CellsHumansMiceProtein BindingRepressor ProteinsRibosomal ProteinsRibosomesRibosome Subunits, SmallRNA PrecursorsAATF protein, humanApoptosis Regulatory ProteinsRepressor ProteinsRibosomal ProteinsRNA Precursors

Identifiers

PMID31363146
PMCPMC6667500
OpenAlexW2965176945

What OpenQuestion holds

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.