Evidence map›Paper›PMID 26867678›Full record

ArticleNature communications2016

SIRT7-dependent deacetylation of the U3-55k protein controls pre-rRNA processing.

Sifan Chen, Maximilian Felix Blank, Aishwarya Iyer, Bingding Huang, Lin Wang, Ingrid Grummt, Renate Voit

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 79 papers.

0numbers the graph read from it
0cells of the map it votes in
79citing papers in PubMed
7.5field-weighted citation impact, top 2% 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

79 citing papers in PubMed, 123 citations in OpenAlex.

  1. Review
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  13. SIRT3/6/7: promising therapeutic targets for pulmonary fibrosis.Frontiers in cell and developmental biology · 2025
    Review
  14. Review
  15. The dark side of SIRT7.Molecular and cellular biochemistry · 2024
    Review
  16. Article
  17. Article
  18. Review
  19. Review
  20. Review

19 more citing papers are in PubMed but not listed here.

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

7 authors at 3 institutions in 1 country.

Sifan ChenDivision of Molecular Biology of the Cell II, German Cancer Research Center, DKFZ-ZMBH Alliance, Im Neuenheimer Fed 581, 69120 Heidelberg, Germany.
Maximilian Felix BlankDivision of Molecular Biology of the Cell II, German Cancer Research Center, DKFZ-ZMBH Alliance, Im Neuenheimer Fed 581, 69120 Heidelberg, Germany.
Aishwarya IyerDivision of Molecular Biology of the Cell II, German Cancer Research Center, DKFZ-ZMBH Alliance, Im Neuenheimer Fed 581, 69120 Heidelberg, Germany.
Bingding HuangDivision of Theoretical Bioinformatics, German Cancer Research Center, 69120 Heidelberg, Germany.
Lin WangGenomics and Proteomics Core Facility, German Cancer Research Center, 69120 Heidelberg, Germany.
Ingrid GrummtDivision of Molecular Biology of the Cell II, German Cancer Research Center, DKFZ-ZMBH Alliance, Im Neuenheimer Fed 581, 69120 Heidelberg, Germany.
Renate VoitDivision of Molecular Biology of the Cell II, German Cancer Research Center, DKFZ-ZMBH Alliance, Im Neuenheimer Fed 581, 69120 Heidelberg, Germany.
Heidelberg University · DEDKFZ-ZMBH Alliance · DEGerman Cancer Research Center · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

SIRT7 is an NAD(+)-dependent protein deacetylase with important roles in ribosome biogenesis and cell proliferation. Previous studies have established that SIRT7 is associated with RNA polymerase I, interacts with pre-ribosomal RNA (rRNA) and promotes rRNA synthesis. Here we show that SIRT7 is also associated with small nucleolar RNP (snoRNPs) that are involved in pre-rRNA processing and rRNA maturation. Knockdown of SIRT7 impairs U3 snoRNA dependent early cleavage steps that are necessary for generation of 18S rRNA. Mechanistically, SIRT7 deacetylates U3-55k, a core component of the U3 snoRNP complex, and reversible acetylation of U3-55k modulates the association of U3-55k with U3 snoRNA. Deacetylation by SIRT7 enhances U3-55k binding to U3 snoRNA, which is a prerequisite for pre-rRNA processing. Under stress conditions, SIRT7 is released from nucleoli, leading to hyperacetylation of U3-55k and attenuation of pre-rRNA processing. The results reveal a multifaceted role of SIRT7 in ribosome biogenesis, regulating both transcription and processing of rRNA.

Indexed as

Blotting, NorthernBlotting, WesternCell Line, TumorChromatin ImmunoprecipitationFluorescent Antibody TechniqueGene Knockdown TechniquesGene Knockout TechniquesHEK293 CellsHumansImmunoprecipitationIn Vitro TechniquesRibonucleoproteins, Small NucleolarRNA PrecursorsRNA Processing, Post-TranscriptionalRNA, Ribosomal, 18SRNA, Small NucleolarRibonucleoproteins, Small Nucleolarribonucleoprotein, U3 small nucleolarRNA PrecursorsRNA, Ribosomal, 18SRNA, Small NucleolarSIRT7 protein, humanSirtuins

Identifiers

PMID26867678
PMCPMC4754350
OpenAlexW2260059766

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

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.