Evidence map›Paper›PMID 17412707›Full record

ArticleNucleic acids research2007

C1D and hMtr4p associate with the human exosome subunit PM/Scl-100 and are involved in pre-rRNA processing.

Geurt Schilders, Erwin van Dijk, Ger J M Pruijn

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 84 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
84citing papers in PubMed, 1 pooled it
3.6field-weighted citation impact, top 7% 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

84 citing papers in PubMed, 1 synthesis or guideline pooled it, 131 citations in OpenAlex.

  1. Pooled it
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  15. Substrate discrimination and quality control require each catalytic activity of TRAMP and the nuclear RNA exosome.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  16. Review
  17. Article
  18. Review
  19. Regulation of human telomerase in homeostasis and disease.Nature reviews. Molecular cell biology · 2020
    Review
  20. Article

24 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

3 authors at 2 institutions in 1 country.

Geurt SchildersDepartment of Biomolecular Chemistry, Nijmegen Center for Molecular Life Sciences, Institute for Molecules and Materials, Radboud University Nijmegen, Nijmegen, The Netherlands.
Erwin van Dijk
Ger J M Pruijn
Radboud University Nijmegen · NLRadboud Institute for Molecular Life Sciences · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The exosome is a complex of 3'-5' exoribonucleases and RNA-binding proteins, which is involved in processing or degradation of different classes of RNA. Previously, the characterization of purified exosome complexes from yeast and human cells suggested that C1D and KIAA0052/hMtr4p are associated with the exosome and thus might regulate its functional activities. Subcellular localization experiments demonstrated that C1D and KIAA0052/hMtr4p co-localize with exosome subunit PM/Scl-100 in the nucleoli of HEp-2 cells. Additionally, the nucleolar accumulation of C1D appeared to be dependent on PM/Scl-100. Protein-protein interaction studies showed that C1D binds to PM/Scl-100, whereas KIAA0052/hMtr4p was found to interact with MPP6, a previously identified exosome-associated protein. Moreover, we demonstrate that C1D, MPP6 and PM/Scl-100 form a stable trimeric complex in vitro. Knock-down of C1D, MPP6 and KIAA0052/hMtr4p by RNAi resulted in the accumulation of 3'-extended 5.8S rRNA precursors, showing that these proteins are required for rRNA processing. Interestingly, C1D appeared to contain RNA-binding activity with a potential preference for structured RNAs. Taken together, our results are consistent with a role for the exosome-associated proteins C1D, MPP6 and KIAA052/hMtr4p in the recruitment of the exosome to pre-rRNA to mediate the 3' end processing of the 5.8S rRNA.

Indexed as

RNA 3' End ProcessingCell LineCell NucleolusCo-Repressor ProteinsExoribonucleasesExosome Multienzyme Ribonuclease ComplexHumansNuclear ProteinsRepressor ProteinsRNA-Binding ProteinsRNA HelicasesRNA PrecursorsRNA, Ribosomal, 5.8SC1D protein, humanCo-Repressor ProteinsExoribonucleasesEXOSC10 protein, humanExosome Multienzyme Ribonuclease ComplexM-phase phosphoprotein 6, humanMTREX protein, humanNuclear ProteinsRepressor ProteinsRNA-Binding ProteinsRNA HelicasesRNA PrecursorsRNA, Ribosomal, 5.8S

Identifiers

PMID17412707
PMCPMC1885644
OpenAlexW1999721918

What OpenQuestion holds

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LicenceCC BY-NC
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.