Evidence map›Paper›PMID 28637748›Full record

ArticleThe Journal of cell biology2017

Impaired spliceosomal UsnRNP assembly leads to Sm mRNA down-regulation and Sm protein degradation.

Archana Bairavasundaram Prusty, Rajyalakshmi Meduri, Bhupesh Kumar Prusty, Jens Vanselow, Andreas Schlosser, Utz Fischer

Abstract read
In one paragraph

Article in The Journal of cell biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
2.5field-weighted citation impact, top 11% 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

26 citing papers in PubMed, 43 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Non-targeting control for MISSION shRNA library silencesMolecular therapy. Nucleic acids · 2021
    Article
  12. Article
  13. Review
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article
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

6 authors at 1 institution in 2 countries.

Archana Bairavasundaram PrustyDepartment of Biochemistry, Biocenter, University of Würzburg, Am Hubland, Würzburg, Germany.
Rajyalakshmi MeduriDepartment of Biochemistry, Biocenter, University of Würzburg, Am Hubland, Würzburg, Germany.
Bhupesh Kumar PrustyDepartment of Microbiology, Biocenter, University of Würzburg, Am Hubland, Würzburg, Germany.ORCID 0000-0001-7051-4670
Jens VanselowRudolf Virchow Center for Experimental Biomedicine, University of Würzburg, Würzburg, Germany.
Andreas SchlosserRudolf Virchow Center for Experimental Biomedicine, University of Würzburg, Würzburg, Germany.ORCID 0000-0003-0612-9932
Utz FischerDepartment of Biochemistry, Biocenter, University of Würzburg, Am Hubland, Würzburg, Germany utz.fischer@biozentrum.uni-wuerzburg.de.ORCID 0000-0002-1465-6591
University of Würzburg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Specialized assembly factors facilitate the formation of many macromolecular complexes in vivo. The formation of Sm core structures of spliceosomal U-rich small nuclear ribonucleoprotein particles (UsnRNPs) requires assembly factors united in protein arginine methyltransferase 5 (PRMT5) and survival motor neuron (SMN) complexes. We demonstrate that perturbations of this assembly machinery trigger complex cellular responses that prevent aggregation of unassembled Sm proteins. Inactivation of the SMN complex results in the initial tailback of Sm proteins on the PRMT5 complex, followed by down-regulation of their encoding mRNAs. In contrast, reduction of pICln, a PRMT5 complex subunit, leads to the retention of newly synthesized Sm proteins on ribosomes and their subsequent lysosomal degradation. Overexpression of Sm proteins under these conditions results in a surplus of Sm proteins over pICln, promoting their aggregation. Our studies identify an elaborate safeguarding system that prevents individual Sm proteins from aggregating, contributing to cellular UsnRNP homeostasis.

Indexed as

AutophagyDown-RegulationHeLa CellsHumansIon ChannelsLysosomesMolecular ChaperonesPhosphorylationProtein AggregatesProtein-Arginine N-MethyltransferasesProtein StabilityProteolysisRibonucleoproteins, Small NuclearRNA InterferenceRNA, MessengerRNA StabilityCLNS1A protein, humanIon ChannelsMolecular ChaperonesPRMT5 protein, humanProtein AggregatesProtein-Arginine N-MethyltransferasesRibonucleoproteins, Small NuclearRNA, MessengerSMN Complex Proteins

Identifiers

PMID28637748
PMCPMC5551706
OpenAlexW2672461416

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.