Evidence map›Paper›PMID 24103640›Full record

ArticleCell communication and signaling : CCS2013

Cold shock Y-box protein-1 proteolysis autoregulates its transcriptional activities.

Claudia R C van Roeyen, Florian G Scurt, Sabine Brandt, Vanessa A Kuhl, Sandra Martinkus, Sonja Djudjaj, Ute Raffetseder, Hans-Dieter Royer, Ioannis Stefanidis, Sandra E Dunn and 5 more

Open access · goldAbstract read
In one paragraph

Article in Cell communication and signaling : CCS, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
1.3field-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

25 citing papers in PubMed, 44 citations in OpenAlex.

  1. Article
  2. Review
  3. Y-box binding proteins in immunity and RNA virus infection.Microbiology and molecular biology reviews : MMBR · 2025
    Review
  4. Article
  5. Review
  6. YB-1 activating cascades as potential targets in KRAS-mutated tumors.Strahlentherapie und Onkologie : Organ der Deutschen Rontgengesellschaft ... [et al] · 2023
    Review
  7. Review
  8. YB-1 Phosphorylation at Serine 209 Inhibits Its Nuclear Translocation.International journal of molecular sciences · 2021
    Article
  9. Article
  10. Review
  11. Article
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  14. Article
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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

15 authors at 6 institutions in 3 countries.

Claudia R C van RoeyenDepartment of Nephrology and Hypertension, Diabetes and Endocrinology, Otto-von-Guericke University Magdeburg, Leipziger Str 44, 39120 Magdeburg, Germany. peter.mertens@med.ovgu.de.
Florian G Scurt
Sabine Brandt
Vanessa A Kuhl
Sandra Martinkus
Sonja Djudjaj
Ute Raffetseder
Hans-Dieter Royer
Ioannis Stefanidis
Sandra E Dunn
Steven Dooley
Honglei Weng
Thomas Fischer
Jonathan A Lindquist
Peter R Mertens
Otto-von-Guericke University Magdeburg · DERWTH Aachen University · DEHeidelberg University · DECenter of Advanced European Studies and Research · DEChild and Family Research Institute · CAUniversity of Thessaly · GR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundThe Y-box protein-1 (YB-1) fulfills pleiotropic functions relating to gene transcription, mRNA processing, and translation. It remains elusive how YB-1 shuttling into the nuclear and cytoplasmic compartments is regulated and whether limited proteolysis by the 20S proteasome releases fragments with distinct function(s) and subcellular distribution(s).

resultsTo address these questions, mapping of domains responsible for subcellular targeting was performed. Three nuclear localization signals (NLS) were identified. NLS-1 (aa 149-156) and NLS-2 (aa 185-194) correspond to residues with unknown function(s), whereas NLS-3 (aa 276-292) matches with a designated multimerization domain. Nuclear export signal(s) were not identified. Endoproteolytic processing by the 20S proteasome before glycine 220 releases a carboxy-terminal fragment (CTF), which localized to the nucleus, indicating that NLS-3 is operative. Genotoxic stress induced proteolytic cleavage and nuclear translocation of the CTF. Co-expression of the CTF and full-length YB-1 resulted in an abrogated transcriptional activation of the MMP-2 promoter, indicating an autoregulatory inhibitory loop, whereas it fulfilled similar trans-repressive effects on the collagen type I promoter.

conclusionCompartmentalization of YB-1 protein derivatives is controlled by distinct NLS, one of which targets a proteolytic cleavage product to the nucleus. We propose a model for an autoregulatory negative feedback loop that halts unlimited transcriptional activation.

Indexed as

AnimalsCell LineCell Line, TumorCells, CulturedHumansMesangial CellsNuclear Export SignalsNuclear Localization SignalsProtein Structure, TertiaryProteolysisRatsTranscription, GeneticY-Box-Binding Protein 1Nuclear Export SignalsNuclear Localization SignalsY-Box-Binding Protein 1

Identifiers

PMID24103640
PMCPMC3766096
OpenAlexW2108088462

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.