Evidence map›Paper›PMID 21888622›Full record

ArticleThe Biochemical journal2012

A global survey of CRM1-dependent nuclear export sequences in the human deubiquitinase family.

Iraia García-Santisteban, Sonia Bañuelos, Jose A Rodríguez

Abstract read
PubMed Publisher
In one paragraph

Article in The Biochemical journal, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
1.5field-weighted citation impact, top 20% 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

24 citing papers in PubMed, 40 citations in OpenAlex.

  1. A Deep-Learning Atlas of XPO1-Mediated Nuclear Export at Proteome Scale.bioRxiv : the preprint server for biology · 2026
    Article
  2. Article
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  4. Article
  5. Review
  6. Article
  7. Article
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  9. Article
  10. Deubiquitinating enzyme USP3 controls CHK1 chromatin association and activation.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  11. Article
  12. Article
  13. Reply to Rodriguez: Mechanism of nuclear-cytosol shuttling of Usp12.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  14. Description of USP12 nuclear export sequence.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  15. Article
  16. Article
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  18. Review
  19. Article
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

Iraia García-SantistebanDepartment of Genetics, Physical Anthropology and Animal Physiology, University of the Basque Country UPV/EHU, B° Sarriena s/n, 48940 Leioa, Spain.
Sonia Bañuelos
Jose A Rodríguez
University of the Basque Country · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The mechanisms that regulate the nucleocytoplasmic localization of human deubiquitinases remain largely unknown. The nuclear export receptor CRM1 binds to specific amino acid motifs termed NESs (nuclear export sequences). By using in silico prediction and experimental validation of candidate sequences, we identified 32 active NESs and 78 inactive NES-like motifs in human deubiquitinases. These results allowed us to evaluate the performance of three programs widely used for NES prediction, and to add novel information to the recently redefined NES consensus. The novel NESs identified in the present study reveal a subset of 22 deubiquitinases bearing motifs that might mediate their binding to CRM1. We tested the effect of the CRM1 inhibitor LMB (leptomycin B) on the localization of YFP (yellow fluorescent protein)- or GFP (green fluorescent protein)-tagged versions of six NES-bearing deubiquitinases [USP (ubiquitin-specific peptidase) 1, USP3, USP7, USP21, CYLD (cylindromatosis) and OTUD7B (OTU-domain-containing 7B)]. YFP-USP21 and, to a lesser extent, GFP-OTUD7B relocated from the cytoplasm to the nucleus in the presence of LMB, revealing their nucleocytoplasmic shuttling capability. Two sequence motifs in USP21 had been identified during our survey as active NESs in the export assay. Using site-directed mutagenesis, we show that one of these motifs mediates USP21 nuclear export, whereas the second motif is not functional in the context of full-length USP21.

Indexed as

Active Transport, Cell NucleusAmino Acid MotifsAmino Acid SequenceBacterial ProteinsCloning, MolecularComputational BiologyEndopeptidasesExportin 1 ProteinGene Expression Regulation, EnzymologicGreen Fluorescent ProteinsHeLa CellsHumansKaryopherinsLuminescent ProteinsModels, MolecularPlasmidsBacterial ProteinsEndopeptidasesExportin 1 ProteinGreen Fluorescent ProteinsKaryopherinsLuminescent ProteinsProtein SubunitsReceptors, Cytoplasmic and Nuclearyellow fluorescent protein, Bacteria

Identifiers

PMID21888622
OpenAlexW1969932442

What OpenQuestion holds

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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.