Evidence map›Paper›PMID 25656054›Full record

ReviewThe Biochemical journal2015

Diversification of importin-α isoforms in cellular trafficking and disease states.

Ruth A Pumroy, Gino Cingolani

Abstract readReview
In one paragraph

Review in The Biochemical journal, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 134 papers.

0numbers the graph read from it
0cells of the map it votes in
134citing papers in PubMed
–field-weighted citation impact
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

134 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Importin-9 recognizes the winged-helix fold of ETS transcription factors to mediate nuclear import.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
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  15. Article
  16. Article
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  18. Review
  19. Article
  20. Article

74 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

2 authors.

Ruth A Pumroy*Department of Biochemistry and Molecular Biology, Thomas Jefferson University, Philadelphia, PA 19107, U.S.A.
Gino Cingolani*Department of Biochemistry and Molecular Biology, Thomas Jefferson University, Philadelphia, PA 19107, U.S.A.

Funding

X-Ray Crystallography and Macromolecular CharacterizationP30CA056036 · NCI · THOMAS JEFFERSON UNIVERSITY · PI DANIEL P SILVER · 1995 to 2026
$94.8M
Multisubunit viral ATPases that couple ATP-hydrolysis to genome translocationR01GM100888 · NIGMS · THOMAS JEFFERSON UNIVERSITY · PI CINGOLANI, GINO · 2012 to 2020
$2.5M
Molecular Basis for Recognition and Nuclear Import of Non-classical NLS CargosR01GM074846 · NIGMS · UPSTATE MEDICAL UNIVERSITY · PI CINGOLANI, GINO · 2006 to 2010
$1.3M
Training Program in Cellular, Biochemical, and Molecular SciencesT32GM100836 · NIGMS · THOMAS JEFFERSON UNIVERSITY · PI BENOVIC, JEFFREY L · 2012 to 2016
$809k
NCI NIH HHS P30 CA056036NIGMS NIH HHS GM074846NIGMS NIH HHS R01 GM074846NIGMS NIH HHS R01 GM100888NIGMS NIH HHS T32 GM100836
6 · The paper itself

Abstract

The human genome encodes seven isoforms of importin α which are grouped into three subfamilies known as α1, α2 and α3. All isoforms share a fundamentally conserved architecture that consists of an N-terminal, autoinhibitory, importin-β-binding (IBB) domain and a C-terminal Arm (Armadillo)-core that associates with nuclear localization signal (NLS) cargoes. Despite striking similarity in amino acid sequence and 3D structure, importin-α isoforms display remarkable substrate specificity in vivo. In the present review, we look at key differences among importin-α isoforms and provide a comprehensive inventory of known viral and cellular cargoes that have been shown to associate preferentially with specific isoforms. We illustrate how the diversification of the adaptor importin α into seven isoforms expands the dynamic range and regulatory control of nucleocytoplasmic transport, offering unexpected opportunities for pharmacological intervention. The emerging view of importin α is that of a key signalling molecule, with isoforms that confer preferential nuclear entry and spatiotemporal specificity on viral and cellular cargoes directly linked to human diseases.

Indexed as

Active Transport, Cell Nucleusalpha KaryopherinsAnimalsCell NucleusGene Expression RegulationHost-Pathogen InteractionsHumansModels, MolecularNuclear Localization SignalsProtein BindingProtein IsoformsProtein Structure, TertiaryProtein TransportSignal TransductionViral ProteinsVirus Diseasesalpha KaryopherinsNuclear Localization SignalsProtein IsoformsViral Proteins

Identifiers

PMID25656054
PMCPMC4405237

What OpenQuestion holds

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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.