Evidence map›Paper›PMID 17000757›Full record

ArticleMolecular and cellular biology2006

Nuclear localization signal and protein context both mediate importin alpha specificity of nuclear import substrates.

Beate Friedrich, Christina Quensel, Thomas Sommer, Enno Hartmann, Matthias Köhler

Abstract read
In one paragraph

Article in Molecular and cellular biology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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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

43 citing papers in PubMed.

  1. CanFrontiers in cellular and infection microbiology · 2025
    Article
  2. An arginine-rich nuclear localization signal (ArgiNLS) strategy for streamlined image segmentation of single cells.Proceedings of the National Academy of Sciences of the United States of America · 2024
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  12. Roles of the CSE1L-mediated nuclear import pathway in epigenetic silencing.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  13. Article
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  16. Nuclear-cytoplasmatic shuttling of proteins in control of cellular oxygen sensing.Journal of molecular medicine (Berlin, Germany) · 2015
    Review
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4 · The record

Corrections and comments

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5 · Who and what money

Authors and funding

5 authors.

Beate FriedrichThe Max Delbrueck Center for Molecular Medicine, Robert Roessle Strasse 10, 13125 Berlin, Germany.
Christina Quensel
Thomas Sommer
Enno Hartmann
Matthias Köhler

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The "classical" nuclear protein import pathway depends on importin alpha and importin beta. Importin alpha binds nuclear localization signal (NLS)-bearing proteins and functions as an adapter to access the importin beta-dependent import pathway. In humans, only one importin beta is known to interact with importin alpha, while six alpha importins have been described. Various experimental approaches provided evidence that several substrates are transported specifically by particular alpha importins. Whether the NLS is sufficient to mediate importin alpha specificity is unclear. To address this question, we exchanged the NLSs of two well-characterized import substrates, the seven-bladed propeller protein RCC1, preferentially transported into the nucleus by importin alpha3, and the less specifically imported substrate nucleoplasmin. In vitro binding studies and nuclear import assays revealed that both NLS and protein context contribute to the specificity of importin alpha binding and transport.

Indexed as

Active Transport, Cell Nucleusalpha KaryopherinsBiological TransportCell Cycle ProteinsCell NucleusEscherichia coliGlutathione TransferaseGuanine Nucleotide Exchange FactorsHeLa CellsHumansNuclear Localization SignalsNuclear ProteinsNucleoplasminsPhosphoproteinsProteinsRecombinant Fusion Proteinsalpha KaryopherinsCell Cycle ProteinsGlutathione TransferaseGuanine Nucleotide Exchange FactorsNuclear Localization SignalsNuclear ProteinsNucleoplasminsPhosphoproteinsProteinsRCC1 protein, humanRecombinant Fusion Proteins

Identifiers

PMID17000757
PMCPMC1636818

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Registered trials

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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.