Evidence map›Paper›PMID 26200863›Full record

ArticleBiophysical journal2015

MD simulations and FRET reveal an environment-sensitive conformational plasticity of importin-β.

Kangkan Halder, Nicole Dölker, Qui Van, Ingo Gregor, Achim Dickmanns, Imke Baade, Ralph H Kehlenbach, Ralf Ficner, Jörg Enderlein, Helmut Grubmüller and 1 more

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.2field-weighted citation impact, top 21% 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

15 citing papers in PubMed, 28 citations in OpenAlex.

  1. Article
  2. Article
  3. Bayesian Nonparametrics for FRET using Realistic Integrative Detectors.bioRxiv : the preprint server for biology · 2025
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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

11 authors at 3 institutions in 1 country.

Kangkan HalderFree Floater (Junior) Research Group "Applied Synthetic Biology", Institute for Microbiology and Genetics, Georg-August University Göttingen, Göttingen, Germany.
Nicole DölkerDepartment of Theoretical and Computational Biophysics, Max-Planck Institute for Biophysical Chemistry, Göttingen, Germany.
Qui VanThird Institute of Physics-Biophysics, Georg-August University Göttingen, Göttingen, Germany.
Ingo GregorThird Institute of Physics-Biophysics, Georg-August University Göttingen, Göttingen, Germany.
Achim DickmannsInstitute for Microbiology and Genetics, Department of Molecular Structural Biology, Georg-August University Göttingen, Göttingen, Germany.
Imke BaadeDepartment of Molecular Biology, Faculty of Medicine, Georg-August University Göttingen, Göttingen, Germany.
Ralph H KehlenbachDepartment of Molecular Biology, Faculty of Medicine, Georg-August University Göttingen, Göttingen, Germany.
Ralf FicnerInstitute for Microbiology and Genetics, Department of Molecular Structural Biology, Georg-August University Göttingen, Göttingen, Germany.
Jörg EnderleinThird Institute of Physics-Biophysics, Georg-August University Göttingen, Göttingen, Germany.
Helmut GrubmüllerDepartment of Theoretical and Computational Biophysics, Max-Planck Institute for Biophysical Chemistry, Göttingen, Germany. Electronic address: hgrubmu@gwdg.de.
Heinz NeumannFree Floater (Junior) Research Group "Applied Synthetic Biology", Institute for Microbiology and Genetics, Georg-August University Göttingen, Göttingen, Germany. Electronic address: hneumann@uni-goettingen.de.
University of Göttingen · DEMax Planck Institute for Biophysical Chemistry · DEMax Planck Society · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The nuclear pore complex mediates nucleocytoplasmic transport of macromolecules in eukaryotic cells. Transport through the pore is restricted by a hydrophobic selectivity filter comprising disordered phenylalanine-glycine-rich repeats of nuclear pore proteins. Exchange through the pore requires specialized transport receptors, called exportins and importins, that interact with cargo proteins in a RanGTP-dependent manner. These receptors are highly flexible superhelical structures composed of HEAT-repeat motifs that adopt various degrees of extension in crystal structures. Here, we performed molecular-dynamics simulations using crystal structures of Importin-β in its free form or in complex with nuclear localization signal peptides as the starting conformation. Our simulations predicted that initially compact structures would adopt extended conformations in hydrophilic buffers, while contracted conformations would dominate in more hydrophobic solutions, mimicking the environment of the nuclear pore. We confirmed this experimentally by Förster resonance energy transfer experiments using dual-fluorophore-labeled Importin-β. These observations explain seemingly contradictory crystal structures and suggest a possible mechanism for cargo protection during passage of the nuclear pore. Such hydrophobic switching may be a general principle for environmental control of protein function.

Indexed as

beta KaryopherinsFluorescence Resonance Energy TransferHumansHydrophobic and Hydrophilic InteractionsMolecular Dynamics SimulationPliabilityProtein ConformationSolutionsSolventsWaterbeta KaryopherinsSolutionsSolventsWater

Identifiers

PMID26200863
PMCPMC4621615
OpenAlexW2098090751

What OpenQuestion holds

Textmetadata
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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.