Evidence map›Paper›PMID 24478460›Full record

ArticleMolecular biology of the cell2014

Transportin acts to regulate mitotic assembly events by target binding rather than Ran sequestration.

Cyril Bernis, Beth Swift-Taylor, Matthew Nord, Sarah Carmona, Yuh Min Chook, Douglass J Forbes

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

18 citing papers in PubMed, 26 citations in OpenAlex.

  1. Structure, function and assembly of nuclear pore complexes.Nature reviews. Molecular cell biology · 2026
    Review
  2. Review
  3. Nuclear transport proteins: structure, function, and disease relevance.Signal transduction and targeted therapy · 2023
    Review
  4. Attenuated Viral Replication of AvianMicrobiology spectrum · 2022
    Article
  5. Review
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Mitotic spindle assembly in animal cells: a fine balancing act.Nature reviews. Molecular cell biology · 2017
    Review
  13. Review
  14. Article
  15. Nuclear transport factors: global regulation of mitosis.Current opinion in cell biology · 2015
    Review
  16. The Ran Pathway in Drosophila melanogaster Mitosis.Frontiers in cell and developmental biology · 2015
    Review
  17. Review
  18. Article
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

6 authors at 2 institutions in 1 country.

Cyril BernisSection of Cell and Developmental Biology, Division of Biological Sciences 0347, University of California-San Diego, La Jolla, CA 92093-0347 Department of Pharmacology, University of Texas Southwestern Medical Center, Dallas, TX 75390-9041.
Beth Swift-Taylor
Matthew Nord
Sarah Carmona
Yuh Min Chook
Douglass J Forbes
University of California, San Diego · USThe University of Texas Southwestern Medical Center · US

Funding

FUNCTIONAL STUDY OF NATIVE AND SYNTHETIC NUCLEIR01GM033279 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI FORBES, DOUGLASS JANE · 1985 to 2015
$7.0M
Structures and Mechanisms of Nuclear Import and ExportR01GM069909 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI CHOOK, YUH MIN · 2004 to 2020
$5.8M
NIGMS NIH HHS R01 GM033279NIGMS NIH HHS R01-GM033279NIGMS NIH HHS R01 GM069909NIGMS NIH HHS R01-GM069909
6 · The paper itself

Abstract

The nuclear import receptors importin β and transportin play a different role in mitosis: both act phenotypically as spatial regulators to ensure that mitotic spindle, nuclear membrane, and nuclear pore assembly occur exclusively around chromatin. Importin β is known to act by repressing assembly factors in regions distant from chromatin, whereas RanGTP produced on chromatin frees factors from importin β for localized assembly. The mechanism of transportin regulation was unknown. Diametrically opposed models for transportin action are as follows: 1) indirect action by RanGTP sequestration, thus down-regulating release of assembly factors from importin β, and 2) direct action by transportin binding and inhibiting assembly factors. Experiments in Xenopus assembly extracts with M9M, a superaffinity nuclear localization sequence that displaces cargoes bound by transportin, or TLB, a mutant transportin that can bind cargo and RanGTP simultaneously, support direct inhibition. Consistently, simple addition of M9M to mitotic cytosol induces microtubule aster assembly. ELYS and the nucleoporin 107-160 complex, components of mitotic kinetochores and nuclear pores, are blocked from binding to kinetochores in vitro by transportin, a block reversible by M9M. In vivo, 30% of M9M-transfected cells have spindle/cytokinesis defects. We conclude that the cell contains importin β and transportin "global positioning system"or "GPS" pathways that are mechanistically parallel.

Indexed as

MitosisAmino Acid SequenceAnimalsbeta KaryopherinsCell ExtractsChromatinCytokinesisDrosophila ProteinsHeLa CellsHumansInterphaseKaryopherinsKinetochoresModels, BiologicalMolecular Sequence DataMutant Proteinsbeta KaryopherinsCell ExtractsChromatinDrosophila ProteinsKaryopherinsMutant ProteinsNuclear Localization SignalsNuclear Pore Complex ProteinsPeptidesran GTP-Binding ProteinTnpo protein, DrosophilaXenopus Proteins

Identifiers

PMID24478460
PMCPMC3967982
OpenAlexW2144386737

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.