Evidence map›Paper›PMID 21209315›Full record

ArticleMolecular biology of the cell2011

Nup98 regulates bipolar spindle assembly through association with microtubules and opposition of MCAK.

Marie K Cross, Maureen A Powers

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
4.0field-weighted citation impact, top 6% 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

34 citing papers in PubMed, 63 citations in OpenAlex.

  1. Article
  2. Review
  3. Advances in the understanding of nuclear pore complexes in human diseases.Journal of cancer research and clinical oncology · 2024
    Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. The Biology of the Nuclear Envelope and Its Implications in Cancer Biology.International journal of molecular sciences · 2019
    Review
  10. Article
  11. Article
  12. Proteomics of phosphorylation and protein dynamics during fertilization and meiotic exit in theProceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Nuclear transport factors: global regulation of mitosis.Current opinion in cell biology · 2015
    Review
  19. Review
  20. 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

2 authors at 1 institution in 1 country.

Marie K CrossDepartment of Cell Biology and Developmental Biology Graduate Program, Emory University School of Medicine, Atlanta, GA 30322, USA.
Maureen A Powers
Emory University · US

Funding

Training Program in Biochemistry, Cell and Molecular BiologyT32GM008367 · NIGMS · EMORY UNIVERSITY · PI BOISE, LAWRENCE H., CORBETT, ANITA H. · 1990 to 2019
$5.6M
FUNCTIONAL ANALYSIS OF VERTEBRATE NUCLEAR TRANSPORTR01GM059975 · NIGMS · EMORY UNIVERSITY · PI POWERS, MAUREEN A. · 1999 to 2009
$2.4M
NIGMS NIH HHS GM-008367NIGMS NIH HHS R01 GM-059975NIGMS NIH HHS R01 GM059975NIGMS NIH HHS T32 GM008367
6 · The paper itself

Abstract

During mitosis, the nuclear pore complex is disassembled and, increasingly, nucleoporins are proving to have mitotic functions when released from the pore. We find a contribution of the nucleoporin Nup98 to mitotic spindle assembly through regulation of microtubule dynamics. When added to Xenopus extract spindle assembly assays, the C-terminal domain of Nup98 stimulates uncontrolled growth of microtubules. Conversely, inhibition or depletion of Nup98 leads to formation of stable monopolar spindles. Spindle bipolarity is restored by addition of purified, recombinant Nup98 C-terminus. The minimal required region of Nup98 corresponds to a portion of the C-terminal domain lacking a previously characterized function. We show association between this region of the C-terminus of Nup98 and both Taxol-stabilized microtubules and the microtubule-depolymerizing mitotic centromere-associated kinesin (MCAK). Importantly, we demonstrate that this domain of Nup98 inhibits MCAK depolymerization activity in vitro. These data support a model in which Nup98 interacts with microtubules and antagonizes MCAK activity, thus promoting bipolar spindle assembly.

Indexed as

AnimalsAntibodiesAntibody SpecificityCell ExtractsKinesinsMeiosisMicrotubulesModels, BiologicalNuclear Pore Complex ProteinsOvumPolymerizationProtein BindingProtein Structure, Tertiaryran GTP-Binding ProteinSpindle ApparatusXenopusAntibodiesCell ExtractsKinesinsmitotic centromere-associated kinesin, Xenopusnuclear pore complex protein 98Nuclear Pore Complex ProteinsNup98 protein, Xenopusran GTP-Binding ProteinXenopus Proteins

Identifiers

PMID21209315
PMCPMC3046062
OpenAlexW2098686783

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.