Evidence map›Paper›PMID 24714498›Full record

ArticleeLife2014

Structural basis for the assembly of the mitotic motor Kinesin-5 into bipolar tetramers.

Jessica E Scholey, Stanley Nithianantham, Jonathan M Scholey, Jawdat Al-Bassam

Abstract read
In one paragraph

Article in eLife, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.

0numbers the graph read from it
0cells of the map it votes in
55citing 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

55 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Designability of α-Helical Protein Filaments.Sub-cellular biochemistry · 2026
    Review
  5. Article
  6. Article
  7. Mechanism and regulation of kinesin motors.Nature reviews. Molecular cell biology · 2025
    Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Distinct regions of the kinesin-5 C-terminal tail are essential for mitotic spindle midzone localization and sliding force.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  16. Article
  17. Article
  18. Acentrosomal spindle assembly and maintenance inMolecular biology of the cell · 2022
    Article
  19. Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors.

Jessica E ScholeyDepartment of Molecular and Cellular Biology, University of California, Davis, Davis, United States.
Stanley Nithianantham
Jonathan M Scholey
Jawdat Al-Bassam

Funding

Mitotic Motors in the Drosophila Embryo.R01GM055507 · NIGMS · UNIVERSITY OF CALIFORNIA DAVIS · PI SCHOLEY, JONATHAN M. · 1997 to 2013
$4.6M
Microtubule Polymerization and Depolymerization Mechanisms by Conserved ProteinsR00GM084292 · NIGMS · UNIVERSITY OF CALIFORNIA AT DAVIS · PI AL-BASSAM, JAWDAT MH · 2011 to 2013
$715k
NIGMS NIH HHS R00-GM08249NIGMS NIH HHS R00 GM084292NIGMS NIH HHS R01-GM05550712S1NIGMS NIH HHS R01-GM55507
6 · The paper itself

Abstract

Chromosome segregation during mitosis depends upon Kinesin-5 motors, which display a conserved, bipolar homotetrameric organization consisting of two motor dimers at opposite ends of a central rod. Kinesin-5 motors crosslink adjacent microtubules to drive or constrain their sliding apart, but the structural basis of their organization is unknown. In this study, we report the atomic structure of the bipolar assembly (BASS) domain that directs four Kinesin-5 subunits to form a bipolar minifilament. BASS is a novel 26-nm four-helix bundle, consisting of two anti-parallel coiled-coils at its center, stabilized by alternating hydrophobic and ionic four-helical interfaces, which based on mutagenesis experiments, are critical for tetramerization. Strikingly, N-terminal BASS helices bend as they emerge from the central bundle, swapping partner helices, to form dimeric parallel coiled-coils at both ends, which are offset by 90°. We propose that BASS is a mechanically stable, plectonemically-coiled junction, transmitting forces between Kinesin-5 motor dimers during microtubule sliding. DOI: http://dx.doi.org/10.7554/eLife.02217.001.

Indexed as

Amino Acid SequenceAnimalsBiopolymersCrystallography, X-RayDrosophilaKinesinsModels, MolecularMolecular Sequence DataProtein ConformationSequence Homology, Amino AcidBiopolymersKinesinscoiled-coilKinesin-5microtubulemitosismotor proteinX-ray structure

Identifiers

PMID24714498
PMCPMC3978770

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.