Evidence map›Paper›PMID 25208566›Full record

ArticleMolecular biology of the cell2014

A unique kinesin-8 surface loop provides specificity for chromosome alignment.

Haein Kim, Cindy Fonseca, Jason Stumpff

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 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
1.4field-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

26 citing papers in PubMed, 44 citations in OpenAlex.

  1. Article
  2. Kinesins inOpen biology · 2025
    Review
  3. Mechanism and regulation of kinesin motors.Nature reviews. Molecular cell biology · 2025
    Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. These motors were made for walking.Protein science : a publication of the Protein Society · 2020
    Review
  11. Review
  12. Bioenergetics of theBiomolecules · 2020
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  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

3 authors at 1 institution in 1 country.

Haein KimDepartment of Molecular Physiology and Biophysics, University of Vermont, Burlington, VT 05405.
Cindy FonsecaDepartment of Molecular Physiology and Biophysics, University of Vermont, Burlington, VT 05405.
Jason StumpffDepartment of Molecular Physiology and Biophysics, University of Vermont, Burlington, VT 05405 jstumpff@uvm.edu.
University of Vermont · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Microtubule length control is essential for the assembly and function of the mitotic spindle. Kinesin-like motor proteins that directly attenuate microtubule dynamics make key contributions to this control, but the specificity of these motors for different subpopulations of spindle microtubules is not understood. Kif18A (kinesin-8) localizes to the plus ends of the relatively slowly growing kinetochore fibers (K-fibers) and attenuates their dynamics, whereas Kif4A (kinesin-4) localizes to mitotic chromatin and suppresses the growth of highly dynamic, nonkinetochore microtubules. Although Kif18A and Kif4A similarly suppress microtubule growth in vitro, it remains unclear whether microtubule-attenuating motors control the lengths of K-fibers and nonkinetochore microtubules through a common mechanism. To address this question, we engineered chimeric kinesins that contain the Kif4A, Kif18B (kinesin-8), or Kif5B (kinesin-1) motor domain fused to the C-terminal tail of Kif18A. Each of these chimeric kinesins localizes to K-fibers; however, K-fiber length control requires an activity specific to kinesin-8s. Mutational studies of Kif18A indicate that this control depends on both its C-terminus and a unique, positively charged surface loop, called loop2, within the motor domain. These data support a model in which microtubule-attenuating kinesins are molecularly "tuned" to control the dynamics of specific subsets of spindle microtubules.

Indexed as

Base SequenceChromosome PositioningHeLa CellsHumansKinesinsKinetochoresMicrotubulesMolecular Sequence DataProtein Structure, TertiaryRecombinant ProteinsSpindle ApparatusKIF18A protein, humanKIF4A protein, humanKinesinsRecombinant Proteins

Identifiers

PMID25208566
PMCPMC4214779
OpenAlexW2158031267

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.