Evidence map›Paper›PMID 36866642›Full record

ArticleJournal of cell science2023

Causes, costs and consequences of kinesin motors communicating through the microtubule lattice.

Kristen J Verhey, Ryoma Ohi

Open access · hybridFull text read
In one paragraph

Article in Journal of cell science, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
6.9field-weighted citation impact, top 2% 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

23 citing papers in PubMed, 33 citations in OpenAlex.

  1. Article
  2. Review
  3. CLASP2 promotes repair of kinesin-1 damage to the microtubule lattice.bioRxiv : the preprint server for biology · 2026
    Article
  4. Article
  5. Motor-Assisted Co-Migration of Intracellular Organelles and Microtubules as a Mechanism for Directed Cargo Transport.BioEssays : news and reviews in molecular, cellular and developmental biology · 2026
    Review
  6. Article
  7. SSNA1 mechanically reinforces the damaged microtubule lattice.bioRxiv : the preprint server for biology · 2026
    Article
  8. The microtubule GTP-tubulin cap size is modulated during cell division.bioRxiv : the preprint server for biology · 2026
    Article
  9. Review
  10. Article
  11. Article
  12. 'Intelligent' proteins.Cellular and molecular life sciences : CMLS · 2025
    Review
  13. Review
  14. Article
  15. Article
  16. Article
  17. Mechanism and regulation of kinesin motors.Nature reviews. Molecular cell biology · 2025
    Review
  18. Article
  19. Modeling study of kinesin-13 MCAK microtubule depolymerase.European biophysics journal : EBJ · 2024
    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

2 authors at 1 institution in 1 country.

Kristen J VerheyDepartment of Cell & Developmental Biology, University of Michigan Medical School, Ann Arbor, MI 48109, USA.ORCID 0000-0001-9329-4981
Ryoma OhiDepartment of Cell & Developmental Biology, University of Michigan Medical School, Ann Arbor, MI 48109, USA.
University of Michigan · US

Funding

Kinesin Motors and Microtubule-based TraffickingR35GM131744 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI Kristen J. Verhey · 2019 to 2026
$6.3M
Regulation of microtubule dynamics during cell divisionR01GM086610 · NIGMS · VANDERBILT UNIVERSITY · PI OHI, RYOMA · 2010 to 2023
$4.5M
NIGMS NIH HHS R01 GM086610NIGMS NIH HHS R35 GM131744NIH HHS R35GM131744
6 · The paper itself

Abstract

Microtubules are critical for a variety of important functions in eukaryotic cells. During intracellular trafficking, molecular motor proteins of the kinesin superfamily drive the transport of cellular cargoes by stepping processively along the microtubule surface. Traditionally, the microtubule has been viewed as simply a track for kinesin motility. New work is challenging this classic view by showing that kinesin-1 and kinesin-4 proteins can induce conformational changes in tubulin subunits while they are stepping. These conformational changes appear to propagate along the microtubule such that the kinesins can work allosterically through the lattice to influence other proteins on the same track. Thus, the microtubule is a plastic medium through which motors and other microtubule-associated proteins (MAPs) can communicate. Furthermore, stepping kinesin-1 can damage the microtubule lattice. Damage can be repaired by the incorporation of new tubulin subunits, but too much damage leads to microtubule breakage and disassembly. Thus, the addition and loss of tubulin subunits are not restricted to the ends of the microtubule filament but rather, the lattice itself undergoes continuous repair and remodeling. This work leads to a new understanding of how kinesin motors and their microtubule tracks engage in allosteric interactions that are critical for normal cell physiology.

Indexed as

KinesinsTubulinCytoskeletonMicrotubule-Associated ProteinsMicrotubulesKinesinsMicrotubule-Associated ProteinsTubulinGTP islandKinesinMicrotubuleMicrotubule latticeMicrotubule repairTubulinTubulin code

Identifiers

PMID36866642
PMCPMC10022682
OpenAlexW4323037554

What OpenQuestion holds

Textfull text, public
LicenceCC BY
measurements read6
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.