Evidence map›Paper›PMID 30297389›Full record

ArticleThe Journal of cell biology2018

Kinesin-binding-triggered conformation switching of microtubules contributes to polarized transport.

Tomohiro Shima, Manatsu Morikawa, Junichi Kaneshiro, Taketoshi Kambara, Shinji Kamimura, Toshiki Yagi, Hiroyuki Iwamoto, Sotaro Uemura, Hideki Shigematsu, Mikako Shirouzu and 5 more

Abstract read
In one paragraph

Article in The Journal of cell biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 66 papers.

0numbers the graph read from it
0cells of the map it votes in
66citing 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

66 citing papers in PubMed.

  1. Article
  2. Review
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  13. 'Intelligent' proteins.Cellular and molecular life sciences : CMLS · 2025
    Review
  14. Structural switching of tubulin in the microtubule lattice.Biochemical Society transactions · 2025
    Review
  15. Mechanism and regulation of kinesin motors.Nature reviews. Molecular cell biology · 2025
    Review
  16. Article
  17. Review
  18. Article
  19. Modeling study of kinesin-13 MCAK microtubule depolymerase.European biophysics journal : EBJ · 2024
    Article
  20. Article

6 more citing papers are in PubMed but not listed here.

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

15 authors.

Tomohiro ShimaLaboratory for Cell Polarity Regulation, RIKEN Center for Biosystems Dynamics Research, Osaka, Japan.ORCID 0000-0001-7972-4965
Manatsu MorikawaDepartment of Cell Biology and Anatomy, Graduate School of Medicine, The University of Tokyo, Tokyo, Japan.
Junichi KaneshiroLaboratory for Comprehensive Bioimaging, RIKEN Center for Biosystems Dynamics Research, Osaka, Japan.
Taketoshi KambaraLaboratory for Cell Polarity Regulation, RIKEN Center for Biosystems Dynamics Research, Osaka, Japan.
Shinji KamimuraDepartment of Biological Sciences, Faculty of Science and Engineering, Chuo University, Tokyo, Japan.
Toshiki YagiDepartment of Life Sciences, Faculty of Life and Environmental Sciences, Prefectural University of Hiroshima, Hiroshima, Japan.ORCID 0000-0002-1379-460X
Hiroyuki IwamotoLife and Environmental Division, SPring-8, Japan Synchrotron Radiation Research Institute, Hyogo, Japan.ORCID 0000-0002-4980-8495
Sotaro UemuraDepartment of Biological Sciences, Graduate School of Science, The University of Tokyo, Tokyo, Japan.
Hideki ShigematsuStructural Biology Group, RIKEN Center for Biosystems Dynamics Research, Kanagawa, Japan.ORCID 0000-0003-3951-8651
Mikako ShirouzuStructural Biology Group, RIKEN Center for Biosystems Dynamics Research, Kanagawa, Japan.
Taro IchimuraLaboratory for Comprehensive Bioimaging, RIKEN Center for Biosystems Dynamics Research, Osaka, Japan.
Tomonobu M WatanabeLaboratory for Comprehensive Bioimaging, RIKEN Center for Biosystems Dynamics Research, Osaka, Japan.
Ryo NittaStructural Biology Group, RIKEN Center for Biosystems Dynamics Research, Kanagawa, Japan.ORCID 0000-0002-6537-9272
Yasushi OkadaLaboratory for Cell Polarity Regulation, RIKEN Center for Biosystems Dynamics Research, Osaka, Japan y.okada@riken.jp.ORCID 0000-0003-2601-3689
Nobutaka HirokawaDepartment of Cell Biology and Anatomy, Graduate School of Medicine, The University of Tokyo, Tokyo, Japan hirokawa@m.u-tokyo.ac.jp.ORCID 0000-0002-0081-5264

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Kinesin-1, the founding member of the kinesin superfamily of proteins, is known to use only a subset of microtubules for transport in living cells. This biased use of microtubules is proposed as the guidance cue for polarized transport in neurons, but the underlying mechanisms are still poorly understood. Here, we report that kinesin-1 binding changes the microtubule lattice and promotes further kinesin-1 binding. This high-affinity state requires the binding of kinesin-1 in the nucleotide-free state. Microtubules return to the initial low-affinity state by washing out the binding kinesin-1 or by the binding of non-hydrolyzable ATP analogue AMPPNP to kinesin-1. X-ray fiber diffraction, fluorescence speckle microscopy, and second-harmonic generation microscopy, as well as cryo-EM, collectively demonstrated that the binding of nucleotide-free kinesin-1 to GDP microtubules changes the conformation of the GDP microtubule to a conformation resembling the GTP microtubule.

Indexed as

KinesinsMicrotubulesAdenylyl ImidodiphosphateAnimalsBiological Transport, ActiveChlorocebus aethiopsDogsGuanosine DiphosphateGuanosine TriphosphateHeLa CellsHumansMadin Darby Canine Kidney CellsVero CellsAdenylyl ImidodiphosphateGuanosine DiphosphateGuanosine TriphosphateKIF5B protein, humanKinesins

Identifiers

PMID30297389
PMCPMC6279379

What OpenQuestion holds

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LicenceCC BY-NC-SA
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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.