Evidence map›Paper›PMID 17124495›Full record

ArticleThe EMBO journal2006

Identification of a strong binding site for kinesin on the microtubule using mutant analysis of tubulin.

Seiichi Uchimura, Yusuke Oguchi, Miho Katsuki, Takeo Usui, Hiroyuki Osada, Jun-ichi Nikawa, Shin'ichi Ishiwata, Etsuko Muto

Open access · hybridAbstract read
In one paragraph

Article in The EMBO journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
0.8field-weighted citation impact, top 32% 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

37 citing papers in PubMed, 64 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. MAPping tubulin mutations.Frontiers in cell and developmental biology · 2023
    Review
  6. TUBB3 and KIF21A in neurodevelopment and disease.Frontiers in neuroscience · 2023
    Review
  7. Electro-detachment of kinesin motor domain from microtubule in silico.Computational and structural biotechnology journal · 2023
    Article
  8. Review
  9. Article
  10. Article
  11. Review
  12. Review
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. Microtubule dynamics: an interplay of biochemistry and mechanics.Nature reviews. Molecular cell biology · 2018
    Review
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

8 authors at 4 institutions in 1 country.

Seiichi UchimuraBrain Development Research Group, Brain Science Institute, RIKEN, Wako, Saitama, Japan.
Yusuke Oguchi
Miho Katsuki
Takeo Usui
Hiroyuki Osada
Jun-ichi Nikawa
Shin'ichi Ishiwata
Etsuko Muto
RIKEN Center for Brain Science · JPRIKEN · JPWaseda University · JPKyushu Institute of Technology · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The kinesin-binding site on the microtubule has not been identified because of the technical difficulties involved in the mutant analyses of tubulin. Exploiting the budding yeast expression system, we succeeded in replacing the negatively charged residues in the alpha-helix 12 of beta-tubulin with alanine and analyzed their effect on kinesin-microtubule interaction in vitro. The microtubule gliding assay showed that the affinity of the microtubules for kinesin was significantly reduced in E410A, D417A, and E421A, but not in E412A mutant. The unbinding force measurement revealed that in the former three mutants, the kinesin-microtubule interaction in the adenosine 5'-[beta,gamma-imido]triphosphate state (AMP-PNP state) became less stable when a load was imposed towards the microtubule minus end. In parallel with this decreased stability, the stall force of kinesin was reduced. Our results implicate residues E410, D417, and E421 as crucial for the kinesin-microtubule interaction in the strong binding state, thereby governing the size of kinesin stall force.

Indexed as

Adenosine DiphosphateAdenylyl ImidodiphosphateAmino Acid SequenceBinding SitesBiomechanical PhenomenaDNA Mutational AnalysisKinesinsMicrotubulesMolecular Sequence DataMutant ProteinsProtein Structure, SecondarySaccharomyces cerevisiaeTubulinAdenosine DiphosphateAdenylyl ImidodiphosphateKinesinsMutant ProteinsTubulin

Identifiers

PMID17124495
PMCPMC1698889
OpenAlexW1988719871

What OpenQuestion holds

Textmetadata
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.