Evidence map›Paper›PMID 29235081›Full record

ReviewBiophysical reviews2018

Overview of the mechanism of cytoskeletal motors based on structure.

Yusuke Kato, Takuya Miyakawa, Masaru Tanokura

Abstract readReview
In one paragraph

Review in Biophysical reviews, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing 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

17 citing papers in PubMed.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Bottom-Up Synthetic Biology Using Cell-Free Protein Synthesis.Advances in biochemical engineering/biotechnology · 2023
    Review
  6. Unorthodox PCNA Binding by Chromatin Assembly Factor 1.International journal of molecular sciences · 2022
    Article
  7. Article
  8. Kinesins in Mammalian Spermatogenesis and Germ Cell Transport.Frontiers in cell and developmental biology · 2022
    Review
  9. Review
  10. High throughput and quantitative enzymology in the genomic era.Current opinion in structural biology · 2021
    Review
  11. Article
  12. Review
  13. Review
  14. Review
  15. Review
  16. Article
  17. 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.

Yusuke KatoInstitute for Enzyme Research, Tokushima University, Tokushima, Japan.
Takuya MiyakawaLaboratory of Basic Science on Healthy Longevity, Department of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, The University of Tokyo, Tokyo, Japan.
Masaru TanokuraLaboratory of Basic Science on Healthy Longevity, Department of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, The University of Tokyo, Tokyo, Japan. amtanok@mail.ecc.u-tokyo.ac.jp.ORCID http://orcid.org/0000-0001-5072-2480

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In the last two decades, a wealth of structural and functional knowledge has been obtained for the three major cytoskeletal motor proteins, myosin, kinesin and dynein, which we review here. The cytoskeletal motor proteins myosin and kinesin are structurally similar in the core architecture of their motor domains and have similar force-producing mechanisms that are coupled with the chemical cycles of ATP binding, hydrolysis, Pi release and subsequent ADP release. The force is generated through conformational changes in the motor domain during Pi release and ATP binding in myosin and kinesin, respectively, and then converted into the rotation of the lever arm or neck linker (referred to as a power stroke) through the common structural pathways. On the other hand, the dynein cytoskeletal motor is an AAA+ protein and has a different structure and power stroke mechanism from those of myosins and kinesins. The linker protruding from the AAA+ ring of dynein swings according to the ATPase states, which, presumably, generates force to carry cargos within a cell. The communication mechanism between the track-binding and ATPase domains of dynein is unique because the two helices that presumably slide with respect to each other work as coordinators for these domains. Details of the mechanism underlying the power stroke and interdomain communication were revealed through recent progress in the structural studies of myosin, kinesin and dynein.

Indexed as

Cytoskeletal motorDyneinForce generationKinesinMyosinStructure

Identifiers

PMID29235081
PMCPMC5899727

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.