Evidence map›Paper›PMID 18079121›Full record

ArticleThe Journal of biological chemistry2008

Human myosin Vc is a low duty ratio nonprocessive motor.

Shinya Watanabe, Tomonobu M Watanabe, Osamu Sato, Junya Awata, Kazuaki Homma, Nobuhisa Umeki, Hideo Higuchi, Reiko Ikebe, Mitsuo Ikebe

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.6field-weighted citation impact, top 15% 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

21 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
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  9. Article
  10. Structural insights into the assembly of a monomeric class V myosin.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  11. Article
  12. Multiple roles for the actin cytoskeleton during regulated exocytosis.Cellular and molecular life sciences : CMLS · 2013
    Review
  13. Article
  14. Plant-Specific Myosin XI, a Molecular Perspective.Frontiers in plant science · 2012
    Article
  15. Walking to work: roles for class V myosins as cargo transporters.Nature reviews. Molecular cell biology · 2011
    Review
  16. Review
  17. Article
  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

9 authors at 2 institutions in 2 countries.

Shinya WatanabeDepartment of Physiology, University of Massachusetts Medical School, Worcester, Massachusetts 01655, USA.
Tomonobu M Watanabe
Osamu Sato
Junya Awata
Kazuaki Homma
Nobuhisa Umeki
Hideo Higuchi
Reiko Ikebe
Mitsuo Ikebe
University of Massachusetts Chan Medical School · USTohoku University · JP

Funding

Regulation of Mammalian Class VI MyosinR01AR048526 · NIAMS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI IKEBE, MITSUO · 2003 to 2007
$1.8M
MOLECULAR REGULATION OF SMOOTH MUSCLE ACTOMYOSINR01AR041653 · NIAMS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI IKEBE, MITSUO · 1992 to 2004
$1.8M
Function of Small G-Protein Binding MyosinR01AR048898 · NIAMS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI IKEBE, MITSUO · 2003 to 2007
$1.8M
Motor Function and Regulation of Myosin VIIR01DC006103 · NIDCD · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI IKEBE, MITSUO · 2003 to 2007
$1.5M
NIAMS NIH HHS AR048526NIAMS NIH HHS AR048898NIAMS NIH HHS AR41653NIDCD NIH HHS DC006103
6 · The paper itself

Abstract

There are three distinct members of the myosin V family in vertebrates, and each isoform is involved in different membrane trafficking pathways. Both myosin Va and Vb have demonstrated that they are high duty ratio motors that are consistent with the processive nature of these motors. Here we report that the ATPase cycle mechanism of the single-headed construct of myosin Vc is quite different from those of other vertebrate myosin V isoforms. K(ATPase) of the actin-activated ATPase was 62 microm, which is much higher than that of myosin Va ( approximately 1 mum). The rate of ADP release from actomyosin Vc was 12.7 s(-1), which was 2 times greater than the entire ATPase cycle rate, 6.5 s(-1). P(i) burst size was 0.31, indicating that the equilibrium of the ATP hydrolysis step is shifted to the prehydrolysis form. Our kinetic model, based on all kinetic data we determined in this study, suggests that myosin Vc spends the majority of the ATPase cycle time in the weak actin binding state in contrast to myosin Va and Vb. Consistently, the two-headed myosin Vc construct did not show processive movement in total internal reflection fluorescence microscope analysis, demonstrating that myosin Vc is a nonprocessive motor. Our findings suggest that myosin Vc fulfills its function as a cargo transporter by different mechanisms from other myosin V isoforms.

Indexed as

ActinsActomyosinAdenosine DiphosphateAdenosine TriphosphatasesAdenosine TriphosphateCloning, MolecularDose-Response Relationship, DrugHumansKineticsMicroscopy, FluorescenceModels, BiologicalModels, ChemicalMyosin Type VProtein IsoformsTime FactorsActinsActomyosinAdenosine DiphosphateAdenosine TriphosphatasesAdenosine TriphosphateMYO5C protein, humanMyosin Type VProtein Isoforms

Identifiers

PMID18079121
PMCPMC2447649
OpenAlexW2082773981

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.