Evidence map›Paper›PMID 21212272›Full record

ArticleThe Journal of biological chemistry2011

The kinetic mechanism of mouse myosin VIIA.

Jessica Haithcock, Neil Billington, Kevin Choi, Jennifer Fordham, James R Sellers, Walter F Stafford, Howard White, Eva Forgacs

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.0field-weighted citation impact, top 21% 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

18 citing papers in PubMed, 25 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Myosin motors in sensory hair bundle assembly.Current opinion in cell biology · 2022
    Review
  6. Article
  7. Article
  8. A new light chain for myosin-7.The Journal of biological chemistry · 2020
    Article
  9. Article
  10. Article
  11. UsingDisease models & mechanisms · 2018
    Review
  12. Article
  13. Review
  14. Review
  15. Article
  16. Functional characterization of the human myosin-7a motor domain.Cellular and molecular life sciences : CMLS · 2012
    Article
  17. Article
  18. 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 5 institutions in 2 countries.

Jessica HaithcockDepartment of Physiological Sciences, Eastern Virginia Medical School, Norfolk, Virginia 23507, USA.
Neil Billington
Kevin Choi
Jennifer Fordham
James R Sellers
Walter F Stafford
Howard White
Eva Forgacs
Eastern Virginia Medical School · USBoston Biomedical Research Institute · USKing's College London · GBNational Heart Lung and Blood Institute · USNational Institutes of Health · US

Funding

Studies of Drosophila Myosin VIIZIAHL006049 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI SELLERS, JAMES · 2010 to 2025
$9.7M
CRYOELECTRONMICROSCOPY OF ACTOS1 ATPASE INTERMEDIATESR01EB000209 · NIBIB · EASTERN VIRGINIA MEDICAL SCHOOL · PI WHITE, HOWARD D. · 2002 to 2008
$2.1M
The Effect Of Deafness Associated Mutations on MyosinVIIA FunctionR03DC009335 · NIDCD · EASTERN VIRGINIA MEDICAL SCHOOL · PI FORGACS, EVA · 2008 to 2010
$501k
NIBIB NIH HHS EB00209NIBIB NIH HHS R01 EB000209NIDCD NIH HHS DC009335NIDCD NIH HHS R03 DC009335
6 · The paper itself

Abstract

Myosin VIIa is crucial in hearing and visual processes. We examined the kinetic and association properties of the baculovirus expressed, truncated mouse myosin VIIa construct containing the head, all 5IQ motifs and the putative coiled coil domain (myosin VIIa-5IQ). The construct appears to be monomeric as determined by analytical ultracentrifugation experiments, and only single headed molecules were detected by negative stain electron microscopy. The relatively high basal steady-state rate of 0.18 s(-1) is activated by actin only by ∼3.5-fold resulting in a V(max) of 0.7 s(-1) and a K(ATPase) of 11.5 μM. There is no single rate-limiting step of the ATP hydrolysis cycle. The ATP hydrolysis step (M·T M·D·P) is slow (12 s(-1)) and the equilibrium constant (K(H)) of 1 suggests significant reversal of hydrolysis. In the presence of actin ADP dissociates with a rate constant of 1.2 s(-1). Phosphate dissociation is relatively fast (>12 s(-1)), but the maximal rate could not be experimentally obtained at actin concentrations ≤ 50 μM because of the weak binding of the myosin VIIa-ADP-P(i) complex to actin. At higher actin concentrations the rate of attached hydrolysis (0.4 s(-1)) becomes significant and partially rate-limiting. Our findings suggest that the myosin VIIa is a "slow", monomeric molecular motor with a duty ratio of 0.6.

Indexed as

Adenosine TriphosphateAmino Acid MotifsAnimalsKineticsMiceMyosinsMyosin VIIaProtein Structure, TertiaryAdenosine TriphosphateMyo7a protein, mouseMyosinsMyosin VIIa

Identifiers

PMID21212272
PMCPMC3059067
OpenAlexW2088882493

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.