Evidence map›Paper›PMID 20385849›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2010

Contribution of the myosin VI tail domain to processive stepping and intramolecular tension sensing.

Alexander R Dunn, Peiying Chuan, Zev Bryant, James A Spudich

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
3.4field-weighted citation impact, top 7% 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

29 citing papers in PubMed, 44 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. High-Resolution Single-Molecule Kinesin Assays at kHz Frame Rates.Methods in molecular biology (Clifton, N.J.) · 2018
    Article
  7. Article
  8. Kinematics of the lever arm swing in myosin VI.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  9. Force-producing ADP state of myosin bound to actin.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  10. Cytoplasmic dynein regulates its attachment to microtubules via nucleotide state-switched mechanosensing at multiple AAA domains.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  11. Article
  12. Stochastic kinetics on networks: when slow is fast.The journal of physical chemistry. B · 2014
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Motor proteins and molecular motors: how to operate machines at the nanoscale.Journal of physics. Condensed matter : an Institute of Physics journal · 2013
    Review
  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

4 authors at 1 institution in 1 country.

Alexander R DunnDepartment of Biochemistry, Stanford University School of Medicine, Stanford, CA 94305, USA.
Peiying Chuan
Zev Bryant
James A Spudich
Stanford University · US

Funding

MYOSIN MOVEMENT IN VITRO: MOLECULAR CHARACTERIZATIONR01GM033289 · NIGMS · STANFORD UNIVERSITY · PI SPUDICH, JAMES · 1985 to 2024
$13.6M
Engineering Molecular MotorsDP2OD004690 · OD · STANFORD UNIVERSITY · PI BRYANT, ZEV · 2008 to 2008
$2.4M
NIGMS NIH HHS GM33289NIGMS NIH HHS R01 GM033289NIH HHS DP2 OD004690
6 · The paper itself

Abstract

Myosin VI is proposed to act as both a molecular transporter and as an anchor in vivo. A portion of the molecule C-terminal to the canonical lever arm, termed the medial tail (MT), has been proposed to act as either a lever arm extension or as a dimerization motif. We describe constructs in which the MT is interrupted by a glycine-rich molecular swivel. Disruption of the MT results in decreased processive run lengths measured using single-molecule fluorescence microscopy and a decreased step size under applied load as measured in an optical trap. We used single-molecule gold nanoparticle tracking and optical trapping to examine the mechanism of coordination between the heads of dimeric myosin VI. We detect two rate-limiting kinetic processes at low (< 200 micromolar) ATP concentrations. Our data can be explained by a model in which intramolecular tension greatly increases the affinity of the lead head for ADP, likely by slowing ADP release from the lead head. This mechanism likely increases both the motor's processivity and its ability to act as an anchor under physiological conditions.

Indexed as

Models, ChemicalProtein Structure, TertiaryAdenosine TriphosphateBiomechanical PhenomenaComputer SimulationDimerizationKineticsMicroscopy, FluorescenceMonte Carlo MethodMyosin Heavy ChainsOptical TweezersAdenosine TriphosphateMyosin Heavy Chainsmyosin VI

Identifiers

PMID20385849
PMCPMC2867888
OpenAlexW1966476933

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.