Evidence map›Paper›PMID 20974847›Full record

ArticleThe Journal of biological chemistry2010

Simultaneous observation of tail and head movements of myosin V during processive motion.

Hailong Lu, Guy G Kennedy, David M Warshaw, Kathleen M Trybus

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.9field-weighted citation impact, top 13% 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

15 citing papers in PubMed, 19 citations in OpenAlex.

  1. Myosin-5 varies its step length to carry cargo straight along the irregular F-actin track.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  2. Myosin-5 varies its steps along the irregular F-actin track.bioRxiv : the preprint server for biology · 2023
    Article
  3. Article
  4. Article
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  7. Vascular disease-causing mutation R258C in ACTA2 disrupts actin dynamics and interaction with myosin.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Quantum dots find their stride in single molecule tracking.Current opinion in chemical biology · 2011
    Review
  15. Myosin Va and myosin VI coordinate their steps while engaged in an in vitro tug of war during cargo transport.Proceedings of the National Academy of Sciences of the United States of America · 2011
    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.

Hailong LuDepartment of Molecular Physiology and Biophysics, University of Vermont, Burlington, Vermont 05405, USA.
Guy G Kennedy
David M Warshaw
Kathleen M Trybus
University of Vermont · US

Funding

Ventricular and Cardiac Fiber Characterization and Integration CoreP01HL059408 · NHLBI · UNIVERSITY OF VERMONT &ST AGRIC COLLEGE · PI ROBBINS, JEFFREY · 1999 to 2014
$26.4M
MUTATIONAL STUDIES OF PROCESSIVE MYOSIN MOTORSR01GM078097 · NIGMS · UNIVERSITY OF VERMONT & ST AGRIC COLLEGE · PI TRYBUS, KATHLEEN M · 2007 to 2019
$4.8M
Myosin Va Cargo Transport: In Vitro Model SystemsR01GM094229 · NIGMS · UNIVERSITY OF VERMONT & ST AGRIC COLLEGE · PI WARSHAW, DAVID M · 2011 to 2020
$2.7M
NHLBI NIH HHS HL059408NHLBI NIH HHS P01 HL059408NIGMS NIH HHS GM078097NIGMS NIH HHS GM094229NIGMS NIH HHS R01 GM078097NIGMS NIH HHS R01 GM094229
6 · The paper itself

Abstract

Processive stepping of myosin Va (myoV) has been tracked by monitoring either the tail position (center of mass) or the position of one or both heads. Here, we combine these two approaches by attaching a quantum dot to one of the motor domains and a bead to the tail. Using laser trapping and total internal reflection microscopy, the position of one head and the tail are observed simultaneously as myoV moves processively on an actin filament bundle against the resistive load of the laser trap. The head moves one step (73 ± 10 nm) for every two steps of the tail (35 ± 9 nm). One tail step occurs concurrently with quantum dot-labeled head movement, whereas the other occurs with movement of the unlabeled head, consistent with a hand-over-hand model. Load increases the probability of the motor taking a back step. The back step is triggered by the motor taking a shorter forward step (head step, 68 ± 11 nm; tail step, 32 ± 10 nm), likely one actin monomer short of its preferred binding site. During a back step, the motor reverses its hand-over-hand motion, with the leading head detaching and reattaching to one of multiple actin sites behind the trailing head. After a back step, the motor can correct its mistake and step processively forward at resistive loads <0.7 piconewton or stall or detach at higher loads. Back stepping may provide a mechanism to ensure efficient cargo delivery even when myoV encounters obstacles within the actin cytoskeletal meshwork or when other motors are attached to the same cargo.

Indexed as

ActinsAnimalsBacterial ProteinsBiochemistryBiophysicsChickensKineticsLasersLuminescent ProteinsMolecular Motor ProteinsMotionMyosin Type VNormal DistributionProbabilityProtein Structure, TertiaryQuantum DotsActinsBacterial ProteinsLuminescent ProteinsMolecular Motor ProteinsMyosin Type Vyellow fluorescent protein, Bacteria

Identifiers

PMID20974847
PMCPMC3009932
OpenAlexW2013058445

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.