Evidence map›Paper›PMID 22940248›Full record

ArticleMolecular cell2012

Processive steps in the reverse direction require uncoupling of the lead head lever arm of myosin VI.

Julie Ménétrey, Tatiana Isabet, Virginie Ropars, Monalisa Mukherjea, Olena Pylypenko, Xiaoyan Liu, Javier Perez, Patrice Vachette, H Lee Sweeney, Anne M Houdusse

Abstract read
In one paragraph

Article in Molecular cell, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing 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

14 citing papers in PubMed.

  1. On the Control of Directionality of Myosin.Journal of the American Chemical Society · 2024
    Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. An intermediate along the recovery stroke of myosin VI revealed by X-ray crystallography and molecular dynamics.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  9. Article
  10. Kinematics of the lever arm swing in myosin VI.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  11. Article
  12. Article
  13. Article
  14. 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

10 authors.

Julie MénétreyStructural Motility, Institut Curie, Centre de Recherche, Paris, France.
Tatiana Isabet
Virginie Ropars
Monalisa Mukherjea
Olena Pylypenko
Xiaoyan Liu
Javier Perez
Patrice Vachette
H Lee Sweeney
Anne M Houdusse

Funding

Structure and Function of Myosin VIR01DC009100 · NIDCD · UNIVERSITY OF PENNSYLVANIA · PI SWEENEY, H LEE · 2007 to 2022
$6.0M
Myosin Va Cargo Transport: In Vitro Model SystemsR01GM094229 · NIGMS · UNIVERSITY OF VERMONT & ST AGRIC COLLEGE · PI WARSHAW, DAVID M · 2011 to 2020
$2.7M
NIDCD NIH HHS DC009100NIDCD NIH HHS R01 DC009100NIGMS NIH HHS GM094229NIGMS NIH HHS R01 GM094229
6 · The paper itself

Abstract

Myosin VI is the only known reverse-direction myosin motor. It has an unprecedented means of amplifying movements within the motor involving rearrangements of the converter subdomain at the C terminus of the motor and an unusual lever arm projecting from the converter. While the average step size of a myosin VI dimer is 30-36 nm, the step size is highly variable, presenting a challenge to the lever arm mechanism by which all myosins are thought to move. Herein, we present structures of myosin VI that reveal regions of compliance that allow an uncoupling of the lead head when movement is modeled on actin. The location of the compliance restricts the possible actin binding sites and predicts the observed stepping behavior. The model reveals that myosin VI, unlike plus-end directed myosins, does not use a pure lever arm mechanism, but instead steps with a mechanism analogous to the kinesin neck-linker uncoupling model.

Indexed as

ActinsAnimalsBinding SitesBiophysical PhenomenaCalmodulinComplianceCrystallography, X-RayModels, BiologicalModels, MolecularMolecular Motor ProteinsMultiprotein ComplexesMyosin Heavy ChainsMyosinsPeptide FragmentsProtein ConformationProtein MultimerizationActinsCalmodulinMolecular Motor ProteinsMultiprotein ComplexesMyosin Heavy ChainsMyosinsmyosin VIPeptide FragmentsRecombinant Fusion Proteins

Identifiers

PMID22940248
PMCPMC3472048

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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.