Evidence map›Paper›PMID 19828438›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2009

Myosin VI undergoes a 180 degrees power stroke implying an uncoupling of the front lever arm.

Jeff G Reifenberger, Erdal Toprak, Hyeongjun Kim, Dan Safer, H Lee Sweeney, Paul R Selvin

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. 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
–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

18 citing papers in PubMed.

  1. Article
  2. Kinematics of the lever arm swing in myosin VI.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Structural and functional insights on the Myosin superfamily.Bioinformatics and biology insights · 2012
    Article
  10. Article
  11. Article
  12. Review
  13. Cargo binding activates myosin VIIA motor function in cells.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
  14. Role of insert-1 of myosin VI in modulating nucleotide affinity.The Journal of biological chemistry · 2011
    Article
  15. Article
  16. Contribution of the myosin VI tail domain to processive stepping and intramolecular tension sensing.Proceedings of the National Academy of Sciences of the United States of America · 2010
    Article
  17. Myosin VI lever arm rotation: fixed or variable?Proceedings of the National Academy of Sciences of the United States of America · 2010
    Article
  18. Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors.

Jeff G ReifenbergerDepartment of Physics, University of Illinois, Urbana, IL 61801, USA.
Erdal Toprak
Hyeongjun Kim
Dan Safer
H Lee Sweeney
Paul R Selvin

Funding

Structure and Function of Myosin VIR01DC009100 · NIDCD · UNIVERSITY OF PENNSYLVANIA · PI SWEENEY, H LEE · 2007 to 2022
$6.0M
Nanometric Fluorescence Imaging of Single Motor ProteinsR01GM068625 · NIGMS · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI SELVIN, PAUL R · 2004 to 2012
$2.8M
GENETICALLY TARGETABLE LABELS FOR LIGHT AND EM (RMI)P20GM072033 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI TSIEN, ROGER Y · 2004 to 2007
$2.5M
NIDCD NIH HHS DC-009100NIDCD NIH HHS R01 DC009100NIGMS NIH HHS GM068625NIGMS NIH HHS GM072033NIGMS NIH HHS P20 GM072033NIGMS NIH HHS R01 GM068625
6 · The paper itself

Abstract

We simultaneously measure both the step size, via FIONA, and the 3-D orientation, via DOPI, of the light-chain domain of individual dimeric myosin VIs. This allows for the correlation of the change in orientation of the light chain domain to the stepping of the motor. Three different pairs of positions were tested using a rigid bifunctional rhodamine on the calmodulin of the IQ domain. The data for all three labeling positions support the model that the light chain domain undergoes a significant rotation of approximately 180 degrees . Contrary to an earlier study [Sun, Y. et al. (2007) Mol Cell 28, 954-964], our data does not support a model of multiple angles of the lever arm of the lead head, nor "wiggly" walking on actin. Instead, we propose that for the two heads of myosin VI to coordinate their processive movement, the lever arm of the lead head must be uncoupled from the converter until the rear head detaches. More specifically, intramolecular strain causes the myosin VI lever arm of the lead head to uncouple from the motor domain, allowing the motor domain to go through its product-release (phosphate and ADP) steps at an unstrained rate. The lever arm of the lead head rebinds to the motor and attains a rigor conformation when the rear head detaches. By coupling the orientation and position information with previously described kinetics, this allows us to explain how myosin VI coordinates its heads processively while maintaining the ability to move under load with a (semi-) rigid lever arm.

Indexed as

AnimalsCell LineCrystallography, X-RayModels, MolecularMyosin Heavy ChainsProtein BindingProtein Structure, QuaternarySwineMyosin Heavy Chainsmyosin VI

Identifiers

PMID19828438
PMCPMC2775346

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.