Evidence map›Paper›PMID 17182734›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2007

The power stroke of myosin VI and the basis of reverse directionality.

Zev Bryant, David Altman, James A Spudich

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.

0numbers the graph read from it
0cells of the map it votes in
52citing 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

52 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Article
  5. The twoFrontiers in physiology · 2024
    Article
  6. Review
  7. Sterically driven current reversal in a molecular motor model.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  8. Unconventional Myosins fromBiomolecules · 2022
    Review
  9. Review
  10. Review
  11. Article
  12. Review
  13. Article
  14. Reexamining the origin of the directionality of myosin V.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  15. Myosins, Actin and Autophagy.Traffic (Copenhagen, Denmark) · 2016
    Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Myosin lever arm directs collective motion on cellular actin network.Proceedings of the National Academy of Sciences of the United States of America · 2014
    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

3 authors.

Zev BryantDepartment of Biochemistry, Stanford University School of Medicine, Stanford, CA 94305-5307, USA.
David Altman
James A Spudich

Funding

MYOSIN MOVEMENT IN VITRO: MOLECULAR CHARACTERIZATIONR01GM033289 · NIGMS · STANFORD UNIVERSITY · PI SPUDICH, JAMES · 1985 to 2024
$13.6M
NIGMS NIH HHS GM 33289NIGMS NIH HHS R01 GM033289
6 · The paper itself

Abstract

Myosin VI supports movement toward the (-) end of actin filaments, despite sharing extensive sequence and structural homology with (+)-end-directed myosins. A class-specific stretch of amino acids inserted between the converter domain and the lever arm was proposed to provide the structural basis of directionality reversal. Indeed, the unique insert mediates a 120 degrees redirection of the lever arm in a crystal structure of the presumed poststroke conformation of myosin VI [Ménétrey J, Bahloul A, Wells AL, Yengo CM, Morris CA, Sweeney HL, Houdusse A (2005) Nature 435:779-785]. However, this redirection alone is insufficient to account for the large (-)-end-directed stroke of a monomeric myosin VI construct. The underlying motion of the myosin VI converter domain must therefore differ substantially from the power stroke of (+)-end-directed myosins. To experimentally map out the motion of the converter domain and lever arm, we have generated a series of truncated myosin VI constructs and characterized the size and direction of the power stroke for each construct using dual-labeled gliding filament assays and optical trapping. Motors truncated near the end of the converter domain generate (+)-end-directed motion, whereas longer constructs move toward the (-) end. Our results directly demonstrate that the unique insert is required for directionality reversal, ruling out a large class of models in which the converter domain moves toward the (-) end. We suggest that the lever arm rotates approximately 180 degrees between pre- and poststroke conformations.

Indexed as

MovementActinsAmino Acid SequenceAnimalsKineticsModels, MolecularMolecular Sequence DataMyosin Heavy ChainsProtein Structure, TertiarySequence AlignmentSwineActinsMyosin Heavy Chainsmyosin VI

Identifiers

PMID17182734
PMCPMC1713167

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.