Evidence map›Paper›PMID 19664948›Full record

ArticleMolecular cell2009

Myosin VI dimerization triggers an unfolding of a three-helix bundle in order to extend its reach.

Monalisa Mukherjea, Paola Llinas, HyeongJun Kim, Mirko Travaglia, Daniel Safer, Julie Ménétrey, Clara Franzini-Armstrong, Paul R Selvin, Anne Houdusse, H Lee Sweeney

Open access · bronzeAbstract read
In one paragraph

Article in Molecular cell, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
8.2field-weighted citation impact, top 2% 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

53 citing papers in PubMed, 100 citations in OpenAlex.

  1. Cardiolipin membranes drive Myosin VI activation, oligomerization, and processive cargo transport.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  2. NAR genomics and bioinformatics · 2024
    Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Landscape-Based View on the Stepping Movement of Myosin VI.The journal of physical chemistry. B · 2022
    Article
  8. Article
  9. Article
  10. Article
  11. Unconventional Myosins: How Regulation Meets Function.International journal of molecular sciences · 2019
    Review
  12. Article
  13. Article
  14. Kinematics of the lever arm swing in myosin VI.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  15. Investigations of human myosin VI targeting using optogenetically controlled cargo loading.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  16. Filopodia formation and endosome clustering induced by mutant plus-end-directed myosin VI.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  17. Self-organization of actin networks by a monomeric myosin.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  18. Article
  19. Review
  20. Myosins, Actin and Autophagy.Traffic (Copenhagen, Denmark) · 2016
    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 at 3 institutions in 2 countries.

Monalisa MukherjeaDepartment of Physiology, University of Pennsylvania School of Medicine, Philadelphia, 19104, USA.
Paola Llinas
HyeongJun Kim
Mirko Travaglia
Daniel Safer
Julie Ménétrey
Clara Franzini-Armstrong
Paul R Selvin
Anne Houdusse
H Lee Sweeney
University of Pennsylvania · USCentre National de la Recherche Scientifique · FRUniversity of Illinois Urbana-Champaign · US

Funding

Structure and Function of Myosin VIR01DC009100 · NIDCD · UNIVERSITY OF PENNSYLVANIA · PI SWEENEY, H LEE · 2007 to 2022
$6.0M
Dynamics of Kinesins, Dyneins, and MyosinsR01AR044420 · NIAMS · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI SELVIN, PAUL R · 2001 to 2010
$4.3M
NIAMS NIH HHS R01 AR044420NIDCD NIH HHS R01 DC009100
6 · The paper itself

Abstract

Myosin VI challenges the prevailing theory of how myosin motors move on actin: the lever arm hypothesis. While the reverse directionality and large powerstroke of myosin VI can be attributed to unusual properties of a subdomain of the motor (converter with a unique insert), these adaptations cannot account for the large step size on actin. Either the lever arm hypothesis needs modification, or myosin VI has some unique form of extension of its lever arm. We determined the structure of the region immediately distal to the lever arm of the motor and show that it is a three-helix bundle. Based on C-terminal truncations that display the normal range of step sizes on actin, CD, fluorescence studies, and a partial deletion of the bundle, we demonstrate that this bundle unfolds upon dimerization of two myosin VI monomers. This unconventional mechanism generates an extension of the lever arm of myosin VI.

Indexed as

Amino Acid SequenceAnimalsDimerizationModels, MolecularMolecular Sequence DataMyosin Heavy ChainsProtein FoldingProtein Structure, TertiarySequence DeletionSwineMyosin Heavy Chainsmyosin VI

Identifiers

PMID19664948
PMCPMC2756668
OpenAlexW2071217600

What OpenQuestion holds

Textmetadata
LicenceTDM
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.