Evidence map›Paper›PMID 26811464›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2016

Calcium can mobilize and activate myosin-VI.

Christopher Batters, Dario Brack, Heike Ellrich, Beate Averbeck, Claudia Veigel

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
4.9field-weighted citation impact, top 4% 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

28 citing papers in PubMed, 48 citations in OpenAlex.

  1. Article
  2. Article
  3. 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
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Unconventional Myosins: How Regulation Meets Function.International journal of molecular sciences · 2019
    Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors at 1 institution in 1 country.

Christopher BattersDepartment of Cellular Physiology, Ludwig-Maximilians-Universität München, 80336 Munich, Germany; Center for Nanosciences München, 80799 Munich, Germany.
Dario BrackDepartment of Cellular Physiology, Ludwig-Maximilians-Universität München, 80336 Munich, Germany; Center for Nanosciences München, 80799 Munich, Germany.
Heike EllrichDepartment of Cellular Physiology, Ludwig-Maximilians-Universität München, 80336 Munich, Germany; Center for Nanosciences München, 80799 Munich, Germany.
Beate AverbeckDepartment of Cellular Physiology, Ludwig-Maximilians-Universität München, 80336 Munich, Germany;
Claudia VeigelDepartment of Cellular Physiology, Ludwig-Maximilians-Universität München, 80336 Munich, Germany; Center for Nanosciences München, 80799 Munich, Germany claudia.veigel@med.uni-muenchen.de.
Ludwig-Maximilians-Universität München · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The ability to coordinate the timing of motor protein activation lies at the center of a wide range of cellular motile processes including endocytosis, cell division, and cancer cell migration. We show that calcium dramatically alters the conformation and activity of the myosin-VI motor implicated in pivotal steps of these processes. We resolved the change in motor conformation and in structural flexibility using single particle analysis of electron microscopic data and identified interacting domains using fluorescence spectroscopy. We discovered that calcium binding to calmodulin increases the binding affinity by a factor of 2,500 for a bipartite binding site on myosin-VI. The ability of calcium-calmodulin to seek out and bridge between binding site components directs a major rearrangement of the motor from a compact dormant state into a cargo binding primed state that is nonmotile. The lack of motility at high calcium is due to calmodulin switching to a higher affinity binding site, which leaves the original IQ-motif exposed, thereby destabilizing the lever arm. The return to low calcium can either restabilize the lever arm, required for translocating the cargo-bound motors toward the center of the cell, or refold the cargo-free motors into an inactive state ready for the next cellular calcium flux.

Indexed as

AnimalsBinding SitesCalciumCalmodulinCells, CulturedChickensMyosin Heavy ChainsSpectrometry, FluorescenceCalciumCalmodulinMyosin Heavy Chainsmyosin VIcalmodulinelectron microscopyunconventional myosin

Identifiers

PMID26811464
PMCPMC4780617
OpenAlexW2266098991

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.