Evidence map›Paper›PMID 24379364›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2014

Calmodulin regulates dimerization, motility, and lipid binding of Leishmania myosin XXI.

Christopher Batters, Heike Ellrich, Constanze Helbig, Katy Anna Woodall, Christian Hundschell, Dario Brack, Claudia Veigel

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.8field-weighted citation impact, top 14% 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

17 citing papers in PubMed, 30 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Review
  6. Emerging Functions of Actins and Actin Binding Proteins in Trypanosomatids.Frontiers in cell and developmental biology · 2020
    Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Self-organization of actin networks by a monomeric myosin.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  13. Calcium can mobilize and activate myosin-VI.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  14. Review
  15. Chaperone-enhanced purification of unconventional myosin 15, a molecular motor specialized for stereocilia protein trafficking.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  16. Review
  17. To understand muscle you must take it apart.Frontiers in physiology · 2014
    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

7 authors at 2 institutions in 1 country.

Christopher BattersDepartment of Cellular Physiology and Center for Nanosciences, Ludwig-Maximilians-Universität München, 80336 München, Germany.
Heike Ellrich
Constanze Helbig
Katy Anna Woodall
Christian Hundschell
Dario Brack
Claudia Veigel
Center for NanoScience · DELudwig-Maximilians-Universität München · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Myosin XXI is the only myosin expressed in Leishmania parasites. Although it is assumed that it performs a variety of motile functions, the motor's oligomerization states, cargo-binding, and motility are unknown. Here we show that binding of a single calmodulin causes the motor to adopt a monomeric state and to move actin filaments. In the absence of calmodulin, nonmotile dimers that cross-linked actin filaments were formed. Unexpectedly, structural analysis revealed that the dimerization domains include the calmodulin-binding neck region, essential for the generation of force and movement in myosins. Furthermore, monomeric myosin XXI bound to mixed liposomes, whereas the dimers did not. Lipid-binding sections overlapped with the dimerization domains, but also included a phox-homology domain in the converter region. We propose a mechanism of myosin regulation where dimerization, motility, and lipid binding are regulated by calmodulin. Although myosin-XXI dimers might act as nonmotile actin cross-linkers, the calmodulin-binding monomers might transport lipid cargo in the parasite.

Indexed as

MovementProtein ConformationArea Under CurveBaculoviridaeCalmodulinDimerizationFluorescenceFluorescence Resonance Energy TransferLeishmaniaMicroscopy, Electron, TransmissionMyosinsOligonucleotidesPhospholipidsPlasmidsCalmodulinMyosinsOligonucleotidesPhospholipidsmotor propertiesunconventional myosin

Identifiers

PMID24379364
PMCPMC3896141
OpenAlexW1998750798

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.