Evidence map›Paper›PMID 23382379›Full record

ArticleThe Journal of biological chemistry2013

Mammalian myosin-18A, a highly divergent myosin.

Stephanie Guzik-Lendrum, Sarah M Heissler, Neil Billington, Yasuharu Takagi, Yi Yang, Peter J Knight, Earl Homsher, James R Sellers

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
5.9field-weighted citation impact, top 3% 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

46 citing papers in PubMed, 75 citations in OpenAlex.

  1. Article
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  4. Article
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  8. Article
  9. Article
  10. Non-muscle myosin 2 at a glance.Journal of cell science · 2023
    Review
  11. Article
  12. Non-muscle myosin 2 filaments are processive in cells.bioRxiv : the preprint server for biology · 2023
    Article
  13. Review
  14. Review
  15. Myosin 18Aα targets the guanine nucleotide exchange factor β-Pix to the dendritic spines of cerebellar Purkinje neurons and promotes spine maturation.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2021
    Article
  16. Article
  17. Review
  18. Review
  19. Article
  20. 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

8 authors at 4 institutions in 3 countries.

Stephanie Guzik-LendrumLaboratory of Molecular Physiology, NHLBI, National Institutes of Health, Bethesda, MD 20892-8015, USA.
Sarah M Heissler
Neil Billington
Yasuharu Takagi
Yi Yang
Peter J Knight
Earl Homsher
James R Sellers
National Institutes of Health · USNational Heart Lung and Blood Institute · USHunan Agricultural University · CNUniversity of Leeds · GB

Funding

Regulation Of Smooth and Nonmuscle MyosinZIAHL001786 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI SELLERS, JAMES · 2009 to 2025
$17.4M
Expression Studies of Other Unconventional MyosinsZIAHL004232 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI SELLERS, JAMES · 2009 to 2025
$11.7M
6 · The paper itself

Abstract

The Mus musculus myosin-18A gene is expressed as two alternatively spliced isoforms, α and β, with reported roles in Golgi localization, in maintenance of cytoskeleton, and as receptors for immunological surfactant proteins. Both myosin-18A isoforms feature a myosin motor domain, a single predicted IQ motif, and a long coiled-coil reminiscent of myosin-2. The myosin-18Aα isoform, additionally, has an N-terminal PDZ domain. Recombinant heavy meromyosin- and subfragment-1 (S1)-like constructs for both myosin-18Aα and -18β species were purified from the baculovirus/Sf9 cell expression system. These constructs bound both essential and regulatory light chains, indicating an additional noncanonical light chain binding site in the neck. Myosin-18Aα-S1 and -18Aβ-S1 molecules bound actin weakly with Kd values of 4.9 and 54 μm, respectively. The actin binding data could be modeled by assuming an equilibrium between two myosin conformations, a competent and an incompetent form to bind actin. Actin binding was unchanged by presence of nucleotide. Both myosin-18A isoforms bound N-methylanthraniloyl-nucleotides, but the rate of ATP hydrolysis was very slow (<0.002 s(-1)) and not significantly enhanced by actin. Phosphorylation of the regulatory light chain had no effect on ATP hydrolysis, and neither did the addition of tropomyosin or of GOLPH3, a myosin-18A binding partner. Electron microscopy of myosin-18A-S1 showed that the lever is strongly angled with respect to the long axis of the motor domain, suggesting a pre-power stroke conformation regardless of the presence of ATP. These data lead us to conclude that myosin-18A does not operate as a traditional molecular motor in cells.

Indexed as

ActinsAdenosine TriphosphateAnimalsBaculoviridaeCell MovementCloning, MolecularHumansHydrolysisKineticsLightMiceMicroscopy, ElectronModels, MolecularMuscle, SkeletalMyosinsPhosphorylationActinsAdenosine TriphosphateMyo18a protein, mouseMyosinsProtein IsoformsTropomyosin

Identifiers

PMID23382379
PMCPMC3611021
OpenAlexW2018109768

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.