Evidence map›Paper›PMID 21498886›Full record

ArticleThe Journal of biological chemistry2011

Drosophila melanogaster myosin-18 represents a highly divergent motor with actin tethering properties.

Stephanie Guzik-Lendrum, Attila Nagy, Yasuharu Takagi, Anne Houdusse, James R Sellers

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.6field-weighted citation impact, top 15% 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

18 citing papers in PubMed, 30 citations in OpenAlex.

  1. Review
  2. Review
  3. 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
  4. Article
  5. Article
  6. Review
  7. MYO18A: An unusual myosin.Advances in biological regulation · 2018
    Review
  8. Article
  9. Article
  10. Review
  11. Kinetic characterization of the sole nonmuscle myosin-2 from the model organism Drosophila melanogaster.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2015
    Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Mammalian myosin-18A, a highly divergent myosin.The Journal of biological chemistry · 2013
    Article
  17. Article
  18. 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

5 authors at 3 institutions in 2 countries.

Stephanie Guzik-LendrumLaboratory of Molecular Physiology, NHLBI, National Institutes of Health, Bethesda, Maryland 20892, USA.
Attila Nagy
Yasuharu Takagi
Anne Houdusse
James R Sellers
National Institutes of Health · USCentre National de la Recherche Scientifique · FRUniversity of North Carolina at Chapel Hill · US

Funding

Expression Studies of Other Unconventional MyosinsZIAHL004232 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI SELLERS, JAMES · 2009 to 2025
$11.7M
Intramural NIH HHS
6 · The paper itself

Abstract

The gene encoding Drosophila myosin-18 is complex and can potentially yield six alternatively spliced mRNAs. One of the major features of this myosin is an N-terminal PDZ domain that is included in some of the predicted alternatively spliced products. To explore the biochemical properties of this protein, we engineered two minimal motor domain (MMD)-like constructs, one that contains the N-terminal PDZ (myosin-18 M-PDZ) domain and one that does not (myosin-18 M-ΔPDZ). These two constructs were expressed in the baculovirus/Sf9 system. The results suggest that Drosophila myosin-18 is highly divergent from most other myosins in the superfamily. Neither of the MMD constructs had an actin-activated MgATPase activity, nor did they even bind ATP. Both myosin-18 M-PDZ and M-ΔPDZ proteins bound to actin with K(d) values of 2.61 and 1.04 μM, respectively, but only about 50-75% of the protein bound to actin even at high actin concentrations. Unbound proteins from these actin binding assays reiterated the 60% saturation maximum, suggesting an equilibrium between actin-binding and non-actin-binding conformations of Drosophila myosin-18 in vitro. Neither the binding affinity nor the substoichiometric binding was significantly affected by ATP. Optical trapping of single molecules in three-bead assays showed short lived interactions of the myosin-18 motors with actin filaments. Combined, these data suggest that this highly divergent motor may function as an actin tethering protein.

Indexed as

Gene Expression RegulationActinsAdenosine TriphosphateAnimalsBaculoviridaeCloning, MolecularDrosophila melanogasterDrosophila ProteinsKineticsMyosinsProtein BindingProtein ConformationProtein DenaturationProtein FoldingProtein Structure, TertiaryRNA, MessengerActinsAdenosine TriphosphateDrosophila Proteinsmyosin-18, DrosophilaMyosinsRNA, Messenger

Identifiers

PMID21498886
PMCPMC3122231
OpenAlexW2156258071

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.