Evidence map›Paper›PMID 2793931›Full record

ArticleThe Journal of cell biology1989

Plasma membrane association of Acanthamoeba myosin I.

H Miyata, B Bowers, E D Korn

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1989. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
13.2field-weighted citation impact, top 1% 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

42 citing papers in PubMed, 120 citations in OpenAlex.

  1. Article
  2. Article
  3. Myosin-I molecular motors at a glance.Journal of cell science · 2016
    Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Kinetics of the interaction of myo1c with phosphoinositides.The Journal of biological chemistry · 2009
    Article
  9. Article
  10. Intramolecular interaction in the tail of Acanthamoeba myosin IC between the SH3 domain and a putative pleckstrin homology domain.Proceedings of the National Academy of Sciences of the United States of America · 2007
    Article
  11. Article
  12. Article
  13. Lytic cycle of Toxoplasma gondii.Microbiology and molecular biology reviews : MMBR · 2000
    Review
  14. Article
  15. Article
  16. Analysis of the regulatory phosphorylation site in Acanthamoeba myosin IC by using site-directed mutagenesis.Proceedings of the National Academy of Sciences of the United States of America · 1998
    Article
  17. Article
  18. Article
  19. Overlapping functions of myosin-I isoforms?The Journal of cell biology · 1996
    Review
  20. 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

3 authors at 1 institution in 1 country.

H MiyataLaboratory of Cell Biology, National Heart, Lung, and Blood Institute, Bethesda, Maryland 20892.
B Bowers
E D Korn
National Heart Lung and Blood Institute · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Myosin I accounted for approximately 2% of the protein of highly purified plasma membranes, which represents about a tenfold enrichment over its concentration in the total cell homogenate. This localization is consistent with immunofluorescence analysis of cells that shows myosin I at or near the plasma membrane as well as diffusely distributed in the cytoplasm with no apparent association with cytoplasmic organelles or vesicles identifiable at the level of light microscopy. Myosin II was not detected in the purified plasma membrane fraction. Although actin was present in about a tenfold molar excess relative to myosin I, several lines of evidence suggest that the principal linkage of myosin I with the plasma membrane is not through F-actin: (a) KI extracted much more actin than myosin I from the plasma membrane fraction; (b) higher ionic strength was required to solubilize the membrane-bound myosin I than to dissociate a complex of purified myosin I and F-actin; and (c) added purified myosin I bound to KI-extracted plasma membranes in a saturable manner with maximum binding four- to fivefold greater than the actin content and with much greater affinity than for pure F-actin (apparent KD of 30-50 nM vs. 10-40 microM in 0.1 M KCl plus 2 mM MgATP). Thus, neither the MgATP-sensitive actin-binding site in the NH2-terminal end of the myosin I heavy chain nor the MgATP-insensitive actin-binding site in the COOH-terminal end of the heavy chain appeared to be the principal mechanism of binding of myosin I to plasma membranes through F-actin. Furthermore, the MgATP-sensitive actin-binding site of membrane-bound myosin I was still available to bind added F-actin. However, the MgATP-insensitive actin-binding site appeared to be unable to bind added F-actin, suggesting that the membrane-binding site is near enough to this site to block sterically its interaction with actin.

Indexed as

AcanthamoebaActinsAdenosine TriphosphateAnimalsCell FractionationCell MembraneCentrifugation, Density GradientKineticsMicroscopy, ElectronMyosinsProtein BindingActinsAdenosine TriphosphateMyosins

Identifiers

PMID2793931
PMCPMC2115813
OpenAlexW2101024664

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.