Evidence map›Paper›PMID 2762319›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1989

Actin filaments mediate Dictyostelium myosin assembly in vitro.

R K Mahajan, K T Vaughan, J A Johns, J D Pardee

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1989. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

23 citing papers in PubMed, 47 citations in OpenAlex.

  1. Article
  2. Filament evanescence of myosin II and smooth muscle function.The Journal of general physiology · 2021
    Review
  3. Review
  4. Review
  5. Article
  6. Cytokinesis: Robust cell shape regulation.Seminars in cell & developmental biology · 2016
    Review
  7. Cell shape regulation through mechanosensory feedback control.Journal of the Royal Society, Interface · 2015
    Article
  8. Article
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  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
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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

4 authors at 1 institution in 1 country.

R K MahajanDepartment of Cell Biology and Anatomy, Cornell University Medical College, New York, NY 10021.
K T Vaughan
J A Johns
J D Pardee
Cornell University · US

Funding

MYOFIBRIL ASSEMBLY IN STRIATED MUSCLER01AM032147 · AM · WEILL MEDICAL COLLEGE OF CORNELL UNIV · PI FISCHMAN, DONALD A · 1985 to 1985
–
NIADDK NIH HHS AM 32147NIGMS NIH HHS GM 32458
6 · The paper itself

Abstract

Because myosin thick filaments form in the actin-rich cortex of nonmuscle cells, we have examined the role of Dictyostelium actin filaments in the assembly of Dictyostelium myosin (type II). Fluorescence energy transfer and light-scattering assembly assays indicate that self-association of Dictyostelium myosin into bipolar thick filaments is kinetically regulated by actin filament networks. Regulation is nucleotide dependent but does not require ATP hydrolysis. Myosin assembly is accelerated approximately 5-fold by actin filaments when either 1 mM ATP or 1 mM adenosine 5'-[beta,gamma-imido]triphosphate (AMP-P[NH]P) is present. However, actin filaments together with 1 mM ADP abolish myosin assembly. Accelerated assembly appears to require transient binding of myosin molecules to actin filaments before incorporation into thick filaments. Fluorescence energy-transfer assays demonstrate that myosin associates with actin filaments at a rate that is equivalent to the accelerated myosin assembly rate, evidence that myosin to actin binding is a rate-limiting step in accelerated thick filament formation. Actin filament networks are also implicated in regulation of thick filament formation, since fragmentation of F-actin networks by severin causes immediate cessation of accelerated myosin assembly. Electron microscopic studies support a model of actin filament-mediated myosin assembly. In ADP, myosin monomers rapidly decorate F-actin, preventing extensive formation of thick filaments. In AMP-P[NH]P, myosin assembles along actin filaments, forming structures that resemble primitive stress fibers. Taken together, these data suggest a model in which site-directed assembly of thick filaments in Dictyostelium is mediated by the interaction of myosin monomers with cortical actin filament networks.

Indexed as

Protozoan ProteinsActinsAdenine NucleotidesDictyosteliumFluorescent DyesFungal ProteinsKineticsLightMacromolecular SubstancesMicrofilament ProteinsMyosinsScattering, RadiationSpectrometry, FluorescenceActinsAdenine NucleotidesFluorescent DyesFungal ProteinsMacromolecular SubstancesMicrofilament ProteinsMyosinsProtozoan Proteinsseverin protein, Dictyostelium

Identifiers

PMID2762319
PMCPMC297797
OpenAlexW1999469923

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.