Evidence map›Paper›PMID 1651941›Full record

ArticleThe Journal of cell biology1991

Modulation of contraction by gelation/solation in a reconstituted motile model.

L W Janson, J Kolega, D L Taylor

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1991. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.

0numbers the graph read from it
0cells of the map it votes in
59citing papers in PubMed
2.3field-weighted citation impact, top 10% 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

59 citing papers in PubMed, 112 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. The role of the Arp2/3 complex in shaping the dynamics and structures of branched actomyosin networks.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  7. Article
  8. Oscillatory fluid flow drives scaling of contraction wave with system size.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  9. Article
  10. Article
  11. Filament rigidity and connectivity tune the deformation modes of active biopolymer networks.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  12. Article
  13. Article
  14. Article
  15. Forcing cells into shape: the mechanics of actomyosin contractility.Nature reviews. Molecular cell biology · 2015
    Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Mathematical modeling of eukaryotic cell migration: insights beyond experiments.Annual review of cell and developmental biology · 2013
    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

3 authors at 1 institution in 1 country.

L W JansonDepartment of Biological Sciences, Carnegie Mellon University, Pittsburgh, Pennsylvania 15213.
J Kolega
D L Taylor
Carnegie Mellon University · US

Funding

STRUCTURAL/CHEMICAL DYNAMICS OF CELL MOVEMENTR37AR032461 · NIAMS · CARNEGIE-MELLON UNIVERSITY · PI TAYLOR, D. LANSING · 1991 to 2000
$257k
STRUCTURAL AND CHEMICAL DYNAMICS OF CELL MOVEMENTR01AR032461 · NIAMS · CARNEGIE-MELLON UNIVERSITY · PI TAYLOR, D. LANSING · 1986 to 1990
–
PREDOCTORAL TRAINING IN CELLULAR AND MOLECULAR BIOLOGYT32GM008067 · NIGMS · CARNEGIE-MELLON UNIVERSITY · PI JONES, ELIZABETH W · 1985 to 1992
–
NIAMS NIH HHS AR-32461NIGMS NIH HHS 5T32GM08067-08
6 · The paper itself

Abstract

The actin-based cytoskeleton is a dynamic component of living cells with major structural and contractile properties involved in fundamental cellular processes. The action of actin-binding proteins can decrease or increase the gel structure. Changes in the actin-based cytoskeleton have long been thought to modulate the myosin II-based contractions involved in these cellular processes, but there has been some debate concerning whether maximal gelation increases or decreases contractile activity. To address this question, we have examined how contractile activity is modulated by the extent of actin gelation. The model system consists of physiologically relevant concentrations and molar ratios of actin filaments (whose lengths are controlled by gelsolin), the actin-cross-linking protein filamin, and smooth muscle myosin II. This system has been studied at the macroscopic and light microscopic levels to relate the gel structure to the rate of contraction. We present results which show that while a minimal amount of structure is necessary to transmit the contractile force, increasing the gel structure inhibits the rate of contraction, despite an increase in the actin-activated Mg(2+)-ATPase activity of myosin. Decreasing the total myosin concentration also inhibits the rate of contraction. Application of cytochalasin D to one side of the contractile network increases the rate of contraction and also induces movement comparable to flare streaming observed in isolated amoeba cytoplasm. These results are interpreted relative to current models of the relationship between the state of gelation and contraction and to the potential effects of such a relationship in the living cell.

Indexed as

Cell MovementActin CytoskeletonActinsActomyosinCalcium-Binding ProteinsCell-Free SystemContractile ProteinsCytochalasin DFilaminsGelsGelsolinIn Vitro TechniquesMicrofilament ProteinsMyosin-Light-Chain KinaseMyosinsSolubilityActinsActomyosinCalcium-Binding ProteinsContractile ProteinsCytochalasin DFilaminsGelsGelsolinMicrofilament ProteinsMyosin-Light-Chain KinaseMyosins

Identifiers

PMID1651941
PMCPMC2289122
OpenAlexW1990654048

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.