Evidence map›Paper›PMID 11860600›Full record

ArticleBMC cell biology2002

Quantitation of the distribution and flux of myosin-II during cytokinesis.

Douglas N Robinson, Guy Cavet, Hans M Warrick, James A Spudich

Open access · goldAbstract read
In one paragraph

Article in BMC cell biology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
2.0field-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

45 citing papers in PubMed, 84 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Molecular Mechanism of Cytokinesis.Annual review of biochemistry · 2019
    Review
  12. Article
  13. 14-3-3 proteins tune non-muscle myosin II assembly.The Journal of biological chemistry · 2018
    Article
  14. Article
  15. Article
  16. Article
  17. Cell shape regulation through mechanosensory feedback control.Journal of the Royal Society, Interface · 2015
    Article
  18. Pharmacological activation of myosin II paralogs to correct cell mechanics defects.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  19. 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

4 authors at 2 institutions in 1 country.

Douglas N RobinsonDepartment of Biochemistry, Stanford University School of Medicine, Stanford, CA 94305-5307, USA. Douglas.Robinson@jhu.edu
Guy Cavet
Hans M Warrick
James A Spudich
Stanford University · USRosetta Stone (United States) · US

Funding

MYOSIN MOVEMENT IN VITRO: MOLECULAR CHARACTERIZATIONR01GM033289 · NIGMS · STANFORD UNIVERSITY · PI SPUDICH, JAMES · 1985 to 2024
$13.6M
NIGMS NIH HHS GM404509NIGMS NIH HHS R01 GM033289
6 · The paper itself

Abstract

backgroundDuring cytokinesis, the cell's equator contracts against the cell's global stiffness. Identifying the biochemical basis for these mechanical parameters is essential for understanding how cells divide. To achieve this goal, the distribution and flux of the cell division machinery must be quantified. Here we report the first quantitative analysis of the distribution and flux of myosin-II, an essential element of the contractile ring.

resultsThe fluxes of myosin-II in the furrow cortex, the polar cortex, and the cytoplasm were examined using ratio imaging of GFP fusion proteins expressed in Dictyostelium. The peak concentration of GFP-myosin-II in the furrow cortex is 1.8-fold higher than in the polar cortex and 2.0-fold higher than in the cytoplasm. The myosin-II in the furrow cortex, however, represents only 10% of the total cellular myosin-II. An estimate of the minimal amount of this motor needed to produce the required force for cell cleavage fits well with this 10% value. The cell may, therefore, regulate the amount of myosin-II sent to the furrow cortex in accordance with the amount needed there. Quantitation of the distribution and flux of a mutant myosin-II that is defective in phosphorylation-dependent thick filament disassembly confirms that heavy chain phosphorylation regulates normal recruitment to the furrow cortex.

conclusionThe analysis indicates that myosin-II flux through the cleavage furrow cortex is regulated by thick filament phosphorylation. Further, the amount of myosin-II observed in the furrow cortex is in close agreement with the amount predicted to be required from a simple theoretical analysis.

Indexed as

AnimalsCell DivisionCell MembraneCells, CulturedCytoplasmCytoskeletonDictyosteliumGenetic VectorsGreen Fluorescent ProteinsLuminescent ProteinsMitosisMyosin Type IIRecombinant Fusion ProteinsSpindle ApparatusTransfectionGreen Fluorescent ProteinsLuminescent ProteinsMyosin Type IIRecombinant Fusion Proteins

Identifiers

PMID11860600
PMCPMC65686
OpenAlexW2160175985

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.