Evidence map›Paper›PMID 22740629›Full record

ArticleMolecular biology of the cell2012

α-Actinin and fimbrin cooperate with myosin II to organize actomyosin bundles during contractile-ring assembly.

Damien Laporte, Nikola Ojkic, Dimitrios Vavylonis, Jian-Qiu Wu

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers.

0numbers the graph read from it
0cells of the map it votes in
61citing papers in PubMed
3.8field-weighted citation impact, top 6% 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

61 citing papers in PubMed, 91 citations in OpenAlex.

  1. Article
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  16. Immune cells fold and damage fungal hyphae.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  17. Article
  18. Review
  19. Article
  20. Plastin 3 in X-Linked Osteoporosis: Imbalance of CaFrontiers in cell and developmental biology · 2020
    Review

1 more citing papers are in PubMed but not listed here.

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.

Damien LaporteDepartment of Molecular Genetics, The Ohio State University, Columbus, OH 43210, USA.
Nikola Ojkic
Dimitrios Vavylonis
Jian-Qiu Wu
Lehigh University · USThe Ohio State University · US

Funding

Molecular Mechanism of the Contractile-Ring Assembly in Fission Yeast CytokinesisR01GM086546 · NIGMS · OHIO STATE UNIVERSITY · PI WU, JIAN-QIU · 2009 to 2013
$1.4M
Modeling and analysis of actin filament organization in yeastR01GM098430 · NIGMS · LEHIGH UNIVERSITY · PI VAVYLONIS, DIMITRIOS · 2012 to 2016
$1.3M
Computational Analysis and Modeling of Contractile Ring AssemblyR21GM083928 · NIGMS · LEHIGH UNIVERSITY · PI HUANG, SHARON XIAOLEI, VAVYLONIS, DIMITRIOS · 2008 to 2009
$386k
NIGMS NIH HHS R01 GM086546NIGMS NIH HHS R01GM086546NIGMS NIH HHS R01 GM098430NIGMS NIH HHS R01GM098430NIGMS NIH HHS R21 GM083928NIGMS NIH HHS R21GM083928
6 · The paper itself

Abstract

The actomyosin contractile ring assembles through the condensation of a broad band of nodes that forms at the cell equator in fission yeast cytokinesis. The condensation process depends on actin filaments that interconnect nodes. By mutating or titrating actin cross-linkers α-actinin Ain1 and fimbrin Fim1 in live cells, we reveal that both proteins are involved in node condensation. Ain1 and Fim1 stabilize the actin cytoskeleton and modulate node movement, which prevents nodes and linear structures from aggregating into clumps and allows normal ring formation. Our computer simulations modeling actin filaments as semiflexible polymers reproduce the experimental observations and provide a model of how actin cross-linkers work with other proteins to regulate actin-filament orientations inside actin bundles and organize the actin network. As predicted by the simulations, doubling myosin II Myo2 level rescues the node condensation defects caused by Ain1 overexpression. Taken together, our work supports a cooperative process of ring self-organization driven by the interaction between actin filaments and myosin II, which is progressively stabilized by the cross-linking proteins.

Indexed as

CytokinesisActin CytoskeletonActininActomyosinCell CycleComputer SimulationMembrane GlycoproteinsMicrofilament ProteinsMicroscopy, FluorescenceModels, BiologicalMyosin Type IIProtein BindingProtein MultimerizationProtein StabilitySchizosaccharomycesSchizosaccharomyces pombe ProteinsActininActomyosinain1 protein, S pombeMembrane GlycoproteinsMicrofilament ProteinsMyosin Type IIplastinSchizosaccharomyces pombe Proteins

Identifiers

PMID22740629
PMCPMC3418305
OpenAlexW2123735680

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.