Evidence map›Paper›PMID 27647921›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2016

Molecular organization of cytokinesis nodes and contractile rings by super-resolution fluorescence microscopy of live fission yeast.

Caroline Laplante, Fang Huang, Irene R Tebbs, Joerg Bewersdorf, Thomas D Pollard

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 84 papers.

0numbers the graph read from it
0cells of the map it votes in
84citing papers in PubMed
–field-weighted citation impact
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

84 citing papers in PubMed.

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  17. Non-muscle myosin 2 at a glance.Journal of cell science · 2023
    Review
  18. Article
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  20. Article

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

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors.

Caroline LaplanteDepartment of Molecular Cellular and Developmental Biology, Yale University, New Haven, CT 06520.
Fang HuangDepartment of Cell Biology, Yale University, New Haven, CT 06520.
Irene R TebbsDepartment of Molecular Cellular and Developmental Biology, Yale University, New Haven, CT 06520; Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520.
Joerg BewersdorfDepartment of Cell Biology, Yale University, New Haven, CT 06520; Department of Biomedical Engineering, Yale University, New Haven, CT 06520.
Thomas D PollardDepartment of Molecular Cellular and Developmental Biology, Yale University, New Haven, CT 06520; Department of Cell Biology, Yale University, New Haven, CT 06520; Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520; thomas.pollard@yale.edu.

Funding

Yale Clinical and Translational Science Award (U Component)UL1TR001863 · NCATS · YALE UNIVERSITY · PI John H. Krystal, LUCILA OHNO-MACHADO · 2016 to 2026
$102.9M
Yale Diabetes Research CenterP30DK045735 · NIDDK · YALE UNIVERSITY · PI Kevan C Herold, GERALD I SHULMAN · 1993 to 2026
$44.0M
Mechanism of cytokinesis in fission yeastR01GM026132 · NIGMS · YALE UNIVERSITY · PI POLLARD, THOMAS D. · 1985 to 2021
$8.8M
NCATS NIH HHS UL1 TR001863NIDDK NIH HHS P30 DK045735NIGMS NIH HHS R01 GM026132Wellcome Trust 203285/Z/16/Z
6 · The paper itself

Abstract

Cytokinesis in animals, fungi, and amoebas depends on the constriction of a contractile ring built from a common set of conserved proteins. Many fundamental questions remain about how these proteins organize to generate the necessary tension for cytokinesis. Using quantitative high-speed fluorescence photoactivation localization microscopy (FPALM), we probed this question in live fission yeast cells at unprecedented resolution. We show that nodes, protein assembly precursors to the contractile ring, are discrete structural units with stoichiometric ratios and distinct distributions of constituent proteins. Anillin Mid1p, Fes/CIP4 homology-Bin/amphiphysin/Rvs (F-BAR) Cdc15p, IQ motif containing GTPase-activating protein (IQGAP) Rng2p, and formin Cdc12p form the base of the node that anchors the ends of myosin II tails to the plasma membrane, with myosin II heads extending into the cytoplasm. This general node organization persists in the contractile ring where nodes move bidirectionally during constriction. We observed the dynamics of the actin network during cytokinesis, starting with the extension of short actin strands from nodes, which sometimes connected neighboring nodes. Later in cytokinesis, a broad network of thick bundles coalesced into a tight ring around the equator of the cell. The actin ring was ∼125 nm wide and ∼125 nm thick. These observations establish the organization of the proteins in the functional units of a cytokinetic contractile ring.

Indexed as

CytokinesisActin CytoskeletonActinsInterphaseMicroscopy, FluorescenceModels, MolecularPhenotypeSchizosaccharomycesSchizosaccharomyces pombe ProteinsActinsSchizosaccharomyces pombe Proteinscontractile ringcytokinesiscytokinetic nodesfission yeastsuper resolution

Identifiers

PMID27647921
PMCPMC5056082

What OpenQuestion holds

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Registered trials

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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.