Evidence map›Paper›PMID 34214524›Full record

ArticleBiophysical journal2021

Formin Cdc12's specific actin assembly properties are tailored for cytokinesis in fission yeast.

Kaitlin E Homa, Vilmos Zsolnay, Caitlin A Anderson, Meghan E O'Connell, Erin M Neidt, Gregory A Voth, Tamara C Bidone, David R Kovar

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
1.0field-weighted citation impact, top 29% 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

6 citing papers in PubMed, 13 citations in OpenAlex.

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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

8 authors at 3 institutions in 1 country.

Kaitlin E HomaDepartment of Molecular Genetics and Cell Biology, Chicago, Illinois.
Vilmos ZsolnayGraduate Program in Biophysical Sciences, Chicago, Illinois.
Caitlin A AndersonDepartment of Molecular Genetics and Cell Biology, Chicago, Illinois.
Meghan E O'ConnellDepartment of Molecular Genetics and Cell Biology, Chicago, Illinois.
Erin M NeidtDepartment of Molecular Genetics and Cell Biology, Chicago, Illinois.
Gregory A VothDepartment of Chemistry, The James Franck Institute, Institute for Biophysical Dynamics and Computation Institute, Chicago, Illinois.
Tamara C BidoneDepartment of Biomedical Engineering, Salt Lake City, Utah; Scientific Computing and Imaging Institute, University of Utah, Salt Lake City, Utah. Electronic address: tamarabidone@sci.utah.edu.
David R KovarDepartment of Molecular Genetics and Cell Biology, Chicago, Illinois; Department of Biochemistry and Molecular Biology, The University of Chicago, Chicago, Illinois. Electronic address: drkovar@uchicago.edu.
Molecular Biology Consortium · USChicago Institute for Psychoanalysis · USUniversity of Utah · US

Funding

Molecular And Cellular Biology Training ProgramT32GM007183 · NIGMS · UNIVERSITY OF CHICAGO · PI GLICK, BENJAMIN S, RICE, PHOEBE A · 1985 to 2021
$23.9M
University of Chicago Initiative for Maximizing Student Development (IMSD) - Renewal 01R25GM109439 · NIGMS · UNIVERSITY OF CHICAGO · PI SCHWARTZ, NANCY B · 2014 to 2023
$5.7M
Graduate Program in Biophysical Sciences at the University of Chicago - Renewal 0T32EB009412 · NIBIB · UNIVERSITY OF CHICAGO · PI ENGEL, GREGORY S, SOSNICK, TOBIN R · 2009 to 2023
$4.9M
Mechanisms of Formin-Mediated Actin Filament Assembly - Renewal 01 - ResubmissionR01GM079265 · NIGMS · UNIVERSITY OF CHICAGO · PI KOVAR, DAVID R · 2007 to 2023
$4.5M
NIBIB NIH HHS T32 EB009412NIGMS NIH HHS R01 GM079265NIGMS NIH HHS R25 GM109439NIGMS NIH HHS T32 GM007183
6 · The paper itself

Abstract

Formins generate unbranched actin filaments by a conserved, processive actin assembly mechanism. Most organisms express multiple formin isoforms that mediate distinct cellular processes and facilitate actin filament polymerization by significantly different rates, but how these actin assembly differences correlate to cellular activity is unclear. We used a computational model of fission yeast cytokinetic ring assembly to test the hypothesis that particular actin assembly properties help tailor formins for specific cellular roles. Simulations run in different actin filament nucleation and elongation conditions revealed that variations in formin's nucleation efficiency critically impact both the probability and timing of contractile ring formation. To probe the physiological importance of nucleation efficiency, we engineered fission yeast formin chimera strains in which the FH1-FH2 actin assembly domains of full-length cytokinesis formin Cdc12 were replaced with the FH1-FH2 domains from functionally and evolutionarily diverse formins with significantly different actin assembly properties. Although Cdc12 chimeras generally support life in fission yeast, quantitative live-cell imaging revealed a range of cytokinesis defects from mild to severe. In agreement with the computational model, chimeras whose nucleation efficiencies are least similar to Cdc12 exhibit more severe cytokinesis defects, specifically in the rate of contractile ring assembly. Together, our computational and experimental results suggest that fission yeast cytokinesis is ideally mediated by a formin with properly tailored actin assembly parameters.

Indexed as

SchizosaccharomycesSchizosaccharomyces pombe ProteinsActin CytoskeletonActinsCytokinesisCytoskeletal ProteinsForminsActinsCdc12 protein, S pombeCytoskeletal ProteinsForminsSchizosaccharomyces pombe Proteins

Identifiers

PMID34214524
PMCPMC8390969
OpenAlexW3175350872

What OpenQuestion holds

Textmetadata
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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.