Evidence map›Paper›PMID 28282023›Full record

ArticleeLife2017

Competition between Tropomyosin, Fimbrin, and ADF/Cofilin drives their sorting to distinct actin filament networks.

Jenna R Christensen, Glen M Hocky, Kaitlin E Homa, Alisha N Morganthaler, Sarah E Hitchcock-DeGregori, Gregory A Voth, David R Kovar

Open access · goldAbstract read
In one paragraph

Article in eLife, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.

0numbers the graph read from it
0cells of the map it votes in
57citing papers in PubMed
6.6field-weighted citation impact, top 2% 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

57 citing papers in PubMed, 92 citations in OpenAlex.

  1. Article
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  5. A role for cross-linking proteins in actin filament network organization and force generation.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
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  11. Review
  12. Mechanisms of actin disassembly and turnover.The Journal of cell biology · 2023
    Review
  13. Article
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  15. Article
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  17. Review
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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

7 authors at 2 institutions in 1 country.

Jenna R ChristensenDepartment of Molecular Genetics and Cell Biology, The University of Chicago, Chicago, United States.ORCID 0000-0003-0323-6169
Glen M HockyDepartment of Chemistry, The University of Chicago, Chicago, United States.ORCID 0000-0002-5637-0698
Kaitlin E HomaDepartment of Molecular Genetics and Cell Biology, The University of Chicago, Chicago, United States.
Alisha N MorganthalerDepartment of Molecular Genetics and Cell Biology, The University of Chicago, Chicago, United States.
Sarah E Hitchcock-DeGregoriDepartment of Pathology and Laboratory Medicine, Robert Wood Johnson Medical School, Rutgers University, New Brunswick, United States.
Gregory A VothDepartment of Chemistry, The University of Chicago, Chicago, United States.
David R KovarDepartment of Molecular Genetics and Cell Biology, The University of Chicago, Chicago, United States.ORCID 0000-0002-5747-0949
University of Chicago · USRutgers, The State University of New Jersey · US

Funding

Mechanisms of Formin-Mediated Actin Filament Assembly - Renewal 01 - ResubmissionR01GM079265 · NIGMS · UNIVERSITY OF CHICAGO · PI KOVAR, DAVID R · 2007 to 2023
$4.5M
Functional Reconstitution of Yeast ExocytosisR01GM071832 · NIGMS · RICE UNIVERSITY · PI MCNEW, JAMES A · 2006 to 2010
$1.4M
Computational studies of Arp2/3 activation and deactivationF32GM113415 · NIGMS · UNIVERSITY OF CHICAGO · PI HOCKY, GLEN · 2015 to 2017
$162k
NIGMS NIH HHS F32 GM113415NIGMS NIH HHS R01 GM071832NIGMS NIH HHS R01 GM079265
6 · The paper itself

Abstract

The fission yeast actin cytoskeleton is an ideal, simplified system to investigate fundamental mechanisms behind cellular self-organization. By focusing on the stabilizing protein tropomyosin Cdc8, bundling protein fimbrin Fim1, and severing protein coffin Adf1, we examined how their pairwise and collective interactions with actin filaments regulate their activity and segregation to functionally diverse F-actin networks. Utilizing multi-color TIRF microscopy of in vitro reconstituted F-actin networks, we observed and characterized two distinct Cdc8 cables loading and spreading cooperatively on individual actin filaments. Furthermore, Cdc8, Fim1, and Adf1 all compete for association with F-actin by different mechanisms, and their cooperative association with actin filaments affects their ability to compete. Finally, competition between Fim1 and Adf1 for F-actin synergizes their activities, promoting rapid displacement of Cdc8 from a dense F-actin network. Our findings reveal that competitive and cooperative interactions between actin binding proteins help define their associations with different F-actin networks.

Indexed as

Protein MultimerizationActin CytoskeletonActin Depolymerizing FactorsCell Cycle ProteinsMembrane GlycoproteinsMicrofilament ProteinsMicroscopy, FluorescenceSchizosaccharomycesSchizosaccharomyces pombe ProteinsActin Depolymerizing FactorsAdf1 protein, S pombeCdc8 protein, S pombeCell Cycle ProteinsMembrane GlycoproteinsMicrofilament ProteinsplastinSchizosaccharomyces pombe Proteinsactin depolymerizing factorbiophysicscell biologycofilinfimbrinfission yeastS. pombestructural biologytropomyosin

Identifiers

PMID28282023
PMCPMC5404920
OpenAlexW2592055451

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.