Evidence map›Paper›PMID 21642440›Full record

ArticleThe Journal of biological chemistry2011

Actin filament bundling by fimbrin is important for endocytosis, cytokinesis, and polarization in fission yeast.

Colleen T Skau, David S Courson, Andrew J Bestul, Jonathan D Winkelman, Ronald S Rock, Vladimir Sirotkin, David R Kovar

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 81 papers.

0numbers the graph read from it
0cells of the map it votes in
81citing papers in PubMed
4.4field-weighted citation impact, top 5% 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

81 citing papers in PubMed, 131 citations in OpenAlex.

  1. Article
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  8. Article
  9. 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
  10. bioRxiv : the preprint server for biology · 2024
    Article
  11. Article
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  16. Review
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21 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

7 authors at 3 institutions in 1 country.

Colleen T SkauDepartment of Molecular Genetics and Cell Biology, University of Chicago, Chicago Illinois 60637, USA.
David S Courson
Andrew J Bestul
Jonathan D Winkelman
Ronald S Rock
Vladimir Sirotkin
David R Kovar
University of Chicago · USSUNY Upstate Medical University · USUniversity of Illinois Chicago · US

Funding

Molecular And Cellular Biology Training ProgramT32GM007183 · NIGMS · UNIVERSITY OF CHICAGO · PI GLICK, BENJAMIN S, RICE, PHOEBE A · 1985 to 2021
$23.9M
Mechanisms of Formin-Mediated Actin Filament Assembly - Renewal 01 - ResubmissionR01GM079265 · NIGMS · UNIVERSITY OF CHICAGO · PI KOVAR, DAVID R · 2007 to 2023
$4.5M
Allostery in myosins studied at the molecular levelR01GM078450 · NIGMS · UNIVERSITY OF CHICAGO · PI ROCK, RONALD S · 2006 to 2015
$2.8M
NIGMS NIH HHS R01 GM078450NIGMS NIH HHS R01GM078450NIGMS NIH HHS R01 GM079265NIGMS NIH HHS R01GM079265NIGMS NIH HHS T32 GM007183
6 · The paper itself

Abstract

Through the coordinated action of diverse actin-binding proteins, cells simultaneously assemble actin filaments with distinct architectures and dynamics to drive different processes. Actin filament cross-linking proteins organize filaments into higher order networks, although the requirement of cross-linking activity in cells has largely been assumed rather than directly tested. Fission yeast Schizosaccharomyces pombe assembles actin into three discrete structures: endocytic actin patches, polarizing actin cables, and the cytokinetic contractile ring. The fission yeast filament cross-linker fimbrin Fim1 primarily localizes to Arp2/3 complex-nucleated branched filaments of the actin patch and by a lesser amount to bundles of linear antiparallel filaments in the contractile ring. It is unclear whether Fim1 associates with bundles of parallel filaments in actin cables. We previously discovered that a principal role of Fim1 is to control localization of tropomyosin Cdc8, thereby facilitating cofilin-mediated filament turnover. Therefore, we hypothesized that the bundling ability of Fim1 is dispensable for actin patches but is important for the contractile ring and possibly actin cables. By directly visualizing actin filament assembly using total internal reflection fluorescence microscopy, we determined that Fim1 bundles filaments in both parallel and antiparallel orientations and efficiently bundles Arp2/3 complex-branched filaments in the absence but not the presence of actin capping protein. Examination of cells exclusively expressing a truncated version of Fim1 that can bind but not bundle actin filaments revealed that bundling activity of Fim1 is in fact important for all three actin structures. Therefore, fimbrin Fim1 has diverse roles as both a filament "gatekeeper" and as a filament cross-linker.

Indexed as

Actin CytoskeletonActin-Related Protein 2-3 ComplexCell Cycle ProteinsCytokinesisEndocytosisMembrane GlycoproteinsMicrofilament ProteinsSchizosaccharomycesSchizosaccharomyces pombe ProteinsActin-Related Protein 2-3 ComplexCdc8 protein, S pombeCell Cycle ProteinsMembrane GlycoproteinsMicrofilament ProteinsplastinSchizosaccharomyces pombe Proteins

Identifiers

PMID21642440
PMCPMC3143655
OpenAlexW2052985914

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.