Evidence map›Paper›PMID 25995115›Full record

ArticleNature communications2015

Single-molecule imaging of a three-component ordered actin disassembly mechanism.

Silvia Jansen, Agnieszka Collins, Samantha M Chin, Casey A Ydenberg, Jeff Gelles, Bruce L Goode

Abstract read
In one paragraph

Article in Nature communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 75 papers.

0numbers the graph read from it
0cells of the map it votes in
75citing 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

75 citing papers in PubMed.

  1. Article
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  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
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  11. Article
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  14. Article
  15. Mechanisms of actin disassembly and turnover.The Journal of cell biology · 2023
    Review
  16. Article
  17. Article
  18. Article
  19. Biochemical and mechanical regulation of actin dynamics.Nature reviews. Molecular cell biology · 2022
    Review
  20. Article

15 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

6 authors.

Silvia JansenDepartment of Biology, Rosenstiel Basic Medical Science Research Center, Brandeis University, 415 South street, Waltham, Massachusetts 02454, USA.
Agnieszka CollinsDepartment of Biology, Rosenstiel Basic Medical Science Research Center, Brandeis University, 415 South street, Waltham, Massachusetts 02454, USA.
Samantha M ChinDepartment of Biology, Rosenstiel Basic Medical Science Research Center, Brandeis University, 415 South street, Waltham, Massachusetts 02454, USA.
Casey A YdenbergDepartment of Biology, Rosenstiel Basic Medical Science Research Center, Brandeis University, 415 South street, Waltham, Massachusetts 02454, USA.
Jeff GellesDepartment of Biochemistry, Brandeis University, 415 South street, Waltham, Massachusetts 02454, USA.ORCID 0000000179103421
Bruce L GoodeDepartment of Biology, Rosenstiel Basic Medical Science Research Center, Brandeis University, 415 South street, Waltham, Massachusetts 02454, USA.

Funding

MECHNISMS REGULATING ACTIN ASSEMBLYR01GM063691 · NIGMS · BRANDEIS UNIVERSITY · PI GOODE, BRUCE L · 2002 to 2019
$7.5M
Molecular Mechanisms coordinating the actin and microtubule cytoskeletonsR01GM098143 · NIGMS · BRANDEIS UNIVERSITY · PI GELLES, JEFF, GOODE, BRUCE L · 2012 to 2019
$2.6M
NIGMS NIH HHS GM063691NIGMS NIH HHS GM098143NIGMS NIH HHS R01 GM063691NIGMS NIH HHS R01 GM098143
6 · The paper itself

Abstract

The mechanisms by which cells destabilize and rapidly disassemble filamentous actin networks have remained elusive; however, Coronin, Cofilin and AIP1 have been implicated in this process. Here using multi-wavelength single-molecule fluorescence imaging, we show that mammalian Cor1B, Cof1 and AIP1 work in concert through a temporally ordered pathway to induce highly efficient severing and disassembly of actin filaments. Cor1B binds to filaments first, and dramatically accelerates the subsequent binding of Cof1, leading to heavily decorated, stabilized filaments. Cof1 in turn recruits AIP1, which rapidly triggers severing and remains bound to the newly generated barbed ends. New growth at barbed ends generated by severing was blocked specifically in the presence of all three proteins. This activity enabled us to reconstitute and directly visualize single actin filaments being rapidly polymerized by formins at their barbed ends while simultanteously being stochastically severed and capped along their lengths, and disassembled from their pointed ends.

Indexed as

Actin CytoskeletonAnimalsCofilin 1Escherichia coliHumansMiceMicrofilament ProteinsMicroscopy, FluorescenceRabbitsras GTPase-Activating ProteinsCofilin 1coronin proteinsDab2ip protein, mouseMicrofilament Proteinsras GTPase-Activating Proteins

Identifiers

PMID25995115
PMCPMC4443854

What OpenQuestion holds

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LicenceCC BY
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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.