Evidence map›Paper›PMID 32723865›Full record

ArticleThe Journal of biological chemistry2020

Catastrophic actin filament bursting by cofilin, Aip1, and coronin.

Vivian W Tang, Ambika V Nadkarni, William M Brieher

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

15 citing papers in PubMed, 28 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Mechanisms of actin disassembly and turnover.The Journal of cell biology · 2023
    Review
  5. Article
  6. The multiple links between actin and mitochondria.Nature reviews. Molecular cell biology · 2023
    Review
  7. Biochemical and mechanical regulation of actin dynamics.Nature reviews. Molecular cell biology · 2022
    Review
  8. Article
  9. Article
  10. Article
  11. Celebrating 20 years of live single-actin-filament studies with five golden rules.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  12. The Amoebal Model for Macropinocytosis.Sub-cellular biochemistry · 2022
    Article
  13. Article
  14. Review
  15. Article
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

3 authors at 1 institution in 1 country.

Vivian W TangDepartment of Cell and Developmental Biology, University of Illinois, Urbana-Champaign, Urbana, Illinois, USA.
Ambika V NadkarniDepartment of Cell and Developmental Biology, University of Illinois, Urbana-Champaign, Urbana, Illinois, USA.
William M BrieherDepartment of Cell and Developmental Biology, University of Illinois, Urbana-Champaign, Urbana, Illinois, USA. Electronic address: wbrieher@illinois.edu.
University of Illinois Urbana-Champaign · US

Funding

Actin Assembly at Cadherin Dependent Adherens JunctionsR01GM106106 · NIGMS · UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN · PI BRIEHER, WILLIAM · 2013 to 2022
$2.6M
Disrupting FSGS1-associated Actin Assembly in GlomerulosclerosisR01DK098398 · NIDDK · UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN · PI TANG, VIVIAN · 2013 to 2017
$1.4M
NIDDK NIH HHS R01 DK098398NIGMS NIH HHS R01 GM106106
6 · The paper itself

Abstract

Cofilin is an actin filament severing protein necessary for fast actin turnover dynamics. Coronin and Aip1 promote cofilin-mediated actin filament disassembly, but the mechanism is somewhat controversial. An early model proposed that the combination of cofilin, coronin, and Aip1 disassembled filaments in bursts. A subsequent study only reported severing. Here, we used EM to show that actin filaments convert directly into globular material. A monomer trap assay also shows that the combination of all three factors produces actin monomers faster than any two factors alone. We show that coronin accelerates the release of Pi from actin filaments and promotes highly cooperative cofilin binding to actin to create long stretches of polymer with a hypertwisted morphology. Aip1 attacks these hypertwisted regions along their sides, disintegrating them into monomers or short oligomers. The results are consistent with a catastrophic mode of disassembly, not enhanced severing alone.

Indexed as

4-ButyrolactoneAcetogeninsActin CytoskeletonActin Depolymerizing FactorsHumansMicrofilament Proteins4-ButyrolactoneAcetogeninsActin Depolymerizing Factorscoronin acetogeninMicrofilament ProteinsWDR1 protein, humanactinAip1burstingcell motilitycofilincoronincytoskeletondepolymerizationelectron microscopy (EM)

Identifiers

PMID32723865
PMCPMC7504925
OpenAlexW3046164575

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.