Evidence map›Paper›PMID 25451933›Full record

ArticleThe Journal of biological chemistry2015

Aip1 promotes actin filament severing by cofilin and regulates constriction of the cytokinetic contractile ring.

Qian Chen, Naomi Courtemanche, Thomas D Pollard

Open access · hybridAbstract readComparative Study
In one paragraph

Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
3.9field-weighted citation impact, top 6% 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

44 citing papers in PubMed, 65 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Beyond Glycolysis: Aldolase A Is a Novel Effector in Reelin-Mediated Dendritic Development.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2024
    Article
  6. Article
  7. Mechanisms of actin disassembly and turnover.The Journal of cell biology · 2023
    Review
  8. Article
  9. Article
  10. Article
  11. Review
  12. Biochemical and mechanical regulation of actin dynamics.Nature reviews. Molecular cell biology · 2022
    Review
  13. Review
  14. Article
  15. Article
  16. Review
  17. Article
  18. Review
  19. Article
  20. Role of Cofilin in Alzheimer's Disease.Frontiers in cell and developmental biology · 2020
    Review
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.

Qian ChenFrom the Departments of Molecular Cellular and Developmental Biology.
Naomi CourtemancheFrom the Departments of Molecular Cellular and Developmental Biology.
Thomas D PollardFrom the Departments of Molecular Cellular and Developmental Biology, Molecular Biophysics and Biochemistry, and Cell Biology Yale University, New Haven, Connecticut 06520-8103 thomas.pollard@yale.edu.
Yale University · US

Funding

MOLECULAR MECHANISMS OF CELLULAR MOTILITYR01GM026338 · NIGMS · YALE UNIVERSITY · PI POLLARD, THOMAS D. · 1985 to 2020
$9.8M
NIGMS NIH HHS R01 GM026338NIGMS NIH HHS R01GM026338
6 · The paper itself

Abstract

Aip1 (actin interacting protein 1) is ubiquitous in eukaryotic organisms, where it cooperates with cofilin to disassemble actin filaments, but neither its mechanism of action nor its biological functions have been clear. We purified both fission yeast and human Aip1 and investigated their biochemical activities with or without cofilin. Both types of Aip1 bind actin filaments with micromolar affinities and weakly nucleate actin polymerization. Aip1 increases up to 12-fold the rate that high concentrations of yeast or human cofilin sever actin filaments, most likely by competing with cofilin for binding to the side of actin filaments, reducing the occupancy of the filaments by cofilin to a range favorable for severing. Aip1 does not cap the barbed ends of filaments severed by cofilin. Fission yeast lacking Aip1 are viable and assemble cytokinetic contractile rings normally, but rings in these Δaip1 cells accumulate 30% less myosin II. Further, these mutant cells initiate the ingression of cleavage furrows earlier than normal, shortening the stage of cytokinetic ring maturation by 50%. The Δaip1 mutation has negative genetic interactions with deletion mutations of both capping protein subunits and cofilin mutations with severing defects, but no genetic interaction with deletion of coronin.

Indexed as

MutationActin CytoskeletonActin Depolymerizing FactorsActinsAdenosine TriphosphateCytokinesisGene DeletionHumansMicrofilament ProteinsMicroscopy, FluorescenceProtein ConformationRecombinant ProteinsSchizosaccharomycesTemperatureTwo-Hybrid System TechniquesActin Depolymerizing Factorsactin interacting protein 1ActinsAdenosine TriphosphateMicrofilament ProteinsRecombinant ProteinsActinAip1CofilinCytokinesisMyosinSeveringYeast

Identifiers

PMID25451933
PMCPMC4303679
OpenAlexW2331356571

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.