Evidence map›Paper›PMID 10366597›Full record

ArticleThe Journal of cell biology1999

Aip1p interacts with cofilin to disassemble actin filaments.

A A Rodal, J W Tetreault, P Lappalainen, D G Drubin, D C Amberg

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 104 papers.

0numbers the graph read from it
0cells of the map it votes in
104citing papers in PubMed
4.0field-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

104 citing papers in PubMed, 220 citations in OpenAlex.

  1. Trial
  2. Article
  3. A genome-wide CRISPR screen defines host determinants of earlybioRxiv : the preprint server for biology · 2026
    Article
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  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Mechanisms of actin disassembly and turnover.The Journal of cell biology · 2023
    Review
  11. Article
  12. Article
  13. Article
  14. Biochemical and mechanical regulation of actin dynamics.Nature reviews. Molecular cell biology · 2022
    Review
  15. Article
  16. Molecular biology of autoinflammatory diseases.Inflammation and regeneration · 2021
    Review
  17. Article
  18. Review
  19. Review
  20. Article

44 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

5 authors at 2 institutions in 2 countries.

A A RodalDepartment of Molecular and Cell Biology, University of California at Berkeley, Berkeley, California 94720, USA.
J W Tetreault
P Lappalainen
D G Drubin
D C Amberg
University of Helsinki · FIUniversity of California, Berkeley · US

Funding

Molecular Analysis of the Yeast Actin CytoskeletonR37GM042759 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI DRUBIN, DAVID G · 2006 to 2015
$4.0M
Regulation of Actin DynamicsR01GM056189 · NIGMS · UPSTATE MEDICAL UNIVERSITY · PI AMBERG, DAVID C · 1998 to 2010
$2.3M
MOLECULAR ANALYSIS OF THE YEAST ACTIN CYTOSKELETONR01GM042759 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI DRUBIN, DAVID G. · 1989 to 2005
$1.6M
NIGMS NIH HHS GM42759NIGMS NIH HHS GM56189NIGMS NIH HHS R01 GM042759NIGMS NIH HHS R01 GM056189NIGMS NIH HHS R37 GM042759
6 · The paper itself

Abstract

Actin interacting protein 1 (Aip1) is a conserved component of the actin cytoskeleton first identified in a two-hybrid screen against yeast actin. Here, we report that Aip1p also interacts with the ubiquitous actin depolymerizing factor cofilin. A two-hybrid-based approach using cofilin and actin mutants identified residues necessary for the interaction of actin, cofilin, and Aip1p in an apparent ternary complex. Deletion of the AIP1 gene is lethal in combination with cofilin mutants or act1-159, an actin mutation that slows the rate of actin filament disassembly in vivo. Aip1p localizes to cortical actin patches in yeast cells, and this localization is disrupted by specific actin and cofilin mutations. Further, Aip1p is required to restrict cofilin localization to cortical patches. Finally, biochemical analyses show that Aip1p causes net depolymerization of actin filaments only in the presence of cofilin and that cofilin enhances binding of Aip1p to actin filaments. We conclude that Aip1p is a cofilin-associated protein that enhances the filament disassembly activity of cofilin and restricts cofilin localization to cortical actin patches.

Indexed as

Actin Depolymerizing FactorsActinsAmino Acid SequenceAntibodiesBinding SitesCloning, MolecularCytoskeletonFungal ProteinsGenes, LethalKineticsMicrofilament ProteinsModels, MolecularMolecular Sequence DataMutationPolymersProtein BindingActin Depolymerizing Factorsactin interacting protein 1ActinsAntibodiesFungal ProteinsMicrofilament ProteinsPolymers

Identifiers

PMID10366597
PMCPMC2133144
OpenAlexW2080945459

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.