Evidence map›Paper›PMID 9230079›Full record

ArticleThe Journal of cell biology1997

The human Arp2/3 complex is composed of evolutionarily conserved subunits and is localized to cellular regions of dynamic actin filament assembly.

M D Welch, A H DePace, S Verma, A Iwamatsu, T J Mitchison

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 230 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
230citing papers in PubMed, 1 pooled it
19.3field-weighted citation impact, top 1% 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

230 citing papers in PubMed, 1 synthesis or guideline pooled it, 513 citations in OpenAlex.

  1. Pooled it
  2. Trial
  3. Article
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  8. Article
  9. Arp2/3-mediated bidirectional actin assembly by SPIN90 dimers.Nature structural & molecular biology · 2025
    Article
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  12. Review
  13. ComprehensiveOncology reports · 2025
    Review
  14. Article
  15. Article
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  17. Article
  18. Article
  19. Genes Co-Expressed withInternational journal of molecular sciences · 2024
    Article
  20. Article

170 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.

M D WelchDepartment of Cellular and Molecular Pharmacology, University of California, San Francisco, California 94143-0450, USA. welch@cgl.ucsf.edu
A H DePace
S Verma
A Iwamatsu
T J Mitchison
University of California, San Francisco · USKirin (Japan) · JP

Funding

ACTIN DYNAMICS AND CELL LOCOMOTIONR01GM048027 · NIGMS · UNIVERSITY OF CALIFORNIA SAN FRANCISCO · PI MITCHISON, TIMOTHY J · 1992 to 2004
$1.8M
NIGMS NIH HHS GM48027NIGMS NIH HHS R01 GM048027
6 · The paper itself

Abstract

The Arp2/3 protein complex has been implicated in the control of actin polymerization in cells. The human complex consists of seven subunits which include the actin related proteins Arp2 and Arp3, and five others referred to as p41-Arc, p34-Arc, p21-Arc, p20-Arc, and p16-Arc (p omplex). We have determined the predicted amino acid sequence of all seven subunits. Each has homologues in diverse eukaryotes, implying that the structure and function of the complex has been conserved through evolution. Human Arp2 and Arp3 are very similar to family members from other species. p41-Arc is a new member of the Sop2 family of WD (tryptophan and aspartate) repeat-containing proteins and may be posttranslationally modified, suggesting that it may be involved in regulating the activity and/or localization of the complex. p34-Arc, p21-Arc, p20-Arc, and p16-Arc define novel protein families. We sought to evaluate the function of the Arp2/3 complex in cells by determining its intracellular distribution. Arp3, p34-Arc, and p21-Arc were localized to the lamellipodia of stationary and locomoting fibroblasts, as well to Listeria monocytogenes assembled actin tails. They were not detected in cellular bundles of actin filaments. Taken together with the ability of the Arp2/3 complex to induce actin polymerization, these observations suggest that the complex promotes actin assembly in lamellipodia and may participate in lamellipodial protrusion.

Indexed as

Cytoskeletal ProteinsActin CytoskeletonActin-Related Protein 2Actin-Related Protein 2-3 ComplexActin-Related Protein 3ActinsAmino Acid SequenceAnimalsCarrier ProteinsCell MovementChick EmbryoFibroblastsHumansListeria monocytogenesMicrofilament ProteinsMolecular Sequence DataActin-Related Protein 2Actin-Related Protein 2-3 ComplexActin-Related Protein 3ActinsACTR2 protein, humanACTR3 protein, humanARPC3 protein, humanCarrier ProteinsCytoskeletal ProteinsMicrofilament Proteins

Identifiers

PMID9230079
PMCPMC2138188
OpenAlexW2157815908

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.