Evidence map›Paper›PMID 24518936›Full record

ArticleNature communications2014

Structural analysis of the transitional state of Arp2/3 complex activation by two actin-bound WCAs.

Malgorzata Boczkowska, Grzegorz Rebowski, David J Kast, Roberto Dominguez

Open access · bronzeAbstract read
In one paragraph

Article in Nature communications, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
4.1field-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

47 citing papers in PubMed, 69 citations in OpenAlex.

  1. Article
  2. Article
  3. The role of actin cytoskeleton component Arp2/3 in inflammatory response.Frontiers in cell and developmental biology · 2025
    Review
  4. Article
  5. Article
  6. Transition State of Arp2/3 Complex Activation by Actin-Bound Dimeric Nucleation-Promoting Factor.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
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  10. Review
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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

4 authors at 1 institution in 1 country.

Malgorzata Boczkowska1] Department of Physiology, Perelman School of Medicine, University of Pennsylvania, 728 Clinical Research Building, 415 Curie Boulevard, Philadelphia, Pennsylvania 19104, USA [2].
Grzegorz Rebowski1] Department of Physiology, Perelman School of Medicine, University of Pennsylvania, 728 Clinical Research Building, 415 Curie Boulevard, Philadelphia, Pennsylvania 19104, USA [2].
David J KastDepartment of Physiology, Perelman School of Medicine, University of Pennsylvania, 728 Clinical Research Building, 415 Curie Boulevard, Philadelphia, Pennsylvania 19104, USA.
Roberto DominguezDepartment of Physiology, Perelman School of Medicine, University of Pennsylvania, 728 Clinical Research Building, 415 Curie Boulevard, Philadelphia, Pennsylvania 19104, USA.
University of Pennsylvania · US

Funding

Structural-Functional Basis of Actin Cytoskeleton DynamicsR01GM073791 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI DOMINGUEZ, ROBERTO · 2005 to 2025
$7.0M
NIGMS NIH HHS R01 GM073791
6 · The paper itself

Abstract

Actin filament nucleation and branching by Arp2/3 complex is activated by nucleation-promoting factors (NPFs), whose C-terminal WCA region contains binding sites for actin (W) and Arp2/3 complex (CA). It is debated whether one or two NPFs are required for activation. Here we present evidence in support of the two-NPF model and show that actin plays a crucial role in the interactions of two mammalian NPFs, N-WASP and WAVE2, with Arp2/3 complex. Competition between actin-WCA and glia maturation factor (GMF) for binding to Arp2/3 complex suggests that during activation the first actin monomer binds at the barbed end of Arp2. Based on distance constraints obtained by time-resolved fluorescence resonance energy transfer, we define the relative position of the two actin-WCAs on Arp2/3 complex and propose an atomic model of the 11-subunit transitional complex.

Indexed as

Actin-Related Protein 2Actin-Related Protein 2-3 ComplexActin-Related Protein 3ActinsAnimalsCattleFluorescence Resonance Energy TransferGlia Maturation FactorMiceProtein Structure, TertiaryWiskott-Aldrich Syndrome Protein FamilyWiskott-Aldrich Syndrome Protein, NeuronalActin-Related Protein 2Actin-Related Protein 2-3 ComplexActin-Related Protein 3ActinsGlia Maturation FactorWiskott-Aldrich Syndrome Protein FamilyWiskott-Aldrich Syndrome Protein, Neuronal

Identifiers

PMID24518936
PMCPMC4364448
OpenAlexW2059835251

What OpenQuestion holds

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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.