Evidence map›Paper›PMID 32917641›Full record

ArticleScience advances2020

Cryo-EM structure of NPF-bound human Arp2/3 complex and activation mechanism.

Austin Zimmet, Trevor Van Eeuwen, Malgorzata Boczkowska, Grzegorz Rebowski, Kenji Murakami, Roberto Dominguez

Open access · goldAbstract read
In one paragraph

Article in Science advances, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.

0numbers the graph read from it
0cells of the map it votes in
52citing papers in PubMed
6.3field-weighted citation impact, top 2% 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

52 citing papers in PubMed, 85 citations in OpenAlex.

  1. Article
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  9. Arp2/3-mediated bidirectional actin assembly by SPIN90 dimers.Nature structural & molecular biology · 2025
    Article
  10. Article
  11. Article
  12. Article
  13. Molecular mechanism of Arp2/3 complex activation by nucleation-promoting factors and an actin monomer.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  14. Article
  15. Article
  16. The role of actin cytoskeleton component Arp2/3 in inflammatory response.Frontiers in cell and developmental biology · 2025
    Review
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  18. Article
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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

6 authors at 1 institution in 1 country.

Austin ZimmetDepartment of Physiology, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA 19104, USA.ORCID 0000-0002-2582-5071
Trevor Van EeuwenDepartment of Biochemistry and Biophysics, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA 19104, USA.ORCID 0000-0003-0549-1702
Malgorzata BoczkowskaDepartment of Physiology, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA 19104, USA.ORCID 0000-0003-1677-023X
Grzegorz RebowskiDepartment of Physiology, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA 19104, USA.ORCID 0000-0002-0766-6302
Kenji MurakamiDepartment of Biochemistry and Biophysics, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA 19104, USA.
Roberto DominguezDepartment of Physiology, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA 19104, USA. droberto@pennmedicine.upenn.edu.ORCID 0000-0003-3186-5229
University of Pennsylvania · US

Funding

Integrative mechanisms of organelle dynamics from the atomic-to-cellular levelRM1GM136511 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI DOMINGUEZ, ROBERTO, HOLZBAUR, ERIKA L · 2020 to 2024
$7.4M
Structural-Functional Basis of Actin Cytoskeleton DynamicsR01GM073791 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI DOMINGUEZ, ROBERTO · 2005 to 2025
$7.0M
STRUCTURAL BIOLOGY TRAINING PROGRAMT32GM008275 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI WAND, A. JOSHUA · 1988 to 2018
$6.0M
BAR PROTEINS LINKING MEMBRANE AND CYTOSKELETON DYNAMICSR01MH087950 · NIMH · UNIVERSITY OF PENNSYLVANIA · PI DOMINGUEZ, ROBERTO · 2010 to 2020
$4.0M
Functional and structural studies of the transition from transcription initiation to elongationR01GM123233 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI MURAKAMI, KENJI · 2017 to 2025
$3.6M
Computational Resource for Structural Biology and Molecular BiophysicsS10OD023592 · OD · UNIVERSITY OF PENNSYLVANIA · PI SHARP, KIM A · 2017 to 2017
$402k
Structure-function study of Arp2/3 complex and a novel role for actin branchingF31HL146077 · NHLBI · UNIVERSITY OF PENNSYLVANIA · PI ZIMMET, AUSTIN · 2019 to 2020
$76k
NHLBI NIH HHS F31 HL146077NIGMS NIH HHS R01 GM073791NIGMS NIH HHS R01 GM123233NIGMS NIH HHS RM1 GM136511NIGMS NIH HHS T32 GM008275NIH HHS S10 OD023592NIMH NIH HHS R01 MH087950
6 · The paper itself

Abstract

Actin-related protein (Arp) 2/3 complex nucleates branched actin networks that drive cell motility. It consists of seven proteins, including two actin-related subunits (Arp2 and Arp3). Two nucleation-promoting factors (NPFs) bind Arp2/3 complex during activation, but the order, specific interactions, and contribution of each NPF to activation are unresolved. Here, we report the cryo-electron microscopy structure of recombinantly expressed human Arp2/3 complex with two WASP family NPFs bound and address the mechanism of activation. A cross-linking assay that captures the transition of the Arps into the activated filament-like conformation shows that actin binding to NPFs favors this transition. Actin-NPF binding to Arp2 precedes binding to Arp3 and is sufficient to promote the filament-like conformation but not activation. Structure-guided mutagenesis of the NPF-binding sites reveals their distinct roles in activation and shows that, contrary to budding yeast Arp2/3 complex, NPF-mediated delivery of actin at the barbed end of both Arps is required for activation of human Arp2/3 complex.

Identifiers

PMID32917641
PMCPMC7274804
OpenAlexW3033932521

What OpenQuestion holds

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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.