Evidence map›Paper›PMID 35622886›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2022

Structure of Arp2/3 complex at a branched actin filament junction resolved by single-particle cryo-electron microscopy.

Bojian Ding, Heidy Y Narvaez-Ortiz, Yuvraj Singh, Glen M Hocky, Saikat Chowdhury, Brad J Nolen

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2022. 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
13.0field-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

44 citing papers in PubMed, 65 citations in OpenAlex.

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  8. The Rho GTPase signaling pathway modulatesFrontiers in immunology · 2026
    Article
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  11. Arp2/3-mediated bidirectional actin assembly by SPIN90 dimers.Nature structural & molecular biology · 2025
    Article
  12. Article
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  17. 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
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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 4 institutions in 2 countries.

Bojian DingDepartment of Biochemistry and Cell Biology, Stony Brook University, Stony Brook, NY 11794.ORCID 0000-0002-6648-3477
Heidy Y Narvaez-OrtizDepartment of Chemistry and Biochemistry and Institute of Molecular Biology, University of Oregon, Eugene, OR 97403.ORCID 0000-0002-6434-6292
Yuvraj SinghDepartment of Chemistry, New York University, New York, NY 10012.ORCID 0000-0003-3022-6871
Glen M HockyDepartment of Chemistry, New York University, New York, NY 10012.ORCID 0000-0002-5637-0698
Saikat ChowdhuryDepartment of Biochemistry and Cell Biology, Stony Brook University, Stony Brook, NY 11794.ORCID 0000-0001-8043-5028
Brad J NolenDepartment of Chemistry and Biochemistry and Institute of Molecular Biology, University of Oregon, Eugene, OR 97403.ORCID 0000-0002-0224-9980
New York University · USUniversity of Oregon · USCentre for Cellular and Molecular Biology · INStony Brook University · US

Funding

Control of actin filament networks by Arp2/3 complex and its regulatorsR35GM136319 · NIGMS · UNIVERSITY OF OREGON · PI Bradley J Nolen · 2020 to 2026
$4.4M
Harnessing simulations to uncover molecular mechanisms of mechanosensingR35GM138312 · NIGMS · NEW YORK UNIVERSITY · PI Glen Hocky · 2020 to 2026
$3.0M
A 200KV CRYO-TEM FOR IMAGING BIOLOGICAL STRUCTURESS10OD012272 · OD · STATE UNIVERSITY NEW YORK STONY BROOK · PI NEIMAN, AARON M · 2015 to 2015
$2.0M
HHS | NIH | National Institute of General Medical Sciences (NIGMS) R35-GM136319NIGMS NIH HHS R35 GM136319NIGMS NIH HHS R35 GM138312NIH HHS S10 OD012272
6 · The paper itself

Abstract

Arp2/3 complex nucleates branched actin filaments that provide pushing forces to drive cellular processes such as lamellipodial protrusion and endocytosis. Arp2/3 complex is intrinsically inactive, and multiple classes of nucleation promoting factors (NPFs) stimulate its nucleation activity. When activated by WASP family NPFs, the complex must bind to the side of a preexisting (mother) filament of actin to complete the nucleation process, ensuring that WASP-mediated activation creates branched rather than linear actin filaments. How actin filaments contribute to activation is currently not understood, largely due to the lack of high-resolution structures of activated Arp2/3 complex bound to the side of a filament. Here, we present the 3.9-Å cryo-electron microscopy structure of the Arp2/3 complex at a branch junction. The structure reveals contacts between Arp2/3 complex and the side of the mother actin filament that likely stimulate subunit flattening, a conformational change that allows the actin-related protein subunits in the complex (Arp2 and Arp3) to mimic filamentous actin subunits. In contrast, limited contact between the bottom half of the complex and the mother filament suggests that clamp twisting, a second major conformational change observed in the active state, is not stimulated by actin filaments, potentially explaining why actin filaments are required but insufficient to trigger nucleation during WASP-mediated activation. Along with biochemical and live-cell imaging data and molecular dynamics simulations, the structure reveals features critical for the interaction of Arp2/3 complex with actin filaments and regulated assembly of branched actin filament networks in cells.

Indexed as

Actin CytoskeletonActin-Related Protein 2-3 ComplexCryoelectron MicroscopyCytoskeletonMolecular Dynamics SimulationProtein ConformationWiskott-Aldrich Syndrome ProteinActin-Related Protein 2-3 ComplexWiskott-Aldrich Syndrome ProteinactinArp2/3cryo-electron microscopycytoskeletonnucleation

Identifiers

PMID35622886
PMCPMC9295785
OpenAlexW4281725683

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.