Evidence map›Paper›PMID 32839613›Full record

ArticleNature structural & molecular biology2020

Cryo-EM reveals the transition of Arp2/3 complex from inactive to nucleation-competent state.

Mohammed Shaaban, Saikat Chowdhury, Brad J Nolen

Open access · greenAbstract read
In one paragraph

Article in Nature structural & molecular biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
4.9field-weighted citation impact, top 4% 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

39 citing papers in PubMed, 62 citations in OpenAlex.

  1. Article
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  4. Arp2/3-mediated bidirectional actin assembly by SPIN90 dimers.Nature structural & molecular biology · 2025
    Article
  5. Article
  6. Akt-phosphorylated UFL1 UFMylates ArpC4 to promote metastasis.Nature structural & molecular biology · 2025
    Article
  7. 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
  8. Article
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  12. Review
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  18. Review
  19. Membrane-dependent actin polymerization mediated by thebioRxiv : the preprint server for biology · 2023
    Article
  20. Article
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

3 authors at 2 institutions in 1 country.

Mohammed ShaabanDepartment of Biochemistry and Cell Biology, Stony Brook University, Stony Brook, NY, USA.ORCID http://orcid.org/0000-0002-4503-0356
Saikat ChowdhuryDepartment of Biochemistry and Cell Biology, Stony Brook University, Stony Brook, NY, USA. saikat.chowdhury@stonybrook.edu.ORCID http://orcid.org/0000-0001-8043-5028
Brad J NolenInstitute of Molecular Biology and Department of Chemistry and Biochemistry, University of Oregon, Eugene, OR, USA. bnolen@uoregon.edu.ORCID http://orcid.org/0000-0002-0224-9980
Stony Brook University · USOregon Research Institute · 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
Mechanisms of regulation of Arp2/3 complexR01GM092917 · NIGMS · UNIVERSITY OF OREGON · PI NOLEN, BRADLEY J · 2010 to 2018
$2.9M
A 200KV CRYO-TEM FOR IMAGING BIOLOGICAL STRUCTURESS10OD012272 · OD · STATE UNIVERSITY NEW YORK STONY BROOK · PI NEIMAN, AARON M · 2015 to 2015
$2.0M
Molecular mechanism of regulated branching nucleation by Arp2/3 complex and WASP proteins - admin supplementR01GM127440 · NIGMS · UNIVERSITY OF OREGON · PI NOLEN, BRADLEY J · 2018 to 2019
$784k
NIGMS NIH HHS R01 GM092917NIGMS NIH HHS R01 GM127440NIGMS NIH HHS R35 GM136319NIH HHS S10 OD012272
6 · The paper itself

Abstract

Arp2/3 complex, a crucial actin filament nucleator, undergoes structural rearrangements during activation by nucleation-promoting factors (NPFs). However, the conformational pathway leading to the nucleation-competent state is unclear due to lack of high-resolution structures of the activated state. Here we report a ~3.9 Å resolution cryo-EM structure of activated Schizosaccharomyces pombe Arp2/3 complex bound to the S. pombe NPF Dip1 and attached to the end of the nucleated actin filament. The structure reveals global and local conformational changes that allow the two actin-related proteins in Arp2/3 complex to mimic a filamentous actin dimer and template nucleation. Activation occurs through a clamp-twisting mechanism, in which Dip1 forces two core subunits in Arp2/3 complex to pivot around one another, shifting half of the complex into a new activated position. By showing how Dip1 stimulates activation, the structure reveals how NPFs can activate Arp2/3 complex in diverse cellular processes.

Indexed as

Actin CytoskeletonActin-Related Protein 2-3 ComplexCryoelectron MicroscopyModels, MolecularProtein BindingProtein ConformationProtein MultimerizationSchizosaccharomycesSchizosaccharomyces pombe ProteinsActin-Related Protein 2-3 ComplexDip1 protein, S pombeSchizosaccharomyces pombe Proteins

Identifiers

PMID32839613
PMCPMC8717925
OpenAlexW3080782312

What Socratic holds

Textmetadata
LicenceTDM
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 Socratic graph.