Evidence map›Paper›PMID 17499050›Full record

ArticleMolecular cell2007

Insights into the influence of nucleotides on actin family proteins from seven structures of Arp2/3 complex.

Brad J Nolen, Thomas D Pollard

Open access · bronzeAbstract read
In one paragraph

Article in Molecular cell, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
3.7field-weighted citation impact, top 7% 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

49 citing papers in PubMed, 74 citations in OpenAlex.

  1. Article
  2. Article
  3. 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
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  8. Review
  9. Mechanism of actin polymerization revealed by cryo-EM structures of actin filaments with three different bound nucleotides.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  10. Article
  11. Conformational changes in Arp2/3 complex induced by ATP, WASp-VCA, and actin filaments.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  12. Article
  13. Identification of Wiskott-Aldrich syndrome protein (WASP) binding sites on the branched actin filament nucleator Arp2/3 complex.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  14. Article
  15. Role and structural mechanism of WASP-triggered conformational changes in branched actin filament nucleation by Arp2/3 complex.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  16. Mechanisms of leiomodin 2-mediated regulation of actin filament in muscle cells.Proceedings of the National Academy of Sciences of the United States of America · 2015
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  17. Article
  18. Review
  19. 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

2 authors at 1 institution in 1 country.

Brad J NolenDepartment of Molecular, Cellular and Developmental Biology, Yale University, New Haven, CT 06520-8103, USA.
Thomas D Pollard
Yale University · US

Funding

Structure and function of Arp 2/3 complex--Subproject 4P01GM066311 · NIGMS · YALE UNIVERSITY · PI POLLARD, THOMAS D. · 2003 to 2013
$16.8M
Structural investigation of Arp2/3 complex activationF32GM074374 · NIGMS · YALE UNIVERSITY · PI NOLEN, BRADLEY J. · 2005 to 2006
$93k
NIGMS NIH HHS F32 GM074374NIGMS NIH HHS F32GM074374NIGMS NIH HHS P01 GM066311NIGMS NIH HHS P01GM066311
6 · The paper itself

Abstract

ATP is required for nucleation of actin filament branches by Arp2/3 complex, but the influence of ATP binding and hydrolysis are poorly understood. We determined crystal structures of bovine Arp2/3 complex cocrystallized with various bound adenine nucleotides and cations. Nucleotide binding favors closure of the nucleotide-binding cleft of Arp3, but no large-scale conformational changes in the complex. Thus, ATP binding does not directly activate Arp2/3 complex but is part of a network of interactions that contribute to nucleation. We compared nucleotide-induced conformational changes of residues lining the cleft in Arp3 and actin structures to construct a movie depicting the proposed ATPase cycle for the actin family. Chemical crosslinking stabilized subdomain 1 of Arp2, revealing new electron density for 69 residues in this subdomain. Steric clashes with Arp3 appear to be responsible for intrinsic disorder of subdomains 1 and 2 of Arp2 in inactive Arp2/3 complex.

Indexed as

Protein Interaction MappingActin CytoskeletonActin-Related Protein 2-3 ComplexActinsAdenosine DiphosphateAdenosine TriphosphatasesAdenosine TriphosphateAnimalsBinding SitesCattleCross-Linking ReagentsGlutaralHumansKineticsMacromolecular SubstancesModels, MolecularActin-Related Protein 2-3 ComplexActinsAdenosine DiphosphateAdenosine TriphosphatasesAdenosine TriphosphateCross-Linking ReagentsGlutaralMacromolecular SubstancesNucleotides

Identifiers

PMID17499050
PMCPMC1997283
OpenAlexW2088468251

What OpenQuestion holds

Textmetadata
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.