Evidence map›Paper›PMID 18381280›Full record

ArticleThe Journal of biological chemistry2008

Functional surfaces on the p35/ARPC2 subunit of Arp2/3 complex required for cell growth, actin nucleation, and endocytosis.

Karen M Daugherty, Bruce L Goode

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.0field-weighted citation impact, top 25% 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

20 citing papers in PubMed, 30 citations in OpenAlex.

  1. Article
  2. The Actin Cytoskeleton Mediates Transmission of "Applied and environmental microbiology · 2021
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Role of ARPC2 in Human Gastric Cancer.Mediators of inflammation · 2017
    Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Purification of native Arp2/3 complex from bovine thymus.Methods in molecular biology (Clifton, N.J.) · 2013
    Article
  15. Article
  16. Article
  17. New mechanisms and functions of actin nucleation.Current opinion in cell biology · 2011
    Review
  18. An actin-filament-binding interface on the Arp2/3 complex is critical for nucleation and branch stability.Proceedings of the National Academy of Sciences of the United States of America · 2010
    Article
  19. 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

2 authors at 1 institution in 1 country.

Karen M DaughertyDepartment of Biochemistry, Brandeis University and the Rosenstiel Basic Medical Sciences Center, Waltham, Massachusetts 02454, USA.
Bruce L Goode
Brandeis University · US

Funding

MECHNISMS REGULATING ACTIN ASSEMBLYR01GM063691 · NIGMS · BRANDEIS UNIVERSITY · PI GOODE, BRUCE L · 2002 to 2019
$7.5M
Macromolecular Structure MechanismT32GM007596 · NIGMS · BRANDEIS UNIVERSITY · PI OPRIAN, DANIEL D · 1985 to 2019
$4.5M
NIGMS NIH HHS GM63691NIGMS NIH HHS R01 GM063691NIGMS NIH HHS T32 GM007596
6 · The paper itself

Abstract

The Arp2/3 complex is comprised of seven evolutionarily conserved subunits and upon activation by WASp or another nucleation promoting factor nucleates the formation of actin filaments. These events are critical for driving a wide range of cellular processes, including motility, endocytosis, and intracellular trafficking. However, an in depth understanding of the Arp2/3 complex activation and nucleation mechanism is still lacking. Here, we used a mutagenesis approach in Saccharomyces cerevisiae to dissect the structural and functional roles of the p35/ARPC2 subunit. Using integrated alleles that target conserved and solvent-exposed residues, we identified surfaces on p35/ARPC2 required for cell growth, actin organization, and endocytosis. In parallel, we purified the mutant Arp2/3 complexes and compared their actin assembly activities both in the presence and in the absence of WASp. The majority of alleles with defects mapped to one face of p35/ARPC2, where there was a close correlation between loss of actin nucleation and endocytosis. A second site required for nucleation and endocytosis was identified near the contact surface between p35/ARPC2 and p19/ARPC4. A third site was identified at a more distal conserved surface, which was critical for endocytosis but not nucleation. These findings pinpoint the key surfaces on p35/ARPC2 required for Arp2/3 complex-mediated actin assembly and cellular function and provide a higher resolution view of Arp2/3 structure and mechanism.

Indexed as

EndocytosisActin-Related Protein 2-3 ComplexActinsAllelesAmino Acid SequenceBinding SitesCell ProliferationDose-Response Relationship, DrugModels, BiologicalMolecular ConformationMolecular Sequence DataMutagenesisPhenotypePlasmidsSaccharomyces cerevisiaeActin-Related Protein 2-3 ComplexActins

Identifiers

PMID18381280
PMCPMC2423265
OpenAlexW2066505352

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.