Evidence map›Paper›PMID 21454476›Full record

ArticleThe Journal of biological chemistry2011

Mechanism of a concentration-dependent switch between activation and inhibition of Arp2/3 complex by coronin.

Su-Ling Liu, Karen M Needham, Jordan R May, Brad J Nolen

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.

0numbers the graph read from it
0cells of the map it votes in
55citing papers in PubMed
3.1field-weighted citation impact, top 9% 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

55 citing papers in PubMed, 78 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. The role of actin cytoskeleton component Arp2/3 in inflammatory response.Frontiers in cell and developmental biology · 2025
    Review
  9. Article
  10. Article
  11. Article
  12. Biochemical and mechanical regulation of actin dynamics.Nature reviews. Molecular cell biology · 2022
    Review
  13. Article
  14. Article
  15. Structure of Arp2/3 complex at a branched actin filament junction resolved by single-particle cryo-electron microscopy.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  16. Review
  17. Article
  18. Article
  19. Review
  20. Actin filament debranching regulates cell polarity during cell migration and asymmetric cell division.Proceedings of the National Academy of Sciences of the United States of America · 2021
    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

4 authors at 1 institution in 1 country.

Su-Ling LiuInstitute of Molecular Biology and Department of Chemistry, University of Oregon, Eugene, Oregon 97403-1229, USA.
Karen M Needham
Jordan R May
Brad J Nolen
University of Oregon · US

Funding

Mechanisms of regulation of Arp2/3 complexR01GM092917 · NIGMS · UNIVERSITY OF OREGON · PI NOLEN, BRADLEY J · 2010 to 2018
$2.9M
NIGMS NIH HHS R01 GM092917
6 · The paper itself

Abstract

Arp2/3 complex is a key actin filament nucleator that assembles branched actin networks in response to cellular signals. The activity of Arp2/3 complex is regulated by both activating and inhibitory proteins. Coronins make up a large class of actin-binding proteins previously shown to inhibit Arp2/3 complex. Although coronins are known to play a role in controlling actin dynamics in diverse processes, including endocytosis and cell motility, the precise mechanism by which they regulate Arp2/3 complex is unclear. We conducted a detailed biochemical analysis of budding yeast coronin, Crn1, and found that it not only inhibits Arp2/3 complex but also activates it. We mapped regions required for activation and found that Crn1 contains a sequence called CA, which is conserved in WASp/Scar proteins, the prototypical activators of Arp2/3 complex. Point mutations in CA abolished activation of Arp2/3 complex by Crn1 in vitro. Confocal microscopy and quantitative actin patch tracking showed that these mutants had defective endocytic actin patch dynamics in Saccharomyces cerevisiae, indicating that activation of Arp2/3 complex by coronin is required for normal actin dynamics in vivo. The switch between the dual modes of regulation by Crn1 is controlled by concentration, and low concentrations of Crn1 enhance filament binding by Arp2/3 complex, whereas high concentrations block binding. Our data support a direct tethering recruitment model for activation of Arp2/3 complex by Crn1 and suggest that Crn1 indirectly inhibits Arp2/3 complex by blocking it from binding actin filaments.

Indexed as

Actin-Related Protein 2Actin-Related Protein 3ActinsAmino Acid SequenceCytoskeletonDose-Response Relationship, DrugEndocytosisKineticsMicrofilament ProteinsMolecular ConformationMolecular Sequence DataProtein Structure, TertiarySaccharomyces cerevisiaeSequence Homology, Amino AcidActin-Related Protein 2Actin-Related Protein 3Actinscoronin proteinsMicrofilament Proteins

Identifiers

PMID21454476
PMCPMC3089548
OpenAlexW2063482892

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.