Evidence map›Paper›PMID 22711700›Full record

ArticleThe Journal of cell biology2012

Arp2/3 complex-dependent actin networks constrain myosin II function in driving retrograde actin flow.

Qing Yang, Xiao-Feng Zhang, Thomas D Pollard, Paul Forscher

Abstract read
In one paragraph

Article in The Journal of cell biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 95 papers.

0numbers the graph read from it
0cells of the map it votes in
95citing papers in PubMed
–field-weighted citation impact
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

95 citing papers in PubMed.

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  16. Friction patterns guide actin network contraction.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  17. Article
  18. Review
  19. Article
  20. Article

35 more citing papers are in PubMed but not listed here.

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.

Qing YangDepartment of Molecular, Cellular, and Developmental Biology, Yale University, New Haven, CT 06511, USA.
Xiao-Feng Zhang
Thomas D Pollard
Paul Forscher

Funding

MEDICAL SCIENTIST TRAINING PROGRAMT32GM007205 · NIGMS · YALE UNIVERSITY · PI KAZMIERCZAK, BARBARA I · 1985 to 2019
$42.9M
MOLECULAR MECHANISMS OF CELLULAR MOTILITYR01GM026338 · NIGMS · YALE UNIVERSITY · PI POLLARD, THOMAS D. · 1985 to 2020
$9.8M
Regulation of Neuronal Motility: the role of actin filament turnoverR01NS028695 · NINDS · YALE UNIVERSITY · PI FORSCHER, PAUL · 1990 to 2024
$7.8M
Ca and Rho GTPase Control of the Neuronal CytoskeletonR01NS051786 · NINDS · YALE UNIVERSITY · PI FORSCHER, PAUL · 2006 to 2009
$1.4M
NIGMS NIH HHS GM-026338NIGMS NIH HHS R01 GM026338NIGMS NIH HHS T32 GM007205NIGMS NIH HHS TG-T32GM07205NINDS NIH HHS R01 NS028695NINDS NIH HHS R01 NS051786NINDS NIH HHS R01-NS051786NINDS NIH HHS R01-NS28695
6 · The paper itself

Abstract

The Arp2/3 complex nucleates actin filaments to generate networks at the leading edge of motile cells. Nonmuscle myosin II produces contractile forces involved in driving actin network translocation. We inhibited the Arp2/3 complex and/or myosin II with small molecules to investigate their respective functions in neuronal growth cone actin dynamics. Inhibition of the Arp2/3 complex with CK666 reduced barbed end actin assembly site density at the leading edge, disrupted actin veils, and resulted in veil retraction. Strikingly, retrograde actin flow rates increased with Arp2/3 complex inhibition; however, when myosin II activity was blocked, Arp2/3 complex inhibition now resulted in slowing of retrograde actin flow and veils no longer retracted. Retrograde flow rate increases induced by Arp2/3 complex inhibition were independent of Rho kinase activity. These results provide evidence that, although the Arp2/3 complex and myosin II are spatially segregated, actin networks assembled by the Arp2/3 complex can restrict myosin II-dependent contractility with consequent effects on growth cone motility.

Indexed as

Actin-Related Protein 2-3 ComplexActinsAnimalsAplysiaGrowth ConesMicroscopy, ElectronMyosin Type IIActin-Related Protein 2-3 ComplexActinsMyosin Type II

Identifiers

PMID22711700
PMCPMC3384413

What OpenQuestion holds

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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.