Evidence map›Paper›PMID 25207437›Full record

ReviewNature reviews. Molecular cell biology2014

Capping protein regulators fine-tune actin assembly dynamics.

Marc Edwards, Adam Zwolak, Dorothy A Schafer, David Sept, Roberto Dominguez, John A Cooper

Erratum issuedOpen access · greenAbstract readReview
In one paragraph

Review in Nature reviews. Molecular cell biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 198 papers.

0numbers the graph read from it
0cells of the map it votes in
198citing papers in PubMed
10.8field-weighted citation impact, top 1% 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

198 citing papers in PubMed, 298 citations in OpenAlex.

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  10. Building the bridges: molecular mechanisms of tunneling nanotube formation.Cellular and molecular life sciences : CMLS · 2026
    Review
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138 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

6 authors at 3 institutions in 1 country.

Marc EdwardsDepartment of Cell Biology and Physiology, Washington University, St. Louis, Missouri 63110, USA.
Adam ZwolakDepartment of Physiology, Perelman School of Medicine, University of Pennsylvania, Philadelphia, Pennsylvania 19104, USA.
Dorothy A SchaferDepartments of Biology and Cell Biology, University of Virginia, Charlottesville, Virginia 22904, USA.
David SeptDepartment of Biomedical Engineering and Center for Computational Medicine and Bioinformatics, University of Michigan, Ann Arbor, Michigan 48109, USA.
Roberto DominguezDepartment of Physiology, Perelman School of Medicine, University of Pennsylvania, Philadelphia, Pennsylvania 19104, USA.
John A CooperDepartment of Cell Biology and Physiology, Washington University, St. Louis, Missouri 63110, USA.
University of Pennsylvania · USWashington University in St. Louis · USUniversity of Michigan–Ann Arbor · US

Funding

Molecular Mechanisms in Actin Assembly &Cell MotilityR01GM038542 · NIGMS · WASHINGTON UNIVERSITY · PI COOPER, JOHN A · 1989 to 2013
$7.4M
Structural-Functional Basis of Actin Cytoskeleton DynamicsR01GM073791 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI DOMINGUEZ, ROBERTO · 2005 to 2025
$7.0M
BAR PROTEINS LINKING MEMBRANE AND CYTOSKELETON DYNAMICSR01MH087950 · NIMH · UNIVERSITY OF PENNSYLVANIA · PI DOMINGUEZ, ROBERTO · 2010 to 2020
$4.0M
REGULATION OF ACTIN CAPPING PROTEINR01GM095509 · NIGMS · WASHINGTON UNIVERSITY · PI COOPER, JOHN A · 2012 to 2015
$1.1M
NIDA NIH HHS 5T90DA02287104NIGMS NIH HHS GM038542NIGMS NIH HHS GM073791NIGMS NIH HHS GM095509NIGMS NIH HHS R01 GM038542NIGMS NIH HHS R01 GM073791NIGMS NIH HHS R01 GM095509NIMH NIH HHS MH087950NIMH NIH HHS R01 MH087950
6 · The paper itself

Abstract

Capping protein (CP) binds the fast growing barbed end of the actin filament and regulates actin assembly by blocking the addition and loss of actin subunits. Recent studies provide new insights into how CP and barbed-end capping are regulated. Filament elongation factors, such as formins and ENA/VASP (enabled/vasodilator-stimulated phosphoprotein), indirectly regulate CP by competing with CP for binding to the barbed end, whereas other molecules, including V-1 and phospholipids, directly bind to CP and sterically block its interaction with the filament. In addition, a diverse and unrelated group of proteins interact with CP through a conserved 'capping protein interaction' (CPI) motif. These proteins, including CARMIL (capping protein, ARP2/3 and myosin I linker), CD2AP (CD2-associated protein) and the WASH (WASP and SCAR homologue) complex subunit FAM21, recruit CP to specific subcellular locations and modulate its actin-capping activity via allosteric effects.

Indexed as

Actin Capping ProteinsActin CytoskeletonAdaptor Proteins, Signal TransducingAmino Acid SequenceCarrier ProteinsCytoskeletal ProteinsDNA-Binding ProteinsHumansMicrofilament ProteinsModels, MolecularPhosphatidylinositol PhosphatesProtein BindingProtein ConformationActin Capping ProteinsAdaptor Proteins, Signal TransducingCARMIL1 protein, humanCarrier ProteinsCD2-associated proteinCytoskeletal ProteinsDNA-Binding ProteinsENA-VASP proteinsMicrofilament ProteinsPhosphatidylinositol PhosphatesWASH protein, human

Identifiers

PMID25207437
PMCPMC4271544
OpenAlexW2021636759

What OpenQuestion 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 OpenQuestion graph.