Evidence map›Paper›PMID 20969875›Full record

ArticleJournal of molecular biology2010

The interaction of capping protein with the barbed end of the actin filament.

Taekyung Kim, John A Cooper, David Sept

Abstract read
In one paragraph

Article in Journal of molecular biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing 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

37 citing papers in PubMed.

  1. Article
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  6. Cytoskeletal association of ATP citrate lyase controls the mechanodynamics of macropinocytosis.Proceedings of the National Academy of Sciences of the United States of America · 2023
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  9. Review
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  13. Crystal structure of human V-1 in the apo form.Acta crystallographica. Section F, Structural biology communications · 2021
    Article
  14. Article
  15. 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

3 authors.

Taekyung KimDepartment of Cell Biology and Physiology, Washington University School of Medicine, St. Louis, MO 63110, USA.
John A Cooper
David Sept

Funding

Molecular Mechanisms in Actin Assembly &Cell MotilityR01GM038542 · NIGMS · WASHINGTON UNIVERSITY · PI COOPER, JOHN A · 1989 to 2013
$7.4M
Protein interactions underlying actin-based motilityR01GM067246 · NIGMS · WASHINGTON UNIVERSITY · PI SEPT, DAVID S. · 2002 to 2006
$1.3M
NIGMS NIH HHS GM38542NIGMS NIH HHS GM67246NIGMS NIH HHS R01 GM038542NIGMS NIH HHS R01 GM067246
6 · The paper itself

Abstract

The interaction of capping protein (CP) with actin filaments is an essential element of actin assembly and actin-based motility in nearly all eukaryotes. The dendritic nucleation model for Arp2/3-based lamellipodial assembly features capping of barbed ends by CP, and the formation of filopodia is proposed to involve inhibition of capping by formins and other proteins. To understand the molecular basis for how CP binds the barbed end of the actin filament, we have used a combination of computational and experimental approaches, primarily involving molecular docking and site-directed mutagenesis. We arrive at a model that supports all of our biochemical data and agrees very well with a cryo-electron microscopy structure of the capped filament. CP interacts with both actin protomers at the barbed end of the filament, and the amphipathic helix at the C-terminus of the β-subunit binds to the hydrophobic cleft on actin, in a manner similar to that of WH2 domains. These studies provide us with new molecular insight into how CP binds to the actin filament.

Indexed as

Protein Interaction MappingActin Capping ProteinsActin CytoskeletonAnimalsKineticsMiceModels, MolecularMolecular Dynamics SimulationMutagenesis, Site-DirectedProtein BindingActin Capping Proteins

Identifiers

PMID20969875
PMCPMC2991585

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Registered trials

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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.