Evidence map›Paper›PMID 26412145›Full record

ArticleNature communications2015

CPI motif interaction is necessary for capping protein function in cells.

Marc Edwards, Patrick McConnell, Dorothy A Schafer, John A Cooper

Abstract read
In one paragraph

Article in Nature communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing 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

28 citing papers in PubMed.

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  9. Membrane-dependent actin polymerization mediated by thebioRxiv : the preprint server for biology · 2023
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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

4 authors.

Marc EdwardsDepartment of Cell Biology and Physiology, Washington University School of Medicine, St Louis, Missouri 63110-1093, USA.
Patrick McConnellDepartment of Cell Biology and Physiology, Washington University School of Medicine, St Louis, Missouri 63110-1093, USA.
Dorothy A SchaferDepartments of Biology and Cell Biology, University of Virginia, Charlottesville, Virginia 22904-4328, USA.
John A CooperDepartment of Cell Biology and Physiology, Washington University School of Medicine, St Louis, Missouri 63110-1093, USA.

Funding

REGULATION OF ACTIN CAPPING PROTEINR01GM095509 · NIGMS · WASHINGTON UNIVERSITY · PI COOPER, JOHN A · 2012 to 2015
$1.1M
NIDA NIH HHS 5T90DA02287104NIGMS NIH HHS GM95509NIGMS NIH HHS R01 GM095509
6 · The paper itself

Abstract

Capping protein (CP) has critical roles in actin assembly in vivo and in vitro. CP binds with high affinity to the barbed end of actin filaments, blocking the addition and loss of actin subunits. Heretofore, models for actin assembly in cells generally assumed that CP is constitutively active, diffusing freely to find and cap barbed ends. However, CP can be regulated by binding of the 'capping protein interaction' (CPI) motif, found in a diverse and otherwise unrelated set of proteins that decreases, but does not abolish, the actin-capping activity of CP and promotes uncapping in biochemical experiments. Here, we report that CP localization and the ability of CP to function in cells requires interaction with a CPI-motif-containing protein. Our discovery shows that cells target and/or modulate the capping activity of CP via CPI motif interactions in order for CP to localize and function in cells.

Indexed as

Actin Capping ProteinsActinsAmino Acid MotifsAnimalsCell Line, TumorEscherichia coliHEK293 CellsHumansMiceMutationRNA InterferenceActin Capping ProteinsActins

Identifiers

PMID26412145
PMCPMC4598739

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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.