Evidence map›Paper›PMID 23904264›Full record

ArticleMolecular biology of the cell2013

Physiological role of the interaction between CARMIL1 and capping protein.

Marc Edwards, Yun Liang, Taekyung Kim, John A Cooper

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
1.5field-weighted citation impact, top 20% 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

26 citing papers in PubMed, 38 citations in OpenAlex.

  1. Article
  2. Review
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  4. Article
  5. Mechanisms of actin disassembly and turnover.The Journal of cell biology · 2023
    Review
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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 at 1 institution in 2 countries.

Marc EdwardsDepartment of Cell Biology and Physiology, Washington University in St. Louis, St. Louis, MO 63110.
Yun Liang
Taekyung Kim
John A Cooper
Washington University in St. Louis · US

Funding

Molecular Mechanisms in Actin Assembly &Cell MotilityR01GM038542 · NIGMS · WASHINGTON UNIVERSITY · PI COOPER, JOHN A · 1989 to 2013
$7.4M
REGULATION OF ACTIN CAPPING PROTEINR01GM095509 · NIGMS · WASHINGTON UNIVERSITY · PI COOPER, JOHN A · 2012 to 2015
$1.1M
NIDA NIH HHS 5T90DA02287104NIGMS NIH HHS GM 38542NIGMS NIH HHS GM 95509NIGMS NIH HHS R01 GM038542NIGMS NIH HHS R01 GM095509
6 · The paper itself

Abstract

The regulation of free barbed ends is central to the control of dynamic actin assembly and actin-based motility in cells. Capping protein (CP) is known to regulate barbed ends and control actin assembly in cells. The CARMIL family of proteins can bind and inhibit CP in vitro, but the physiological significance of the interaction of CARMIL with CP in cells is poorly understood. Mammalian cells lacking CARMIL1 have defects in lamellipodia, macropinocytosis, cell migration, and Rac1 activation. Here we investigate the physiological significance of the CARMIL1-CP interaction, using a point mutant with a well-defined biochemical defect. We find that the CARMIL1-CP interaction is essential for the assembly of lamellipodia, the formation of ruffles, and the process of macropinocytosis. In contrast, the interaction of CARMIL1 with CP shows little to no importance for other functions of CARMIL1, including localization of CARMIL1 to the membrane, activation of Rac1, and cell migration. One implication is that lamellipodia are only marginally important for cell migration in a wound-healing model. The results also suggest that the ability of CARMIL1 to inhibit CP in cells may be regulated.

Indexed as

Actin Capping ProteinsAmino Acid MotifsBinding SitesCarrier ProteinsCell MovementHumansMicrofilament ProteinsPinocytosisPoint MutationProtein BindingPseudopodiarac1 GTP-Binding ProteinActin Capping ProteinsCARMIL1 protein, humanCarrier ProteinsMicrofilament Proteinsrac1 GTP-Binding ProteinRAC1 protein, human

Identifiers

PMID23904264
PMCPMC3784379
OpenAlexW2099118892

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.