Evidence map›Paper›PMID 26466680›Full record

ArticleMolecular biology of the cell2015

CARMIL2 is a novel molecular connection between vimentin and actin essential for cell migration and invadopodia formation.

M Hunter Lanier, Taekyung Kim, John A Cooper

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
2.8field-weighted citation impact, top 10% 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

35 citing papers in PubMed, 55 citations in OpenAlex.

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  14. Impact of Vimentin on Regulation of Cell Signaling and Matrix Remodeling.Frontiers in cell and developmental biology · 2022
    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

3 authors at 1 institution in 1 country.

M Hunter LanierDepartment of Cell Biology and Physiology, Washington University in St. Louis, St. Louis, MO 63110.
Taekyung KimDepartment of Cell Biology and Physiology, Washington University in St. Louis, St. Louis, MO 63110.
John A CooperDepartment of Cell Biology and Physiology, Washington University in St. Louis, St. Louis, MO 63110 jacooper@wustl.edu.
Washington University in St. Louis · US

Funding

REGULATION OF ACTIN CAPPING PROTEINR01GM095509 · NIGMS · WASHINGTON UNIVERSITY · PI COOPER, JOHN A · 2012 to 2015
$1.1M
The Role of CARMIL2 in Cell Migration and InvasionF30CA171595 · NCI · WASHINGTON UNIVERSITY · PI LANIER, MICHAEL HUNTER · 2012 to 2014
$105k
NCI NIH HHS F30 CA171595NCI NIH HHS F30CA171595NIGMS NIH HHS GM95509NIGMS NIH HHS R01 GM095509
6 · The paper itself

Abstract

Cancer cell migration requires the regulation of actin networks at protrusions associated with invadopodia and other leading edges. Carcinomas become invasive after undergoing an epithelial-mesenchymal transition characterized by the appearance of vimentin filaments. While vimentin expression correlates with cell migration, the molecular connections between vimentin- and actin-based membrane protrusions are not understood. We report here that CARMIL2 (capping protein, Arp2/3, myosin-I linker 2) provides such a molecular link. CARMIL2 localizes to vimentin, regulates actin capping protein (CP), and binds to membranes. CARMIL2 is necessary for invadopodia formation, as well as cell polarity, lamellipodial assembly, membrane ruffling, macropinocytosis, and collective cell migration. Using point mutants and chimeras with defined biochemical and cellular properties, we discovered that localization to vimentin and CP binding are both essential for the function of CARMIL2 in cells. On the basis of these results, we propose a model in which dynamic vimentin filaments target CARMIL2 to critical membrane-associated locations, where CARMIL2 regulates CP, and thus actin assembly, to create cell protrusions.

Indexed as

Actin Capping ProteinsActinsCell Line, TumorCell MembraneCell MovementCell Surface ExtensionsEpithelial-Mesenchymal TransitionHumansIntermediate FilamentsMicrofilament ProteinsNeoplasmsPodosomesVimentinActin Capping ProteinsActinsCARMIL1 protein, humanMicrofilament ProteinsVimentin

Identifiers

PMID26466680
PMCPMC4678016
OpenAlexW2262828252

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.