Evidence map›Paper›PMID 11018051›Full record

ArticleThe Journal of cell biology2000

Cortactin localization to sites of actin assembly in lamellipodia requires interactions with F-actin and the Arp2/3 complex.

S A Weed, A V Karginov, D A Schafer, A M Weaver, A W Kinley, J A Cooper, J T Parsons

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 190 papers.

0numbers the graph read from it
0cells of the map it votes in
190citing papers in PubMed
7.9field-weighted citation impact, top 2% 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

190 citing papers in PubMed, 411 citations in OpenAlex.

  1. Article
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  15. TheFrontiers in synaptic neuroscience · 2024
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130 more citing papers are in PubMed but not listed here.

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

7 authors at 2 institutions in 1 country.

S A WeedDepartment of Microbiology and Cancer Center, University of Virginia Health Sciences Center, Charlottesville, Virginia 22908, USA.
A V Karginov
D A Schafer
A M Weaver
A W Kinley
J A Cooper
J T Parsons
University of Virginia · USWashington University in St. Louis · US

Funding

STRUCTURE AND FUNCTION OF A CELLULAR TYROSINE PROTEIN KINASEP01CA040042 · NCI · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI MACARA, IAN G · 1985 to 2009
$10.5M
Molecular Mechanisms in Actin Assembly &Cell MotilityR01GM038542 · NIGMS · WASHINGTON UNIVERSITY · PI COOPER, JOHN A · 1989 to 2013
$7.4M
Function of Cortactin, a Src TargetR01CA029243 · NCI · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI PARSONS, J THOMAS · 1985 to 2005
$1.5M
DETERMINING THE ROLE OF CORTACTIN IN SIGNAL TRANSDUCTIONF32CA075695 · NCI · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI WEED, SCOTT A · 1997 to 1999
–
AVIAN TUMOR VIRUS ANTIGENSR37CA029243 · NCI · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI PARSONS, J THOMAS · 1992 to 1999
–
NCI NIH HHS CA29243NCI NIH HHS CA40042NCI NIH HHS F32 CA075695NCI NIH HHS P01 CA040042NCI NIH HHS R01 CA029243NCI NIH HHS R37 CA029243NIGMS NIH HHS GM38542NIGMS NIH HHS R01 GM038542
6 · The paper itself

Abstract

Cortactin is an actin-binding protein that is enriched within the lamellipodia of motile cells and in neuronal growth cones. Here, we report that cortactin is localized with the actin-related protein (Arp) 2/3 complex at sites of actin polymerization within the lamellipodia. Two distinct sequence motifs of cortactin contribute to its interaction with the cortical actin network: the fourth of six tandem repeats and the amino-terminal acidic region (NTA). Cortactin variants lacking either the fourth tandem repeat or the NTA failed to localize at the cell periphery. Tandem repeat four was necessary for cortactin to stably bind F-actin in vitro. The NTA region interacts directly with the Arp2/3 complex based on affinity chromatography, immunoprecipitation assays, and binding assays using purified components. Cortactin variants containing the NTA region were inefficient at promoting Arp2/3 actin nucleation activity. These data provide strong evidence that cortactin is specifically localized to sites of dynamic cortical actin assembly via simultaneous interaction with F-actin and the Arp2/3 complex. Cortactin interacts via its Src homology 3 (SH3) domain with ZO-1 and the SHANK family of postsynaptic density 95/dlg/ZO-1 homology (PDZ) domain-containing proteins, suggesting that cortactin contributes to the spatial organization of sites of actin polymerization coupled to selected cell surface transmembrane receptor complexes.

Indexed as

Cytoskeletal ProteinsPseudopodiaActin-Related Protein 2Actin-Related Protein 3ActinsAmino Acid SequenceAnimalsBinding SitesBiological TransportCells, CulturedCortactinMiceMicrofilament ProteinsMolecular Sequence DataProtein BindingProtein Structure, TertiaryActin-Related Protein 2Actin-Related Protein 3ActinsActr2 protein, mouseActr3 protein, mouseCortactinCttn protein, mouseCytoskeletal ProteinsMicrofilament Proteinsrac GTP-Binding Proteins

Identifiers

PMID11018051
PMCPMC2189811
OpenAlexW2010781630

What OpenQuestion holds

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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.