Evidence map›Paper›PMID 9312002›Full record

ArticleThe EMBO journal1997

A novel proline-rich motif present in ActA of Listeria monocytogenes and cytoskeletal proteins is the ligand for the EVH1 domain, a protein module present in the Ena/VASP family.

K Niebuhr, F Ebel, R Frank, M Reinhard, E Domann, U D Carl, U Walter, F B Gertler, J Wehland, T Chakraborty

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 129 papers.

0numbers the graph read from it
0cells of the map it votes in
129citing papers in PubMed
28.0field-weighted citation impact, top 1% 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

129 citing papers in PubMed, 415 citations in OpenAlex.

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  14. Phosphoproteomic Analysis ofFrontiers in cellular and infection microbiology · 2021
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  17. Ancestral roles of atypical cadherins in planar cell polarity.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
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69 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

10 authors at 1 institution in 1 country.

K NiebuhrAbteilung Zellbiologie und Immunologie/AG Molekulare Erkennung, Mascheroder Weg 1, 38124 Braunschweig, Germany.
F Ebel
R Frank
M Reinhard
E Domann
U D Carl
U Walter
F B Gertler
J Wehland
T Chakraborty
German Respiratory Society · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The ActA protein of the intracellular pathogen Listeria monocytogenes induces a dramatic reorganization of the actin-based cytoskeleton. Two profilin binding proteins, VASP and Mena, are the only cellular proteins known so far to bind directly to ActA. This interaction is mediated by a conserved module, the EVH1 domain. We identify E/DFPPPPXD/E, a motif repeated 4-fold within the primary sequence of ActA, as the core of the consensus ligand for EVH1 domains. This motif is also present and functional in at least two cellular proteins, zyxin and vinculin, which are in this respect major eukaryotic analogs of ActA. The functional importance of the novel protein-protein interaction was examined in the Listeria system. Removal of EVH1 binding sites on ActA reduces bacterial motility and strongly attenuates Listeria virulence. Taken together we demonstrate that ActA-EVH1 binding is a paradigm for a novel class of eukaryotic protein-protein interactions involving a proline-rich ligand that is clearly different from those described for SH3 and WW/WWP domains. This class of interactions appears to be of general importance for processes dependent on rapid actin remodeling.

Indexed as

ProlineAmino Acid SequenceAnimalsBacterial ProteinsBinding SitesCarrier ProteinsCell Adhesion MoleculesCytoskeletal ProteinsGlycoproteinsHeLa CellsHumansListeria monocytogenesMembrane ProteinsMetalloproteinsMiceMice, Inbred StrainsactA protein, Listeria monocytogenesBacterial ProteinsCarrier ProteinsCell Adhesion MoleculesCytoskeletal ProteinsEnah protein, mouseGlycoproteinsMembrane ProteinsMetalloproteinsMicrofilament ProteinsOligopeptidesPhosphoproteinsProlineVasodilator-Stimulated PhosphoproteinVinculinZyxinZYX protein, humanZyx protein, mouse

Identifiers

PMID9312002
PMCPMC1170174
OpenAlexW2152869893

What OpenQuestion holds

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Read underepoch 390

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.