The tandem repeat domain in the Listeria monocytogenes ActA protein controls the rate of actin-based motility, the percentage of moving bacteria, and the localization of vasodilator-stimulated phosphoprotein and profilin.

doi:10.1083/jcb.135.3.647

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Article

The tandem repeat domain in the Listeria monocytogenes ActA protein controls the rate of actin-based motility, the percentage of moving bacteria, and the localization of vasodilator-stimulated phosphoprotein and profilin.

The Journal of cell biology - 1 Nov 1996

Smith G A, Theriot J A, Portnoy D A

Abstract excerpt

The ActA protein is responsible for the actin-based movement of Listeria monocytogenes in the cytosol of eukaryotic cells. Analysis of mutants in which we varied the number of proline-rich repeats (PRR; consensus sequence DFPPPPTDEEL) revealed a linear relationship between the number of PRRs and...

Topics

Actins
Animals
Bacterial Proteins
Cell Adhesion Molecules
Cell Line
Contractile Proteins
DNA, Bacterial
Humans
Lethal Dose 50
Listeria monocytogenes
Membrane Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Mice

Mice, Inbred BALB C

Microfilament Proteins

Mutation

Phosphoproteins

Polymers

Profilins

Source

Open in PubMed Open full text

Identifiers

PMID: 8909540
DOI: 10.1083/jcb.135.3.647
PMCID: PMC2121076

Genes

VASP

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-8909540-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

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The tandem repeat domain in the Listeria monocytogenes ActA protein controls the rate of actin-based motility, the percentage of moving bacteria, and the localization of vasodilator-stimulated phosphoprotein and profilin.PMID 8909540Read ↗

The amino-terminal part of ActA is critical for the actin-based motility of Listeria monocytogenes; the central proline-rich region acts as a stimulator.Semantic proximity Read ↗

Systematic mutational analysis of the amino-terminal domain of the Listeria monocytogenes ActA protein reveals novel functions in actin-based motility.Semantic proximity Read ↗

Three regions within ActA promote Arp2/3 complex-mediated actin nucleation and Listeria monocytogenes motility.Semantic proximity Read ↗

Targeting of Listeria monocytogenes ActA protein to the plasma membrane as a tool to dissect both actin-based cell morphogenesis and ActA function.Semantic proximity Read ↗

Isolation of Listeria monocytogenes mutants with high-level in vitro expression of host cytosol-induced gene products.Semantic proximity Read ↗

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The actin-polymerization protein from Listeria ivanovii is a large repeat protein which shows only limited amino acid sequence homology to ActA from Listeria monocytogenes.Semantic proximity Read ↗

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Actin assembly-inducing protein ActA promotes FcγRIa-mediated <i>Listeria</i> internalizationSemantic proximity Read ↗

FrzE of Myxococcus xanthus is homologous to both CheA and CheY of Salmonella typhimurium.Semantic proximity Read ↗

A gene-expression program reflecting the innate immune response of cultured intestinal epithelial cells to infection by Listeria monocytogenes.Semantic proximity Read ↗

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