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

doi:10.1002/j.1460-2075.1995.tb07274.x

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Article

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

The EMBO journal - 15 Jun 1995

Friederich E, Gouin E, Hellio R, Kocks C, Cossart P, Louvard D

Abstract excerpt

Actin assembly on the surface of Listeria monocytogenes in the cytoplasm of infected cells provides a model to study actin-based motility and changes in cell shape. We have shown previously that the ActA protein, exposed on the bacterial surface, is required for polarized nucleation of actin filaments. To investigate whether plasma membrane-associated ActA can control the organization of microfilaments and cell...

Topics

Actins
Amino Acid Sequence
Animals
Bacterial Proteins
Base Sequence
Cell Line
Cell Membrane
Cell Size
Cytoskeleton
Fibroblasts
Haplorhini

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

HeLa Cells

Humans

Listeria monocytogenes

Membrane Proteins

Molecular Sequence Data

Morphogenesis

Mutation

Source

Open in PubMed Open full text

Identifiers

PMID: 7796802
DOI: 10.1002/j.1460-2075.1995.tb07274.x
PMCID: PMC398392

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-7796802-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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Targeting of Listeria monocytogenes ActA protein to the plasma membrane as a tool to dissect both actin-based cell morphogenesis and ActA function.PMID 7796802Read ↗

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 ↗

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

Stability of the Listeria monocytogenes ActA protein in mammalian cells is regulated by the N-end rule pathway.Semantic proximity Read ↗

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

Listeria monocytogenesActA is a key player in evading autophagic recognitionSemantic proximity Read ↗

InlB: an invasion protein of Listeria monocytogenes with a novel type of surface association.Semantic proximity Read ↗

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 ↗

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.Semantic proximity Read ↗

Listeria monocytogenes ActA-mediated escape from autophagic recognition.Semantic proximity Read ↗

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

Dimeric structure of the cell shape protein MreC and its functional implications.Semantic proximity Read ↗

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