ArticleThe EMBO journal1995
Targeting of Listeria monocytogenes ActA protein to the plasma membrane as a tool to dissect both actin-based cell morphogenesis and ActA function.
Article in The EMBO journal, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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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.
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Who cites it
25 citing papers in PubMed, 80 citations in OpenAlex.
- ActA promotes Listeria monocytogenes aggregation, intestinal colonization and carriage.PLoS pathogens · 2013Article
- Yogi Berra, Forrest Gump, and the discovery of Listeria actin comet tails.Molecular biology of the cell · 2012Article
- The stress-induced virulence protein InlH controls interleukin-6 production during murine listeriosis.Infection and immunity · 2010Article
- The Listeria monocytogenes virulence factor InlJ is specifically expressed in vivo and behaves as an adhesin.Infection and immunity · 2008Article
- Actin-dependent movement of bacterial pathogens.Nature reviews. Microbiology · 2006Review
- Morphology of the lamellipodium and organization of actin filaments at the leading edge of crawling cells.Biophysical journal · 2005Article
- Villin enhances hepatocyte growth factor-induced actin cytoskeleton remodeling in epithelial cells.Molecular biology of the cell · 2003Article
- Pivotal role of VASP in Arp2/3 complex-mediated actin nucleation, actin branch-formation, and Listeria monocytogenes motility.The Journal of cell biology · 2001Article
- Listeria pathogenesis and molecular virulence determinants.Clinical microbiology reviews · 2001Review
- gC1q-R/p32, a C1q-binding protein, is a receptor for the InlB invasion protein of Listeria monocytogenes.The EMBO journal · 2000Article
- Growing an actin gel on spherical surfaces.Biophysical journal · 2000Article
- LPP, an actin cytoskeleton protein related to zyxin, harbors a nuclear export signal and transcriptional activation capacity.Molecular biology of the cell · 2000Article
- Villin-like actin-binding proteins are expressed ubiquitously in Arabidopsis.Plant physiology · 2000Article
- The actin-based nanomachine at the leading edge of migrating cells.Biophysical journal · 1999Article
- Polymerizing microtubules activate site-directed F-actin assembly in nerve growth cones.Molecular biology of the cell · 1999Article
- Interactions of Listeria monocytogenes with mammalian cells during entry and actin-based movement: bacterial factors, cellular ligands and signaling.The EMBO journal · 1998Review
- Interactions of the bacterial pathogen Listeria monocytogenes with mammalian cells: bacterial factors, cellular ligands, and signaling.Folia microbiologica · 1998Review
- ActA is a dimer.Proceedings of the National Academy of Sciences of the United States of America · 1997Article
- Ribotypes and virulence gene polymorphisms suggest three distinct Listeria monocytogenes lineages with differences in pathogenic potential.Infection and immunity · 1997Article
- Common themes in microbial pathogenicity revisited.Microbiology and molecular biology reviews : MMBR · 1997Review
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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 shape, variants of ActA, in which the bacterial membrane signal had been replaced by a plasma membrane anchor sequence, were produced in mammalian cells. While both cytoplasmic and membrane-bound forms of ActA increased the F-actin content, only membrane-associated ActA caused the formation of plasma membrane extensions. This finding suggests that ActA acts as an actin filament nucleator and shows that permanent association with the inner face of the plasma membrane is required for changes in cell shape. Based on the observation that the amino-terminal segment of ActA and the remaining portion which includes the proline-rich repeats cause distinct phenotypic modifications in transfected cells, we propose a model in which two functional domains of ActA cooperate in the nucleation and dynamic turnover of actin filaments. The present approach is a new model system to dissect the mechanism of action of ActA and to further investigate interactions of the plasma membrane and the actin cytoskeleton during dynamic changes of cell shape.
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Registered trials
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.