ArticleCellular microbiology2007
Localization of protein kinase C epsilon to macrophage vacuoles perforated by Listeria monocytogenes cytolysin.
Article in Cellular microbiology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 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
10 citing papers in PubMed, 20 citations in OpenAlex.
- Review
- Bacterial infections and cancer.EMBO reports · 2018Review
- Host cell perforation by listeriolysin O (LLO) activates a CaMolecular biology of the cell · 2018Article
- Review
- Shigella IpaH0722 E3 ubiquitin ligase effector targets TRAF2 to inhibit PKC-NF-κB activity in invaded epithelial cells.PLoS pathogens · 2013Article
- The bacterial and cellular determinants controlling the recruitment of mTOR to the Salmonella-containing vacuole.Biology open · 2012Article
- Galectin 8 targets damaged vesicles for autophagy to defend cells against bacterial invasion.Nature · 2012Article
- A diacylglycerol-dependent signaling pathway contributes to regulation of antibacterial autophagy.Cell host & microbe · 2010Article
- Protein kinase C delta is essential for optimal macrophage-mediated phagosomal containment of Listeria monocytogenes.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
- Protein kinase C as a stress sensor.Cellular signalling · 2007Review
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
Three proteins secreted by Listeria monocytogenes facilitate escape from macrophage vacuoles: the cholesterol-dependent cytolysin listeriolysin O (LLO), a phosphoinositide-specific phospholipase C (PI-PLC) and a broad-range phospholipase C (PC-PLC). LLO and PI-PLC can activate several members of the protein kinase C (PKC) family during infection. PKCepsilon is a novel PKC that contributes to macrophage activation, defence against bacterial infection, and phagocytosis; however, a role for PKCepsilon in Lm infections has not been described. To study PKCepsilon dynamics, PKCepsilon-YFP chimeras were visualized in macrophages during Lm infection. PKCepsilon-YFP was recruited to forming vacuoles during macrophage phagocytosis of Lm and again later to fully formed Lm vacuoles. The PKCepsilon-YFP localization to the fully formed Lm vacuole was LLO-dependent but independent of PI-PLC or PC-PLC. PKCepsilon-YFP recruitment often followed LLO perforation of the membrane, as indicated by localization of PKCepsilon-YFP to Lm vacuoles after they released small fluorescent dyes into the cytoplasm. PKCepsilon-YFP recruitment to vesicles also followed phagocytosis of LLO-containing liposomes or osmotic lysis of endocytic vesicles, indicating that vacuole perforation by LLO was the chief cause of the PKCepsilon response. These studies implicate PKCepsilon in a cellular mechanism for recognizing damaged membranous organelles, including the disrupted vacuoles created when Lm escapes into cytoplasm.
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