Localization of protein kinase C ε to macrophage vacuoles perforated by Listeria monocytogenes cytolysin
dc.contributor.author | Shaughnessy, Lee M. | en_US |
dc.contributor.author | Lipp, Peter | en_US |
dc.contributor.author | Lee, Kyung-Dall | en_US |
dc.contributor.author | Swanson, Joel A. | en_US |
dc.date.accessioned | 2010-06-01T20:08:35Z | |
dc.date.available | 2010-06-01T20:08:35Z | |
dc.date.issued | 2007-07 | en_US |
dc.identifier.citation | Shaughnessy, Lee M.; Lipp, Peter; Lee, Kyung-Dall; Swanson, Joel A. (2007). "Localization of protein kinase C ε to macrophage vacuoles perforated by Listeria monocytogenes cytolysin." Cellular Microbiology 9(7): 1695-1704. <http://hdl.handle.net/2027.42/73267> | en_US |
dc.identifier.issn | 1462-5814 | en_US |
dc.identifier.issn | 1462-5822 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/73267 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=17346313&dopt=citation | en_US |
dc.description.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. PKCε is a novel PKC that contributes to macrophage activation, defence against bacterial infection, and phagocytosis; however, a role for PKCε in Lm infections has not been described. To study PKCε dynamics, PKCε-YFP chimeras were visualized in macrophages during Lm infection. PKCε-YFP was recruited to forming vacuoles during macrophage phagocytosis of Lm and again later to fully formed Lm vacuoles. The PKCε-YFP localization to the fully formed Lm vacuole was LLO-dependent but independent of PI-PLC or PC-PLC. PKCε-YFP recruitment often followed LLO perforation of the membrane, as indicated by localization of PKCε-YFP to Lm vacuoles after they released small fluorescent dyes into the cytoplasm. PKCε-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 PKCε response. These studies implicate PKCε in a cellular mechanism for recognizing damaged membranous organelles, including the disrupted vacuoles created when Lm escapes into cytoplasm. | en_US |
dc.format.extent | 407170 bytes | |
dc.format.extent | 3109 bytes | |
dc.format.mimetype | application/pdf | |
dc.format.mimetype | text/plain | |
dc.publisher | Blackwell Publishing Ltd | en_US |
dc.rights | © 2007 The Authors; Journal compilation © 2007 Blackwell Publishing Ltd | en_US |
dc.title | Localization of protein kinase C ε to macrophage vacuoles perforated by Listeria monocytogenes cytolysin | en_US |
dc.type | Article | en_US |
dc.subject.hlbsecondlevel | Molecular, Cellular and Developmental Biology | en_US |
dc.subject.hlbtoplevel | Health Sciences | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.contributor.affiliationum | Department of Microbiology and Immunology, University of Michigan Medical School, Ann Arbor, MI 48109, USA. | en_US |
dc.contributor.affiliationum | Department of Pharmaceutical Sciences, College of Pharmacy, University of Michigan, Ann Arbor, MI 48109, USA. | en_US |
dc.contributor.affiliationother | Institute for Molecular Cell Biology, Saarland University, Homburg, Germany. | en_US |
dc.identifier.pmid | 17346313 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/73267/1/j.1462-5822.2007.00903.x.pdf | |
dc.identifier.doi | 10.1111/j.1462-5822.2007.00903.x | en_US |
dc.identifier.source | Cellular Microbiology | en_US |
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dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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