Source:http://linkedlifedata.com/resource/pubmed/id/16906144
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
9
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pubmed:dateCreated |
2006-9-1
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pubmed:abstractText |
The intracellular pathogen Legionella pneumophila avoids fusion with lysosomes and subverts membrane transport from the endoplasmic reticulum to create an organelle that supports bacterial replication. Transport of endoplasmic reticulum-derived vesicles to the Legionella-containing vacuole (LCV) requires bacterial proteins that are translocated into host cells by a type IV secretion apparatus called Dot/Icm. Recent observations have revealed recruitment of the host GTPase Rab1 to the LCV by a process requiring the Dot/Icm system. Here, a visual screen was used to identify L. pneumophila mutants with defects in Rab1 recruitment. One of the factors identified in this screen was DrrA, a new Dot/Icm substrate protein translocated into host cells. We show that DrrA is a potent and highly specific Rab1 guanine nucleotide-exchange factor (GEF). DrrA can disrupt Rab1-mediated secretory transport to the Golgi apparatus by competing with endogenous exchange factors to recruit and activate Rab1 on plasma membrane-derived organelles. These data establish that intracellular pathogens have the capacity to directly modulate the activation state of a specific member of the Rab family of GTPases and thus further our understanding of the mechanisms used by bacterial pathogens to manipulate host vesicular transport.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DrrA protein, Bacteria,
http://linkedlifedata.com/resource/pubmed/chemical/Guanine Nucleotide Exchange Factors,
http://linkedlifedata.com/resource/pubmed/chemical/rab1 GTP-Binding Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
1465-7392
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
8
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
971-7
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pubmed:dateRevised |
2011-11-3
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pubmed:meshHeading |
pubmed-meshheading:16906144-Animals,
pubmed-meshheading:16906144-Bacterial Proteins,
pubmed-meshheading:16906144-Biological Transport, Active,
pubmed-meshheading:16906144-Cell Membrane,
pubmed-meshheading:16906144-Cells, Cultured,
pubmed-meshheading:16906144-DNA-Binding Proteins,
pubmed-meshheading:16906144-Female,
pubmed-meshheading:16906144-Golgi Apparatus,
pubmed-meshheading:16906144-Guanine Nucleotide Exchange Factors,
pubmed-meshheading:16906144-Legionella pneumophila,
pubmed-meshheading:16906144-Mice,
pubmed-meshheading:16906144-Mutation,
pubmed-meshheading:16906144-Protein Transport,
pubmed-meshheading:16906144-Vacuoles,
pubmed-meshheading:16906144-rab1 GTP-Binding Proteins
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pubmed:year |
2006
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pubmed:articleTitle |
The Legionella pneumophila effector protein DrrA is a Rab1 guanine nucleotide-exchange factor.
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pubmed:affiliation |
Section of Microbial Pathogenesis, Yale University School of Medicine, Boyer Center for Molecular Medicine, 295 Congress Avenue, New Haven, CT 06536, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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