| pubmed-article:16906144 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16906144 | lifeskim:mentions | umls-concept:C0023238 | lld:lifeskim |
| pubmed-article:16906144 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:16906144 | lifeskim:mentions | umls-concept:C0120465 | lld:lifeskim |
| pubmed-article:16906144 | lifeskim:mentions | umls-concept:C1419187 | lld:lifeskim |
| pubmed-article:16906144 | pubmed:issue | 9 | lld:pubmed |
| pubmed-article:16906144 | pubmed:dateCreated | 2006-9-1 | lld:pubmed |
| pubmed-article:16906144 | 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. | lld:pubmed |
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| pubmed-article:16906144 | pubmed:language | eng | lld:pubmed |
| pubmed-article:16906144 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16906144 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:16906144 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:16906144 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16906144 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16906144 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:16906144 | pubmed:issn | 1465-7392 | lld:pubmed |
| pubmed-article:16906144 | pubmed:author | pubmed-author:RoyCraig RCR | lld:pubmed |
| pubmed-article:16906144 | pubmed:author | pubmed-author:LambrightDavi... | lld:pubmed |
| pubmed-article:16906144 | pubmed:author | pubmed-author:MurataTakahir... | lld:pubmed |
| pubmed-article:16906144 | pubmed:author | pubmed-author:ToomreDerek... | lld:pubmed |
| pubmed-article:16906144 | pubmed:author | pubmed-author:IngmundsonAly... | lld:pubmed |
| pubmed-article:16906144 | pubmed:author | pubmed-author:DelpratoAnnaA | lld:pubmed |
| pubmed-article:16906144 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16906144 | pubmed:volume | 8 | lld:pubmed |
| pubmed-article:16906144 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16906144 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16906144 | pubmed:pagination | 971-7 | lld:pubmed |
| pubmed-article:16906144 | pubmed:dateRevised | 2011-11-3 | lld:pubmed |
| pubmed-article:16906144 | pubmed:meshHeading | pubmed-meshheading:16906144... | lld:pubmed |
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| pubmed-article:16906144 | pubmed:meshHeading | pubmed-meshheading:16906144... | lld:pubmed |
| pubmed-article:16906144 | pubmed:meshHeading | pubmed-meshheading:16906144... | lld:pubmed |
| pubmed-article:16906144 | pubmed:meshHeading | pubmed-meshheading:16906144... | lld:pubmed |
| pubmed-article:16906144 | pubmed:meshHeading | pubmed-meshheading:16906144... | lld:pubmed |
| pubmed-article:16906144 | pubmed:meshHeading | pubmed-meshheading:16906144... | lld:pubmed |
| pubmed-article:16906144 | pubmed:year | 2006 | lld:pubmed |
| pubmed-article:16906144 | pubmed:articleTitle | The Legionella pneumophila effector protein DrrA is a Rab1 guanine nucleotide-exchange factor. | lld:pubmed |
| pubmed-article:16906144 | pubmed:affiliation | Section of Microbial Pathogenesis, Yale University School of Medicine, Boyer Center for Molecular Medicine, 295 Congress Avenue, New Haven, CT 06536, USA. | lld:pubmed |
| pubmed-article:16906144 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:16906144 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:16906144 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:16906144 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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