| pubmed-article:17947549 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17947549 | lifeskim:mentions | umls-concept:C0004627 | lld:lifeskim |
| pubmed-article:17947549 | lifeskim:mentions | umls-concept:C0752093 | lld:lifeskim |
| pubmed-article:17947549 | lifeskim:mentions | umls-concept:C0012727 | lld:lifeskim |
| pubmed-article:17947549 | lifeskim:mentions | umls-concept:C1419187 | lld:lifeskim |
| pubmed-article:17947549 | lifeskim:mentions | umls-concept:C1152881 | lld:lifeskim |
| pubmed-article:17947549 | lifeskim:mentions | umls-concept:C1704666 | lld:lifeskim |
| pubmed-article:17947549 | lifeskim:mentions | umls-concept:C1517892 | lld:lifeskim |
| pubmed-article:17947549 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
| pubmed-article:17947549 | lifeskim:mentions | umls-concept:C0208973 | lld:lifeskim |
| pubmed-article:17947549 | pubmed:issue | 5852 | lld:pubmed |
| pubmed-article:17947549 | pubmed:dateCreated | 2007-11-9 | lld:pubmed |
| pubmed-article:17947549 | pubmed:abstractText | Rab guanosine triphosphatases (GTPases) regulate vesicle trafficking in eukaryotic cells by reversibly associating with lipid membranes. Inactive Rab GTPases are maintained in the cytosol by binding to GDP-dissociation inhibitor (GDI). It is believed that specialized proteins are required to displace GDI from Rab GTPases before Rab activation by guanosine diphosphate-guanosine 5'-triphosphate (GDP-GTP) exchange factors (GEFs). Here, we found that SidM from Legionella pneumophila could act as both GEF and GDI-displacement factor (GDF) for Rab1. Rab1 released from GDI was inserted into liposomal membranes and was used as a substrate for SidM-mediated nucleotide exchange. During host cell infection, recruitment of Rab1 to Legionella-containing vacuoles depended on the GDF activity of SidM. Thus, GDF and GEF activity can be promoted by a single protein, and GDF activity can coordinate Rab1 recruitment from the GDI-bound pool. | lld:pubmed |
| pubmed-article:17947549 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17947549 | pubmed:language | eng | lld:pubmed |
| pubmed-article:17947549 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17947549 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:17947549 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17947549 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:17947549 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17947549 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17947549 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:17947549 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17947549 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17947549 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:17947549 | pubmed:issn | 1095-9203 | lld:pubmed |
| pubmed-article:17947549 | pubmed:author | pubmed-author:IsbergRalph... | lld:pubmed |
| pubmed-article:17947549 | pubmed:author | pubmed-author:MachnerMatthi... | lld:pubmed |
| pubmed-article:17947549 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:17947549 | pubmed:day | 9 | lld:pubmed |
| pubmed-article:17947549 | pubmed:volume | 318 | lld:pubmed |
| pubmed-article:17947549 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:17947549 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:17947549 | pubmed:pagination | 974-7 | lld:pubmed |
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| pubmed-article:17947549 | pubmed:meshHeading | pubmed-meshheading:17947549... | lld:pubmed |
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| pubmed-article:17947549 | pubmed:meshHeading | pubmed-meshheading:17947549... | lld:pubmed |
| pubmed-article:17947549 | pubmed:year | 2007 | lld:pubmed |
| pubmed-article:17947549 | pubmed:articleTitle | A bifunctional bacterial protein links GDI displacement to Rab1 activation. | lld:pubmed |
| pubmed-article:17947549 | pubmed:affiliation | Department of Molecular Biology and Microbiology, Tufts University School of Medicine, Boston, MA 02111, USA. | lld:pubmed |
| pubmed-article:17947549 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:17947549 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:17947549 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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