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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5852
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pubmed:dateCreated |
2007-11-9
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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.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
1095-9203
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
9
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pubmed:volume |
318
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
974-7
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pubmed:meshHeading |
pubmed-meshheading:17947549-Bacterial Proteins,
pubmed-meshheading:17947549-Cytoplasm,
pubmed-meshheading:17947549-Guanine Nucleotide Dissociation Inhibitors,
pubmed-meshheading:17947549-Guanine Nucleotide Exchange Factors,
pubmed-meshheading:17947549-Guanosine 5'-O-(3-Thiotriphosphate),
pubmed-meshheading:17947549-Guanosine Diphosphate,
pubmed-meshheading:17947549-Humans,
pubmed-meshheading:17947549-Legionella pneumophila,
pubmed-meshheading:17947549-Liposomes,
pubmed-meshheading:17947549-Protein Binding,
pubmed-meshheading:17947549-Protein Structure, Tertiary,
pubmed-meshheading:17947549-Recombinant Proteins,
pubmed-meshheading:17947549-Vacuoles,
pubmed-meshheading:17947549-rab1 GTP-Binding Proteins
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pubmed:year |
2007
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pubmed:articleTitle |
A bifunctional bacterial protein links GDI displacement to Rab1 activation.
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pubmed:affiliation |
Department of Molecular Biology and Microbiology, Tufts University School of Medicine, Boston, MA 02111, USA.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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