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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
6041
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pubmed:dateCreated |
2011-7-22
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pubmed:abstractText |
The bacterial pathogen Legionella pneumophila exploits host cell vesicle transport by transiently manipulating the activity of the small guanosine triphosphatase (GTPase) Rab1. The effector protein SidM recruits Rab1 to the Legionella-containing vacuole (LCV), where it activates Rab1 and then AMPylates it by covalently adding adenosine monophosphate (AMP). L. pneumophila GTPase-activating protein LepB inactivates Rab1 before its removal from LCVs. Because LepB cannot bind AMPylated Rab1, the molecular events leading to Rab1 inactivation are unknown. We found that the effector protein SidD from L. pneumophila catalyzed AMP release from Rab1, generating de-AMPylated Rab1 accessible for inactivation by LepB. L. pneumophila mutants lacking SidD were defective for Rab1 removal from LCVs, identifying SidD as the missing link connecting the processes of early Rab1 accumulation and subsequent Rab1 removal during infection.
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pubmed:grant |
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pubmed:commentsCorrections |
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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 |
http://linkedlifedata.com/resource/pubmed/chemical/5'-Guanylic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Monophosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Guanine Nucleotide Exchange Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Guanosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/LepB protein, Legionella pneumophila,
http://linkedlifedata.com/resource/pubmed/chemical/Ligands,
http://linkedlifedata.com/resource/pubmed/chemical/Mutant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/SidM protein, Legionella pneumophila,
http://linkedlifedata.com/resource/pubmed/chemical/rab1 GTP-Binding Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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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 |
22
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pubmed:volume |
333
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
453-6
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pubmed:dateRevised |
2011-11-14
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pubmed:meshHeading |
pubmed-meshheading:21680813-5'-Guanylic Acid,
pubmed-meshheading:21680813-Adenosine Monophosphate,
pubmed-meshheading:21680813-Animals,
pubmed-meshheading:21680813-Bacterial Proteins,
pubmed-meshheading:21680813-COS Cells,
pubmed-meshheading:21680813-Cercopithecus aethiops,
pubmed-meshheading:21680813-Golgi Apparatus,
pubmed-meshheading:21680813-Guanine Nucleotide Exchange Factors,
pubmed-meshheading:21680813-Guanosine Triphosphate,
pubmed-meshheading:21680813-Humans,
pubmed-meshheading:21680813-Legionella pneumophila,
pubmed-meshheading:21680813-Ligands,
pubmed-meshheading:21680813-Macrophages,
pubmed-meshheading:21680813-Mice,
pubmed-meshheading:21680813-Mice, Inbred A,
pubmed-meshheading:21680813-Models, Biological,
pubmed-meshheading:21680813-Mutant Proteins,
pubmed-meshheading:21680813-U937 Cells,
pubmed-meshheading:21680813-Vacuoles,
pubmed-meshheading:21680813-rab1 GTP-Binding Proteins
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pubmed:year |
2011
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pubmed:articleTitle |
De-AMPylation of the small GTPase Rab1 by the pathogen Legionella pneumophila.
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pubmed:affiliation |
Cell Biology and Metabolism Program, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892, USA.
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pubmed:publicationType |
Journal Article,
Research Support, N.I.H., Intramural
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