De-AMPylation of the small GTPase Rab1 by the pathogen Legionella pneumophila.

@article{Neunuebel2011DeAMPylationOT,
  title={De-AMPylation of the small GTPase Rab1 by the pathogen Legionella pneumophila.},
  author={M Ramona Neunuebel and Yang Chen and Andrew H. Gaspar and Peter S. Backlund and Alfred Yergey and Matthias P Machner},
  journal={Science},
  year={2011},
  volume={333 6041},
  pages={453-6}
}
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… CONTINUE READING
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