Affiliation:
1. Department of Physical Biochemistry, Max Planck Institute of Molecular Physiology, Dortmund, NRW, 44227, Germany.
Abstract
Legionella
Hijacks Rab
Legionella pneumophila
can infect eukaryotic cells and takes up residence within intracellular vacuoles, where it multiplies. In order to produce and maintain this intracellular niche, the pathogen must manipulate membrane trafficking within the host cell. Now,
Müller
et al.
(p.
946
, published online 22 July) describe the ability of
Legionella pneumophila
to manipulate vesicular trafficking by the covalent modification of the small guanosine triphosphatase (GTPase) Rab1, which normally regulates the transport of endoplasmic reticulum–derived vesicles in eukaryotic cells. The
Legionella
protein DrrA is released into the cytosol of infected cells, where it specifically AMPylates a tyrosine residue of one of the regulating regions of Rab1. The modification renders the Rab protein inaccessible to GTPase-activating proteins and thus locks it in its active guanosine triphosphate–bound state.
Publisher
American Association for the Advancement of Science (AAAS)
Cited by
311 articles.
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