The Legionella effector protein DrrA AMPylates the membrane traffic regulator Rab1b
| Autor: | Roger S. Goody, Heide Peters, Wulf Blankenfeldt, Julia Blümer, Aymelt Itzen, Matthias P. Müller |
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| Rok vydání: | 2010 |
| Předmět: |
Models
Molecular GTPase-activating protein Guanosine GTPase Guanosine triphosphate Legionella pneumophila Mass Spectrometry chemistry.chemical_compound Bacterial Proteins Chlorocebus aethiops Animals Guanine Nucleotide Exchange Factors Adenylylation Multidisciplinary Crystallography biology RAB1 biology.organism_classification Adenosine Monophosphate Cell biology Protein Structure Tertiary rab1 GTP-Binding Proteins chemistry Biochemistry Guanosine diphosphate rab GTP-Binding Proteins COS Cells |
| Zdroj: | Science (New York, N.Y.). 329(5994) |
| ISSN: | 1095-9203 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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