The immunity-related GTPase Irga6 dimerizes in a parallel head-to-head fashion

The immunity-related GTPases (IRGs) constitute a powerful cell-autonomous resistance system against several intracellular pathogens. Irga6 is a dynamin-like protein that oligomerizes at the parasitophorous vacuolar membrane (PVM) of Toxoplasma gondii leading to its vesiculation. Based on a previous...

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Bibliographic Details
Main Author: Schulte, Kathrin (author)
Other Authors: Pawlowski, Nikolaus (author), Faelber, Katja (author), Fröhlich, Chris (author), Howard, Jonathan (author), Daumke, Oliver (author)
Format: article
Language:eng
Published: 2016
Subjects:
Innate immunity
IRG proteins
GTPase
Dynamin superfamily
Dimerization
Oligomerization
Online Access:http://hdl.handle.net/10400.7/555
Country:Portugal
Oai:oai:arca.igc.gulbenkian.pt:10400.7/555
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Summary:The immunity-related GTPases (IRGs) constitute a powerful cell-autonomous resistance system against several intracellular pathogens. Irga6 is a dynamin-like protein that oligomerizes at the parasitophorous vacuolar membrane (PVM) of Toxoplasma gondii leading to its vesiculation. Based on a previous biochemical analysis, it has been proposed that the GTPase domains of Irga6 dimerize in an antiparallel fashion during oligomerization.

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