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First published online March 29, 2004

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Innate interference with membrane trafficking

Interferons play essential roles in innate immunity, stimulating synthesis of numerous proteins required for intracellular defence against pathogens. These include proteins such as nitric oxide synthase 2 (NOS2/iNOS) and dsRNA-dependent protein kinase (PKR), as well as several GTPases. Members of the 47 kDa GTPase family, for example, are essential for protection from certain intracellular pathogens; however, their precise roles are unclear. Jens Zerrahn and co-workers have therefore investigated the function of a -interferon-inducible member of this family, IIGP (see p. 1747). Intriguingly, they find that IIGP interacts in two-hybrid assays with hook 3 – a microtubule-binding linker protein implicated in membrane trafficking. The authors use coimmunoprecipitation and fluorescence microscopy to show that this interaction occurs in vivo on Golgi membranes. They also demonstrate that IIGP must be GTP bound to interact with hook 3 and use deletion mutants to examine the regions of the proteins that interact. Their findings suggest that IIGP somehow regulates intracellular membrane trafficking. It could, for instance, target endosomal/phagosomal compartments in which pathogens reside, promoting degradation of their contents, or interfere with nutrient provision.

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Related articles in JCS:

IIGP, a member of the IFN inducible and microbial defense mediating 47 kDa GTPase family, interacts with the microtubule binding protein hook3

Frank Kaiser, Stefan H. E. Kaufmann, and Jens Zerrahn
JCS 2004 117: 1747-1756. [Abstract] [Full Text]  

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Related articles in JCS Similar articles in this journal Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Google Scholar Google Scholar Search for Related Content Social Bookmarking                         What's this?