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Sci. STKE, 13 November 2007
Vol. 2007, Issue 412, p. tw419
[DOI: 10.1126/stke.4122007tw419]

EDITORS' CHOICE

Microbiology Doing Double Duty

Stella M. Hurtley

Science, AAAS, Cambridge CB2 1LQ, UK

During intracellular vesicular trafficking, delivery of Rab guanosine triphosphatases (GTPases) to sites of activation involves their release from a guanine nucleotide dissociation inhibitor (GDI) by a so-called GDI displacement factor (GDF). The identification of GDFs has been difficult. Now Machner and Isberg provide evidence for the existence of such an activity, surprisingly in a bifunctional protein--a guanine nucleotide exchange protein associated with the formation of a replication vacuole by the intracellular pathogen Legionella pneumophila.

M. P. Machner, R. R. Isberg, A bifunctional bacterial protein links GDI displacement to Rab1 activation. Science 318, 974-977 (2007). [Abstract] [Full Text]

Citation: S. M. Hurtley, Doing Double Duty. Sci. STKE 2007, tw419 (2007).



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