Editors' ChoiceMicrobiology

Doing Double Duty

See allHide authors and affiliations

Science's STKE  13 Nov 2007:
Vol. 2007, Issue 412, pp. tw419
DOI: 10.1126/stke.4122007tw419

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]

Stay Connected to Science Signaling