Abstract：
:Prenylated Rab proteins exist in the cytosol as soluble, high-affinity complexes with GDI that need to be disrupted for membrane attachment and targeting of Rab proteins. The Legionella pneumophila protein DrrA displaces GDI from Rab1:GDI complexes, incorporating Rab1 into Legionella-containing vacuoles and activating Rab1 by exchanging GDP for GTP. Here, we present the crystal structure of a complex between the GEF domain of DrrA and Rab1 and a detailed kinetic analysis of this exchange. DrrA efficiently catalyzes nucleotide exchange and mimics the general nucleotide exchange mechanism of mammalian GEFs for Ras-like GTPases. We show that the GEF activity of DrrA is sufficient to displace prenylated Rab1 from the Rab1:GDI complex. Thus, apparent GDI displacement by DrrA is linked directly to nucleotide exchange, suggesting a basic model for GDI displacement and specificity of Rab localization that does not require discrete GDI displacement activity.
journal_name
Mol Celljournal_title
Molecular cellauthors
Schoebel S,Oesterlin LK,Blankenfeldt W,Goody RS,Itzen Adoi
10.1016/j.molcel.2009.11.014subject
Has Abstractpub_date
2009-12-25 00:00:00pages
1060-72issue
6eissn
1097-2765issn
1097-4164pii
S1097-2765(09)00828-4journal_volume
36pub_type
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