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Reference: Ignatev A, et al. (2008) A structural model of the GDP dissociation inhibitor rab membrane extraction mechanism. J Biol Chem 283(26):18377-84

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Abstract


RabGDI-facilitated extraction of prenylated Rab proteins from membranes plays an important role in vesicular membrane trafficking. The investigated thermodynamic properties of yeast Rab:GDI and Rab:MRS6 complexes demonstrated differences in the Rab binding properties of the closely related RabGDI and MRS6 proteins, consistent with their functional diversity. The importance of the Rab C-terminus and its prenylation for GDI/MRS6 binding was demonstrated using both biochemical and structural data. The presented structures of the apo-form yeast RabGDI and its two complexes with unprenylated Rab proteins, together with the earlier published structures of the prenylated Ypt1:RabGDI provide evidence of allosteric regulation of the GDI lipid binding site opening, which plays a key role in the proposed mechanism of GDI mediated Rab extraction. We suggest a model for the interaction of GDI with prenylated Rab proteins which incorporates a stepwise increase in affinity as the 3 different partial interactions are successively formed.

Reference Type
Journal Article
Authors
Ignatev A, Kravchenko S, Rak A, Goody RS, Pylypenko O
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