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. 2017 Oct 25;10(3):227–242. doi: 10.1080/21541248.2017.1371268

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© 2017 The Author(s). Published with license by Taylor & Francis

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 15. — Mechanism of GG-Rab5 extraction from the endosome membrane into the cytoplasm. A sequential recognition and stabilization proceeds from (A) membrane-bound un-complexed Rab5(GDP) tilted towards the membrane surface with only partially accessible switch regions. (B) GDI recognizes Rab5 via its RBP and forms initial contacts with the switch regions. (C) The orientation of GDI slightly changes in order to allow interactions of the GDI CCR and the Rab5 HVR while the GG-binding pocket opens. (D) When the GG chains are accommodated within the GG-binding pocket, the Rab5(GDP):GDI complex detaches from the membrane. (E) The soluble complex is characterized by 1) manifold interactions between the GDI RBP and Rab5 switch regions, 2) Rab-specific recognition of Rab5 HVR by the GDI CCR, and 3) an opening of the GG-binding pocket with Rab5 GG-chains inserted.