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. 2018 Jan 3;9:44. doi: 10.1038/s41467-017-02110-1

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© The Author(s) 2017

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 6 — Mechanistic model of the dependence of GtgE-mediated Rab32-cleavage on SopD2. The cooperation of SopD2 and GtgE allows rapid Rab32-inactivation since the proteolysis is a result of a series of fast enzymatic conversions. Rab32 is recruited to the membrane by a corresponding GEF (BLOC-3). The resulting SCV-bound GTP-loaded GTPase is then rapidly converted by the action of the GAP SopD2. Eventually, Rab32:GDP is cleaved quickly by GtgE. GEF guanine-nucleotide exchange factor, GDI GDP-dissociation inhibitor