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  • Title: Rab13 Traffics on Vesicles Independent of Prenylation.
    Author: Ioannou MS, Girard M, McPherson PS.
    Journal: J Biol Chem; 2016 May 13; 291(20):10726-35. PubMed ID: 26969162.
    Abstract:
    Rab GTPases are critical regulators of membrane trafficking. The canonical view is that Rabs are soluble in their inactive GDP-bound form, and only upon activation and conversion to their GTP-bound state are they anchored to membranes through membrane insertion of a C-terminal prenyl group. Here we demonstrate that C-terminal prenylation is not required for Rab13 to associate with and traffic on vesicles. Instead, inactive Rab13 appears to associate with vesicles via protein-protein interactions. Only following activation does Rab13 associate with the plasma membrane, presumably with insertion of the C-terminal prenyl group into the membrane.
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