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Membrane targeting of the small GTPase Rab9 is accompanied by nucleotide exchange

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Abstract

THE Rab GTPases are key regulators of vesicular transport1–6. A fraction of Rab proteins is present in the cytosol, bound with GDP, complexed to a protein termed GDI7–10. Rab9 is localized prim-arily to late endosomes, where it aids the transport of mannose 6-phosphate receptors to the trans-Golgi network11. It has been proposed that Rab proteins are delivered to specific membranes by GDI, and that this process is accompanied by the exchange of bound GDP for GTP1–3. In addition, Rab localization requires carboxy-terminal prenylation and specific structural determinants12–14. Here we describe the reconstitution of the selec-tive targeting of prenylated Rab9 protein onto late endosome mem-branes and show that this process is accompanied by endosome-triggered nucleotide exchange.

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Authors and Affiliations

  1. Department of Biochemistry, Stanford University School of Medicine, Stanford, California, 94305-5307, USA

    Thierry Soldati, Allan D. Shapiro, A. Barbara Dirac Svejstrup & Suzanne R. Pfefffer

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  1. Thierry Soldati
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  2. Allan D. Shapiro
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  3. A. Barbara Dirac Svejstrup
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  4. Suzanne R. Pfefffer
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Soldati, T., Shapiro, A., Dirac Svejstrup, A. et al. Membrane targeting of the small GTPase Rab9 is accompanied by nucleotide exchange. Nature 369, 76–78 (1994). https://doi.org/10.1038/369076a0

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