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      Targeting Rab GTPases to distinct membrane compartments.

      Nature reviews. Molecular cell biology
      Animals, Cattle, Cell Line, Cell Membrane, metabolism, Cytosol, GTP Phosphohydrolases, Guanosine Diphosphate, Humans, Models, Biological, Models, Molecular, Phosphorylation, Phylogeny, Protein Prenylation, Protein Structure, Tertiary, Saccharomyces cerevisiae, rab GTP-Binding Proteins, physiology

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          Abstract

          Rab GTPases are key to membrane-trafficking events in eukaryotic cells, and human cells contain more than 60 Rab proteins that are localized to distinct compartments. The recent determination of the structure of a monoprenylated Rab GTPase bound to GDP-dissociation inhibitor provides new molecular details that are relevant to models of Rab delivery. The further discovery of an integral membrane protein that can dissociate prenylated Rab proteins from GDP-dissociation inhibitor gives new insights into the mechanisms of Rab localization.

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