Membrane targeting of the small GTPase Rab9 is accompanied by nucleotide exchange
摘要：
THE Rab GTPases are key regulators of vesicular transport. A fraction of Rab proteins is present in the cytosol, bound with GDP, complexed to a protein termed GDI. Rab9 is localized prim-arily to late endosomes, where it aids the transport of mannose 6-phosphate receptors to thenetwork. 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 GTP. In addition, Rab localization requires carboxy-terminal prenylation and specific structural determinants. 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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关键词：
Animals Rats Endoplasmic Reticulum CHO Cells Intracellular Membranes GTP Phosphohydrolases GTP-Binding Proteins Guanine Nucleotide Dissociation Inhibitors rab GTP-Binding Proteins Guanine Nucleotides
DOI：
10.1038/369076a0
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