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γS to prenylated Rab9 complexed with Rab GDI. Rab GDI inhibits nucleotide exchange on Rab proteins because it stabilizes them in the GDP-bound conformation. The authors succeeded in identifying a factor that relieves this inhibition and provided an elegant demonstration that this protein is a GDI-releasing factor rather than a nucleotide exchange factor. These results lend direct support to the hypothesis that release of GDI and GDP/GTP exchange are catalyzed by distinct factors. Furthermore, this paper shows that the GDI-displacement factor here identified acts on endosomal Rab proteins (Rab5, Rab7 and Rab9) but is inactive on Rab1, a Rab protein of the secretory pathway.
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Wilson AL, Erdman RA,. Maltese WA: Association of Rab1B with GDP-dissociation inhibitor (GDI) is required for recycling but not initial membrane targeting of the rab protein. J Biol Chem 1996, 271:10932-10940. Can REP itself deliver prenylated Rab proteins to membranes or is Rab GDI required as an intermediate? The solution to this problem was found using an ingenious mutagenesis approach. The authors exploited a Rab1B effector mutant (Asp44→Asn) that fails to form a complex with Rab GDI. This defect is not due to the inability of the mutant protein to undergo prenylation, which occurs normally. The mutant protein was also shown to be efficiently delivered to the membrane but was absent from the cytosol. This study therefore demonstrates that newly synthesized Rab1 B can be prenylated and delivered to the membrane by REP without requiring a Rab GDI bound intermediate. In contrast, Rab GDI is absolutely required for the recycling of Rab1B from the membrane to the cytosol.
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Schalk I, Zeng K, Wu S-K, Stura EA, Matteson J, Huang M, Tandon A, Wilson IA, Balch WE: Structure and mutational analysis of Rab GDP-dissociation inhibitor. Nature 1996, 381:42-48. This paper reports the crystal structure of the first described bovine Rab GDI (Rab GDI-I or a isoform) to a resolution of 1.8 A. Rab GDI is organized into two domains, one of which shares structural similarity with FAD-dependent flavoproteins. The sequences that are conserved between Rab GDI and REP form a compact structure at the apex of the molecule. This domain is implicated in the interaction with Rab proteins and mutations in these sequences consistently cause a drastic reduction in the binding of Rab proteins and in the ability of Rab GDI to extract Rab proteins from membranes. Once the structure of a Rab protein is solved, it will be interesting to determine how Rab proteins can interact with Rab GDI in a nucleotide-dependent manner. Presumably, the effector region of Rab proteins is implicated in this interaction. The availability of the structure is expected to provide important insights into the molecular mechanism whereby Rab GDI interacts with Rab proteins and controls their association with the membrane.
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Takei K, McPherson PS, Schmid SL, De Camilli P: Tubular membrane invaginations coated by dynamin rings are induced by GTP-γS in nerve terminals. Nature 1995, 374:186-190.
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Walworth NC, Brennwald P, Kabcenell AK, Garrett M, Novick P: Hydrolysis of GTP by sec4 protein plays an important role in vesicular transport and is stimulated by a GTPase-activating protein in Saccharomyces cerevisiae. Mol Cell Biol 1992, 12:2017-2028.
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The GTPase Rab3a negatively controls calcium-dependent exocytosis in neuroendocrine cells
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Johannes L, Lledo P-M, Roa M, Vincent J-D, Henry J-P, Darchen F: The GTPase Rab3a negatively controls calcium-dependent exocytosis in neuroendocrine cells. EMBO J 1994, 13:2029-2037.
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GTPase activity of rab5 acts as a timer for endocytic membrane fusion
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32P]XTP hydrolysis by the protein bound on the endosome membrane were measured. The Rab5 mutant stimulated early endosome fusion in the presence of XTP but also in the presence of XTPγS, a nonhydrolyzable analogue of XTP, indicating that nucleotide triphosphate hydrolysis by Rab5 is not obligatory for early endosome fusion. Kinetics analysis indicated that nucleotide hydrolysis occurred in the presence but also in the absence of membrane fusion. This means that membrane-bound Rab5 undergoes futile cycles of XTP (and consequently GTP for wild-type Rab5) binding and hydrolysis. Binding of the Rab5 effector, rabaptin-5, however, stabilized Rab5 in the nucleotide triphosphate bound form. The authors propose that GTP hydrolysis by Rab5 acts as a timer that determines the frequency of membrane docking/fusion events in the early endocytic pathway. GTP hydrolysis by Rab5 would limit the activity of Rab5 so that endocytic transport occurs but excessive homotypic fusion between endosomes is avoided.
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Rybin, V.1
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Docking of yeast vacuoles is catalyzed by the Ras-like GTPase Ypt7p after symmetric priming by Sec18p (NSF)
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Mayer A, Wickner W: Docking of yeast vacuoles is catalyzed by the Ras-like GTPase Ypt7p after symmetric priming by Sec18p (NSF). J Cell Biol 1997, 136:307-317. Using biochemical and morphological assays, the authors of this paper analyzed the biochemical requirements in the docking and fusion of yeast vacuoles in vitro. Prior to docking both vacuole membranes require the activity of Sec17p (α-SNAP) and Sec18p (NSF). The small GTPase Ypt7p instead is required at the docking stage. This is the first demonstration that a member of the Rab family is directly involved in the docking process itself.
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Peter F, Nuoffer C, Pind SN, Balch WE: Guanine nucleotide dissociation inhibitor is essential for Rab1 function in budding from the endoplasmic reticulum and transport through the Golgi stack. J Cell Biol 1994, 126:1393-1406.
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Riederer MA, Soldati T, Shapiro AD, Lin J, Pfeffer S: Lysosome biogenesis requires Rab9 function and receptor recycling from endosomes to the trans Golgi network. J Cell Biol 1994, 125:573-582.
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Barlowe C, Orci L, Yeung T, Hosobuchi M, Hamamoto S, Salama N, Rexach MF, Ravazzola M, Amherdt M, Schekman R: COPII: a membrane coat formed by Sec proteins that drive vesicle budding from the endoplasmic reticulum. Cell 1994, 77:895-907.
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