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• W2114736119 abstract "AbstractRab/Ypt GTPases are key regulators of membrane trafficking and together with SNARE proteins mediate selective fusion of vesicles with target compartments. A family of GTPase-activating enzymes (GAPs) specific for Rab/Ypt GTPases has been discovered, but little is known about their function and substrate specificity in vivo. Here we show that the GAP activity of Gyp1p, a yeast member of this family, is specifically required for recycling of the SNARE Snc1p and the membrane dye FM4-64, implying that inactivation of a Rab/Ypt GTPase may be necessary for recycling of membrane material. Interestingly, recycling of GFP-Snc1p in gyp1Δ cells is partially restored by reducing the activity of Ypt1p. Moreover, GFP-Snc1p accumulated intracellularly in wild-type cells expressing a GTP-locked, mutant form of Ypt1p (Ypt1p-Q67L), suggesting that GTP hydrolysis of Ypt1p is essential for recycling. Ypt6p is known to be required for the fusion of recycling vesicles to the late Golgi compartment. Interestingly, the deletions of GYP1 and YPT6 were synthetic lethal, raising the possibility that at least two distinct pathways are involved in recycling of membrane material. We thank P. Novick, N. Segev, H. Pelham, H. Riezman, and S. Alberts for plasmids and yeast strains. We are grateful to Monika Gersbach for expert technical assistance, C. Boone's laboratory for help in the synthetic-lethal analysis, Nicolas Pagé for robot expertise, members of the Haguenauer-Tsapis and Peter groups for stimulating discussion, and Marc Sohrmann for critical reading of the manuscript.J.-M.G. is supported by the CNRS, and work in the M.P. laboratory is supported by the Swiss National Science Foundation, the Functional Genome Center Zurich, and the ETH/Zurich." @default.
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• W2114736119 date "2004-05-01" @default.
• W2114736119 modified "2023-10-08" @default.
• W2114736119 title "The GTPase-Activating Enzyme Gyp1p Is Required for Recycling of Internalized Membrane Material by Inactivation of the Rab/Ypt GTPase Ypt1p" @default.
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• W2114736119 doi "https://doi.org/10.1128/mcb.24.9.3815-3826.2004" @default.
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