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A more recent version of this article appeared on April 1, 2006
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Submitted on November 2, 2005
Revised on January 12, 2006
Accepted on January 20, 2006
*Centre for Molecular Medicine and Therapeutics, Child and Family Research Institute, Departments of Medical Genetics and Biochemistry and Molecular Biology, University of British Columbia, Vancouver, British Columbia V5Z 4H4, Canada; Department of Biology and Integrated Imaging Center, Johns Hopkins University, Baltimore, MD 21218
Monitoring Editor: Sean Munro
Tethering complexes contribute to the specificity of membrane fusion by recognizing organelle features on both donor and acceptor membranes. The Golgi Associated Retrograde Protein (GARP) tethering complex is required for retrograde traffic from both early and late endosomes to the trans-Golgi network (TGN), presenting a paradox as to how a single complex can interact specifically with vesicles from multiple upstream compartments. We have found that a subunit of the GARP complex, Vps54, can be separated into N-terminal and C-terminal regions that have different functions. Whereas the N-terminus of Vps54 is important for GARP complex assembly and stability, a conserved C-terminal domain mediates localization to an early endocytic compartment. Mutation of this C-terminal domain has no effect on retrograde transport from late endosomes. However, a specific defect in retrieval of Snc1 from early endosomes is observed when recycling from late endosomes to the Golgi is blocked. These data suggest that separate domains recruit tethering complexes to different upstream compartments to regulate individual trafficking pathways.
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