A syntaxin 10–SNARE complex distinguishes two distinct transport routes from endosomes to the trans-Golgi in human cells

• DOI: 10.1083/jcb.200707136
• Publication Date: 2008-01-14T22:27:22Z
• Authors: Ian G. Ganley; Eric Espinosa; Suzanne R. Pfeffer
• Keywords: Rab; Transport protein; Vesicular Transport Proteins; Vesicular Transport Proteins

Mannose 6-phosphate receptors (MPRs) are transported from endosomes to the Golgi after delivering lysosomal enzymes endocytic pathway. This process requires Rab9 guanosine triphosphatase (GTPase) and putative tether GCC185. We show in human cells that a soluble NSF attachment protein receptor (SNARE) complex comprised of syntaxin 10 (STX10), STX16, Vti1a, VAMP3 is required for this MPR transport but not STX6-dependent TGN46 or cholera toxin early Golgi. Depletion STX10 leads missorting hypersecretion hexosaminidase. Mouse rat lack and, thus, must use different target membrane SNARE process. GCC185 binds directly STX16 competed by Rab6. These data support model which helps Rab9-bearing vesicles deliver their cargo trans-Golgi suggest Rab GTPases can regulate SNARE-tether interactions. Importantly, our provide clear molecular distinction between MPRs trans-Golgi.