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Published online January 14, 2008
doi:10.1083/jcb.200707136
The Journal of Cell Biology, Vol. 180, No. 1, 159-172
The Rockefeller University Press, 0021-9525 $30.00
© 2008 Ganley et al.
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Article

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

Ian G. Ganley, Eric Espinosa, and Suzanne R. Pfeffer

Department of Biochemistry, Stanford University School of Medicine, Stanford, CA 94305

Correspondence to Suzanne R. Pfeffer: pfeffer{at}stanford.edu

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

Abbreviations used in this paper: CD, cation dependent; CI, cation independent; EEA1, early endosome antigen 1; MPR, mannose 6-phosphate receptor; STX, syntaxin.


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