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MBC in Press, published online ahead of print August 2, 2006
Mol. Biol. Cell 10.1091/mbc.E06-02-0153

A more recent version of this article appeared on October 1, 2006
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Submitted on February 22, 2006
Revised on July 21, 2006
Accepted on July 24, 2006

A Functional Role for the GCC185 Golgin in Mannose 6-Phosphate Receptor Recycling

Jonathan V. Reddy, Alondra Schweizer Burguete, Khambhampaty Sridevi, Ian G. Ganley, Ryan M. Nottingham, and Suzanne R. Pfeffer

Department of Biochemistry, Stanford University School of Medicine, Stanford, CA 94305-5307

Monitoring Editor: Adam Linstedt

Mannose 6-phosphate receptors (MPRs) deliver newly synthesized lysosomal enzymes to endosomes and then recycle to the Golgi. MPR recycling requires Rab9 GTPase; Rab9 recruits the cytosolic adaptor, TIP47 and enhances its ability to bind to MPR cytoplasmic domains during transport vesicle formation. Rab9-bearing vesicles then fuse with the trans Golgi network in living cells, but nothing is known about how these vesicles identify and dock with their target. We show here that GCC185, a member of the Golgin family of putative tethering proteins, is a Rab9 effector that is required for MPR recycling from endosomes to the trans Golgi network (TGN) in living cells and in vitro. GCC185 does not rely on Rab9 for its TGN localization; depletion of GCC185 slightly alters the Golgi ribbon but does not interfere with Golgi function. Loss of GCC185 triggers enhanced degradation of mannose 6-phosphate receptors and enhanced secretion of hexosaminidase. These data assign a specific pathway to an interesting, TGN-localized protein, and suggest that GCC185 may participate in the docking of late-endosome-derived, Rab9-bearing transport vesicles at the TGN.

Address correspondence to: Suzanne R. Pfeffer (pfeffer{at}stanford.edu)




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