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, Suzanne R. Pfeffer

Research output: Contribution to journalArticlepeer-review

102 Citations (Scopus)

Abstract

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 (TGN) 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 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.

Original languageEnglish
Pages (from-to)4353-4363
Number of pages11
JournalMolecular Biology of the Cell
Volume17
Issue number10
DOIs
Publication statusPublished - Oct 2006

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