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Volume 272, Number 44, Issue of October 31, 1997 pp. 27737-27744
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

A Novel Assay Reveals a Role for Soluble N-Ethylmaleimide-sensitive Fusion Attachment Protein in Mannose 6-Phosphate Receptor Transport from Endosomes to the Trans Golgi Network

(Received for publication, June 11, 1997, and in revised form, September 2, 1997)

From the Department of Biochemistry, Stanford University School of Medicine, Stanford, California 94305-5307

Soluble N-ethylmaleimide-sensitive fusion protein (NSF) attachment protein (-SNAP) is a soluble protein that enables the NSF ATPase to associate with membranes and facilitate membrane trafficking events. Although NSF and -SNAP have been shown to be required for many membrane transport processes, their role in the transport of mannose 6-phosphate receptors from endosomes to the trans Golgi network was not established. We present here a novel in vitro assay that monitors the transport of cation-dependent mannose 6-phosphate receptors between endosomes and the trans Golgi network. The assay relies on the trans Golgi network localization of tyrosine sulfotransferase and monitors transport of mannose 6-phosphate receptors engineered to contain a consensus sequence for modification by this enzyme. Using this new assay we show that -SNAP strongly stimulates transport in reactions containing limiting amounts of cytosol. Together with -SNAP, NSF can increase the extent of transport. These data show that -SNAP, a soluble component of the SNAP receptor machinery, facilitates transport from endosomes to the trans Golgi network.

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