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¹ Friedrich Miescher Laboratory, Max Planck Society, D-72076 Tübingen, Germany
² Max Planck Institute for Biophysical Chemistry, Department of Molecular Genetics, D-37070 Göttingen, Germany
³ University of Cambridge, Wellcome Trust Centre for Molecular Mechanisms in Disease, Cambridge CB2 2XY, United Kingdom

Address correspondence to Anne Spang, Friedrich-Miescher-Laboratorium, Spemannstrasse 39, D-72076 Tübingen, Germany. Tel.: 49-7071-601-840. Fax: 49-7071-601-455. E-mail: anne.spang{at}tuebingen.mpg.de

In eukaryotic cells, secretion is achieved by vesicular transport. Fusion of such vesicles with the correct target compartment relies on SNARE proteins on both vesicle (v-SNARE) and the target membranes (t-SNARE). At present it is not clear how v-SNAREs are incorporated into transport vesicles. Here, we show that binding of ADP-ribosylation factor (ARF)–GTPase-activating protein (GAP) to ER-Golgi v-SNAREs is an essential step for recruitment of Arf1p and coatomer, proteins that together form the COPI coat. ARF-GAP acts catalytically to recruit COPI components. Inclusion of v-SNAREs into COPI vesicles could be mediated by direct interaction with the coat. The mechanisms by which v-SNAREs interact with COPI and COPII coat proteins seem to be different and may play a key role in determining specificity in vesicle budding.

Key Words: Arf; ARF-GAP; COPI; ER-Golgi SNAREs; protein transport

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