ARF-GAP-mediated interaction between the ER-Golgi v-SNAREs and the COPI coat.

Friedrich Miescher Laboratory, Max Planck Society, D-72076 Tuebingen, Germany.
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.
Mesh Terms:
ADP-Ribosylation Factor 1, ADP-Ribosylation Factors, COP-Coated Vesicles, Coat Protein Complex I, DNA-Binding Proteins, Endoplasmic Reticulum, Fungal Proteins, GTPase-Activating Proteins, Intracellular Membranes, Membrane Proteins, Microsomes, Protein Binding, Recombinant Fusion Proteins, SNARE Proteins, Saccharomyces cerevisiae Proteins, Vesicular Transport Proteins
J. Cell Biol. Apr. 29, 2002; 157(3);395-404 [PUBMED:11970962]
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