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

http://www.ncbi.nlm.nih.gov/pubmed/11970962

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.

Pubmed ID: 11970962 RIS Download

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

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