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ID:
16483.0,
MPI für biophysikalische Chemie / Ehemalige Abteilungen |
ARF-GAP-mediated interaction between the ER-Golgi v-SNAREs and the COPI coat |
Authors: | Rein, U.; Andag, U.; Duden, R.; Schmitt, H. D.; Spang, A. | Language: | English | Date of Publication (YYYY-MM-DD): | 2002-04-29 | Title of Journal: | Journal of Cell Biology | Volume: | 157 | Issue / Number: | 3 | Start Page: | 395 | End Page: | 404 | Review Status: | Peer-review | Audience: | Not Specified | Abstract / Description: | 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. | Free Keywords: | Arf; ARF-GAP; COPI; ER-Golgi SNAREs; protein transport | Comment of the Author/Creator: | Date: 2002, APR 29 | External Publication Status: | published | Document Type: | Article |
Communicated by: | N. N. | Affiliations: | MPI für biophysikalische Chemie/AG Hans-Dieter Schmitt
| External Affiliations: | Friedrich Miescher Lab, Max Planck Soc, D-72076 Tubingen, Germany; Univ Cambridge, Wellcome Trust Ctr Mol Mechanisms Dis, Cambridge CB2 2XY, England
| Identifiers: | URL:http://jcb.rupress.org/content/157/3/395.full.pdf+... | |
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