Please note that eDoc will be permanently shut down in the first quarter of 2021!      Home News About Us Contact Contributors Disclaimer Privacy Policy Help FAQ
Home Search Quick Search Advanced Fulltext Browse Collections Persons My eDoc Session History Login Name: Password: Documentation Help Support Wiki Direct access to document ID:	Institute: MPI für biophysikalische Chemie     Collection: Ehemalige Abteilungen     Display Documents   history 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+... The scope and number of records on eDoc is subject to the collection policies defined by each institute - see "info" button in the collection browse view.