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          Institute: MPI für biophysikalische Chemie     Collection: Ehemalige Abteilungen     Display Documents



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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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