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

Rein, U., Andag, U., Duden, R., Schmitt, H. D., & Spang, A. (2002). ARF-GAP-mediated interaction between the ER-Golgi v-SNAREs and the COPI coat. Journal of Cell Biology, 157(3), 395-404. Retrieved from http://jcb.rupress.org/content/157/3/395.full.pdf+html.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0012-F3E9-6 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0028-9CED-6
Genre: Journal Article

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599643.pdf (Publisher version), 468KB
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 Creators:
Rein, U., Author
Andag, U., Author
Duden, R., Author
Schmitt, H. D.1, Author              
Spang, A., Author
Affiliations:
1Research Group of Membrane Transport in Yeast, MPI for biophysical chemistry, Max Planck Society, ou_578597              

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Free keywords: Arf; ARF-GAP; COPI; ER-Golgi SNAREs; protein transport
 Abstract: 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.

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Language(s): eng - English
 Dates: 2002-04-29
 Publication Status: Published in print
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 Table of Contents: -
 Rev. Method: Peer
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Title: Journal of Cell Biology
Source Genre: Journal
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Pages: - Volume / Issue: 157 (3) Sequence Number: - Start / End Page: 395 - 404 Identifier: -