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  The SNAREs vti1a and vti1b have distinct localization and SNARE complex partners

Kreykenbohm, V., Wenzel, D., Antonin, W., Atlachkine, V., & Fischer von Mollard, G. (2002). The SNAREs vti1a and vti1b have distinct localization and SNARE complex partners. European Journal of Cell Biology, 81(5), 273-280. Retrieved from http://www.sciencedirect.com/science?_ob=MImg&_imagekey=B7GJ2-4DPMB1J-77-1&_cdi=20194&_user=38661&_pii=S0171933504702307&_origin=search&_coverDate=05%2F01%2F2002&_sk=999189994&view=c&wchp=dGLbVlW-zSkzV&md5=a0c3856ae8237be42afdd774621621c3&ie=/sdarticle.pdf.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0012-F3DF-D Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0028-9CE8-0
Genre: Journal Article

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Kreykenbohm, V., Author
Wenzel, D.1, Author              
Antonin, W.2, Author              
Atlachkine, V., Author
Fischer von Mollard, G., Author
Affiliations:
1Facility for Electron Microscopy, MPI for biophysical chemistry, Max Planck Society, ou_578615              
2Department of Neurobiology, MPI for biophysical chemistry, Max Planck Society, ou_578595              

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Free keywords: SNARE proteins; membrane fusion; Golgi; TGN; endosome
 Abstract: Two mammalian proteins, vti1a and vti1b, are homologous to the yeast Q-SNARE Vti1p which is part of several SNARE complexes in different transport steps. In vitro experiments suggest distinct functions for vti1a and vti1b. Here we compared the subcellular localization of endogenous vti1a and vti1b by immunofluorescence and immuno-electron microscopy. Both proteins had a distinct but overlapping localization. vti1a was found predominantly on the Golgi and the TGN, vti1b mostly on tubules and vesicles in the TGN area and on endosomes. vti1a coimmunoprecipitated with VAMP-4, syntaxin 6, and syntaxin 16. These four SNAREs could assemble into a SNARE complex of conserved structure because one SNARE motif of each subgroup is present. vtila-beta, VAMP-4, syntaxin 6, and syntaxin 16 are coenriched with small synaptic vesicles and with clathrin- coated vesicles isolated from rat brain synaptosomes. Therefore, this SNARE complex may have a role in synaptic vesicle biogenesis or recycling.

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 Dates: 2002-05
 Publication Status: Published in print
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 Rev. Method: Peer
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Title: European Journal of Cell Biology
Source Genre: Journal
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Pages: - Volume / Issue: 81 (5) Sequence Number: - Start / End Page: 273 - 280 Identifier: -