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The Journal of Neuroscience, August 1, 2000, 20(15):5724-5732

The SNARE Vti1a- Is Localized to Small Synaptic Vesicles and Participates in a Novel SNARE Complex

Wolfram Antonin², Dietmar Riedel², and Gabriele Fischer von Mollard¹

¹ Zentrum Biochemie und Molekulare Zellbiologie, Abteilung Biochemie II, Universität Göttingen, 37073 Göttingen, Germany, and ² Abteilung Neurobiologie, Max-Planck Institut für Biophysikalische Chemie, 37077 Göttingen, Germany

Specific soluble N-ethylmaleimide-sensitive factor attachment protein (SNAP) receptor (SNARE) proteins are required for different membrane transport steps. The SNARE Vti1a has been colocalized with Golgi markers and Vti1b with Golgi and the trans-Golgi network or endosomal markers in fibroblast cell lines. Here we study the distribution of Vti1a and Vti1b in brain. Vti1b was found in synaptic vesicles but was not enriched in this organelle. A brain-specific splice variant of Vti1a was identified that had an insertion of seven amino acid residues next to the putative SNARE-interacting helix. This Vti1a- was enriched in small synaptic vesicles and clathrin-coated vesicles isolated from nerve terminals. Vti1a- also copurified with the synaptic vesicle R-SNARE synaptobrevin during immunoisolation of synaptic vesicles and endosomes. Therefore, both synaptobrevin and Vti1a- are integral parts of synaptic vesicles throughout their life cycle. Vti1a- was part of a SNARE complex in nerve terminals, which bound N-ethylmaleimide-sensitive factor and -SNAP. This SNARE complex was different from the exocytic SNARE complex because Vti1a- was not coimmunoprecipitated with syntaxin 1 or SNAP-25. These data suggest that Vti1a- does not function in exocytosis but in a separate SNARE complex in a membrane fusion step during recycling or biogenesis of synaptic vesicles.

Key words: SNARE; synaptic vesicle; clathrin-coated vesicle; endosome; Vti1; nerve terminal; membrane traffic

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Copyright © 2000 Society for Neuroscience  0270-6474/00/20155724-09$05.00/0

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