The v-ATPase V0 subunit a1 is required for a late step in synaptic vesicle exocytosis in Drosophila.

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Hiesinger, P.R., Fayyazuddin, A., Mehta, S.Q., Rosenmund, T., Schulze, K.L., Zhai, R.G., Verstreken, P., Cao, Y., Zhou, Y., Kunz, J., and Bellen, H.J. – 2005

The V(0) complex forms the proteolipid pore of an ATPase that acidifies vesicles. In addition, an independent function in membrane fusion has been proposed largely based on yeast vacuolar fusion experiments. We have isolated mutations in the largest V(0) component vha100-1 in flies in an unbiased genetic screen for synaptic malfunction. The protein is only required in neurons, colocalizes with markers for synaptic vesicles as well as active zones, and interacts with t-SNAREs. Loss of vha100-1 leads to vesicle accumulation in synaptic terminals, suggesting a deficit in release. The amplitude of spontaneous release events and release with hypertonic stimulation indicate normal levels of neurotransmitter loading, yet mutant embryos display severe defects in evoked synaptic transmission and FM1-43 uptake. Our data suggest that Vha100-1 functions downstream of SNAREs in synaptic vesicle fusion.

Titel
The v-ATPase V0 subunit a1 is required for a late step in synaptic vesicle exocytosis in Drosophila.
Verfasser
Hiesinger, P.R., Fayyazuddin, A., Mehta, S.Q., Rosenmund, T., Schulze, K.L., Zhai, R.G., Verstreken, P., Cao, Y., Zhou, Y., Kunz, J., and Bellen, H.J.
Verlag
Cell Press
Datum
2005-05-20
Kennung
doi: 10.1016/j.cell.2005.03.012
Erschienen in
Cell 121(4): 607-20
Sprache
eng
Art
Text
Rechte
© 2005 Elsevier Inc. Published by Elsevier Inc.
NeuroCure