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

ABSTRACT: 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.

SUBMITTER: Hiesinger PR 

PROVIDER: S-EPMC3351201 | biostudies-literature | 2005 May

REPOSITORIES: biostudies-literature

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

Hiesinger P Robin PR   Fayyazuddin Amir A   Mehta Sunil Q SQ   Rosenmund Tanja T   Schulze Karen L KL   Zhai R Grace RG   Verstreken Patrik P   Cao Yu Y   Zhou Yi Y   Kunz Jeannette J   Bellen Hugo J HJ  

Cell 20050501 4

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 le  ...[more]

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