AI Article Synopsis
- Vacuolar ATPase (V-ATPase) is a crucial enzyme for acidifying intracellular compartments, with ATP6V0C as a key subunit in its structure.
- This study focused on the neuron-specific expression of atp6v0c2, a new isoform of the V-ATPase c-subunit in developing zebrafish CNS, revealing its expression in certain CNS neurons shortly after they become post-mitotic.
- Findings indicate that ATP6V0C2 protein associates with presynaptic vesicle marker SV2, linking it to neurotransmitter handling, and loss-of-function tests show its role in regulating neuronal excitability.
Article Abstract
Vacuolar ATPase (V-ATPase) is a multi-subunit enzyme that plays an important role in the acidification of a variety of intracellular compartments. ATP6V0C is subunit c of the V(0) domain that forms the proteolipid pore of the enzyme. In the present study, we investigated the neuron-specific expression of atp6v0c2, a novel isoform of the V-ATPase c-subunit, during the development of the zebrafish CNS. Zebrafish atp6v0c2 was isolated from a genome-wide analysis of the zebrafish mib(ta52b) mutant designed to identify genes differentially regulated by Notch signaling. Whole-mount in situ hybridization revealed that atp6v0c2 is expressed in a subset of CNS neurons beginning several hours after the emergence of post-mitotic neurons. The ATP6V0C2 protein is co-localized with the presynaptic vesicle marker, SV2, suggesting that it is involved in neurotransmitter storage and/or secretion in neurons. In addition, the loss-of-function experiment suggests that ATP6V0C2 is involved in the control of neuronal excitability.
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| http://dx.doi.org/10.1002/dvdy.22383 | DOI Listing |
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