Link to bioRxiv paper:
http://biorxiv.org/cgi/content/short/2023.01.31.526435v1?rss=1

Authors: LEVEQUE, C., MAULET, Y., WANG, Q., RAME, M., MOCHIDA, S., SANGIARDI, M., YOUSSOUF, F., IBORRA, C., SEAGAR, M., VITALE, N., EL FAR, O.

Abstract:
V-ATPase is an important factor in synaptic vesicle acidification and is implicated in synaptic transmission. Rotation of the extra-membranous V1 sector drives proton transfer through the membrane-embedded multi-subunit V0 sector of the V-ATPase. Intra-vesicular protons are then used to drive neurotransmitter uptake by synaptic vesicles. V0a and V0c, two membrane subunits of the V0 sector have been shown to interact with SNARE proteins and their photo-inactivation rapidly impairs synaptic transmission. V0d, a soluble subunit of the V0 sector strongly interacts with its membrane embedded subunits and is crucial for the canonic proton transfer activity of the V-ATPase. Our investigations show that the loop 1.2 of V0c interacts with complexin, a major partner of the SNARE machinery and that V0d1 binding to V0c inhibits this interaction, as well as V0c association with SNARE complex. Injection of recombinant V0d1 in rat superior cervical ganglion neurons rapidly reduced neurotransmission. In chromaffin cells, V0d1 overexpression and V0c silencing modified in a comparable manner several parameters of unitary exocytotic events. Our data suggest that V0c subunit promotes exocytosis via interactions with complexin and SNAREs and that this activity can be antagonized by exogenous V0d.

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