Rama, S; Boumedine-Guignon, N; Sangiardi, M; Youssouf, F; Maulet, Y; Lévêque, C; Belghazi, M; ... El Far, O; + view all Rama, S; Boumedine-Guignon, N; Sangiardi, M; Youssouf, F; Maulet, Y; Lévêque, C; Belghazi, M; Seagar, M; Debanne, D; El Far, O; - view fewer (2019) Chromophore-Assisted Light Inactivation of the V-ATPase V0c Subunit Inhibits Neurotransmitter Release Downstream of Synaptic Vesicle Acidification. Molecular Neurobiology , 56 (5) pp. 3591-3602. 10.1007/s12035-018-1324-1.

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Abstract

Synaptic vesicle proton V-ATPase is an essential component in synaptic vesicle function. Active acidification of synaptic vesicles, triggered by the V-ATPase, is necessary for neurotransmitter storage. Independently from its proton transport activity, an additional important function of the membrane-embedded sector of the V-ATPase has been uncovered over recent years. Subunits a and c of the membrane sector of this multi-molecular complex have been shown to interact with SNARE proteins and to be involved in modulating neurotransmitter release. The c-subunit interacts with the v-SNARE VAMP2 and facilitates neurotransmission. In this study, we used chromophore-assisted light inactivation and monitored the consequences on neurotransmission on line in CA3 pyramidal neurons. We show that V-ATPase c-subunit V0c is a key element in modulating neurotransmission and that its specific inactivation rapidly inhibited neurotransmission.

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