The membrane domain of vacuolar H(+)ATPase: a crucial player in neurotransmitter exocytotic release

Cellular and Molecular Life Sciences : CMLS
Nicolas Morel, Sandrine Poëa-Guyon

Abstract

V-ATPases are multimeric enzymes made of two sectors, a V1 catalytic domain and a V0 membrane domain. They accumulate protons in various intracellular organelles. Acidification of synaptic vesicles by V-ATPase energizes the accumulation of neurotransmitters in these storage organelles and is therefore required for efficient synaptic transmission. In addition to this well-accepted role, functional studies have unraveled additional hidden roles of V0 in neurotransmitter exocytosis that are independent of the transport of protons. V0 interacts with SNAREs and calmodulin, and perturbing these interactions affects neurotransmitter release. Here, we discuss these data in relation with previous results obtained in reconstituted membranes and on yeast vacuole fusion. We propose that V0 could be a sensor of intra-vesicular pH that controls the exocytotic machinery, probably regulating SNARE complex assembly during the synaptic vesicle priming step, and that, during the membrane fusion step, V0 might favor lipid mixing and fusion pore stability.

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Citations

Oct 9, 2015·Translational Neurodegeneration·Yong-Bo HuGang Wang
Apr 22, 2016·Scientific Reports·Sergio Couoh-CardelLiviu Movileanu
Mar 2, 2017·Protein Science : a Publication of the Protein Society·Rebecca A OotStephan Wilkens
Jul 9, 2020·PloS One·Francisco Vidal-DomènechBelén Ramos
Aug 27, 2018·Histochemistry and Cell Biology·Nikhil R YedullaBhanu P Jena
Dec 21, 2020·Transfusion and Apheresis Science : Official Journal of the World Apheresis Association : Official Journal of the European Society for Haemapheresis·Li CaiWenbiao Liang
May 3, 2021·Progress in Neurobiology·Eric J R JansenGerard J M Martens
May 15, 2021·Nature Reviews. Disease Primers·David S KnopmanDavid T Jones

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