caa a22 4500 606177396 CHVBK 20210128100752.0 cr unu---uuuuu 210128e20150701xx s 000 0 eng 10.1007/s00018-015-1886-2 doi (NATIONALLICENCE)springer-10.1007/s00018-015-1886-2 The membrane domain of vacuolar H+ATPase: a crucial player in neurotransmitter exocytotic release [Elektronische Daten] [Nicolas Morel, Sandrine Poëa-Guyon] 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. Springer Basel, 2015 V-ATPase nationallicence Neurotransmitter release nationallicence Exocytosis nationallicence SNARE nationallicence Fusion pore nationallicence Calmodulin nationallicence V-ATPase : Vacuolar-type H+ATPase nationallicence V0 : V-ATPase membrane domain nationallicence V1 : V-ATPase catalytic domain nationallicence ACh : Acetylcholine nationallicence SNARE : Soluble NSF attachment receptor proteins nationallicence CALI : Chromophore-assisted light inactivation nationallicence ARNO : ADP ribosylation factor nucleotide-binding site opener nationallicence Arf6 : ADP-ribosylation factor-6 nationallicence Morel Nicolas Centre de Neurosciences Paris-Sud, Centre National de la Recherche Scientifique, Unité Mixte de Recherche 8195 and Université Paris-Sud, 91405, Orsay, France aut Poëa-Guyon Sandrine Centre de Neurosciences Paris-Sud, Centre National de la Recherche Scientifique, Unité Mixte de Recherche 8195 and Université Paris-Sud, 91405, Orsay, France aut Cellular and Molecular Life Sciences Springer Basel 72/13(2015-07-01), 2561-2573 1420-682X 72:13<2561 2015 72 18 https://doi.org/10.1007/s00018-015-1886-2 text/html Onlinezugriff via DOI BK010053 XK010053 XK010000 Metadata rights reserved Springer special CC-BY-NC licence nationallicence 1 review-article jats NATIONALLICENCE NATIONALLICENCE NL-springer NATIONALLICENCE 856 40 https://doi.org/10.1007/s00018-015-1886-2 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Morel Nicolas Centre de Neurosciences Paris-Sud, Centre National de la Recherche Scientifique, Unité Mixte de Recherche 8195 and Université Paris-Sud, 91405, Orsay, France aut NATIONALLICENCE 700 1- Poëa-Guyon Sandrine Centre de Neurosciences Paris-Sud, Centre National de la Recherche Scientifique, Unité Mixte de Recherche 8195 and Université Paris-Sud, 91405, Orsay, France aut NATIONALLICENCE 773 0- Cellular and Molecular Life Sciences Springer Basel 72/13(2015-07-01), 2561-2573 1420-682X 72:13<2561 2015 72 18