A. Hurtado-lorenzo, M. Skinner, J. El-annan, M. Futai, G. H. Sun-wada et al., V-ATPase interacts with ARNO and Arf6 in early endosomes and regulates the protein degradative pathway, Nature cell biology, vol.8, issue.2, pp.124-136, 2006.

K. Yokoyama, M. Nakano, H. Imamura, M. Yoshida, and M. Tamakoshi, Rotation of the proteolipid ring in the V-ATPase, J Biol Chem, vol.278, issue.27, pp.24255-24258, 2003.

M. Toei, R. Saum, and M. Forgac, Regulation and Isoform Function of the V-ATPases, Biochemistry, vol.49, issue.23, pp.4715-4723, 2010.

P. R. Hiesinger, A. Fayyazuddin, S. Q. Mehta, T. Rosenmund, K. L. Schulze et al., The v-ATPase V(0) Subunit a1 Is Required for a Late Step in Synaptic Vesicle Exocytosis in Drosophila, Cell, vol.121, issue.4, pp.607-620, 2005.

S. Poea-guyon, M. R. Ammar, M. Erard, M. Amar, A. W. Moreau et al., The V-ATPase membrane domain is a sensor of granular pH that controls the exocytotic machinery, J Cell Biol, vol.203, issue.2, pp.283-298, 2013.
URL : https://hal.archives-ouvertes.fr/hal-00913450

D. Giovanni, J. Boudkkazi, S. Mochida, S. Bialowas, A. Samari et al., El Far O (2010) V-ATPase membrane sector associates with synaptobrevin to modulate neurotransmitter release, Neuron, vol.67, issue.2, pp.268-279

O. El-far and M. Seagar, A role for V-ATPase subunits in synaptic vesicle fusion?, J Neurochem, vol.117, issue.4, pp.603-612, 2011.
URL : https://hal.archives-ouvertes.fr/inserm-00581211

K. Hayami, T. Noumi, H. Inoue, G. Sun-wada, T. Yoshimizu et al., The murine genome contains one functional gene and two pseudogenes coding for the 16 kDa proteolipid subunit of vacuolar H(+)-ATPase, Gene, vol.273, issue.2, pp.199-206, 2001.

G. Sun-wada, Y. Murata, A. Yamamoto, H. Kanazawa, Y. Wada et al., Acidic endomembrane organelles are required for mouse postimplantation development, Dev Biol, vol.228, issue.2, pp.315-325, 2000.

H. Inoue, T. Noumi, M. Nagata, H. Murakami, and H. Kanazawa, Targeted disruption of the gene encoding the proteolipid subunit of mouse vacuolar H(+)-ATPase leads to early embryonic lethality, Biochim Biophys Acta, vol.1413, issue.3, pp.130-138, 1999.

O. Tour, R. M. Meijer, D. A. Zacharias, S. R. Adams, and R. Y. Tsien, Genetically targeted chromophoreassisted light inactivation, Nat Biotechnol, vol.21, issue.12, pp.1505-1508, 2003.

M. Ochsner, Photophysical and photobiological processes in the photodynamic therapy of tumours, J Photochem Photobiol B, vol.39, issue.1, pp.1-18, 1997.

Y. Sano, W. Watanabe, and S. Matsunaga, Chromophore-assisted laser inactivation -towards a spatiotemporal-functional analysis of proteins, and the ablation of chromatin, organelle and cell function, J Cell Sci, vol.127, issue.8, pp.1621-1629, 2014.

P. Yan, Y. Xiong, B. Chen, S. Negash, T. C. Squier et al., Fluorophore-assisted light inactivation of calmodulin involves singlet-oxygen mediated cross-linking and methionine oxidation, Biochemistry, vol.45, issue.15, pp.4736-4748, 2006.

K. W. Marek and G. W. Davis, Transgenically encoded protein photoinactivation (FlAsH-FALI): acute inactivation of synaptotagmin I, Neuron, vol.36, issue.5, pp.805-813, 2002.

N. Morel, S. Poea-guyon, M. R. Ammar, and N. Vitale, V-ATPase is a pH sensor controlling vesicular membrane fusion, 2014.
URL : https://hal.archives-ouvertes.fr/hal-01101322

, Med Sci (Paris), pp.631-633

K. L. Meerbrey, G. Hu, J. D. Kessler, K. Roarty, M. Z. Li et al., Elledge SJ The pINDUCER lentiviral toolkit for inducible RNA interference in vitro and in vivo, Proceedings of the National Academy of Sciences of the United States of America, vol.108, issue.9, pp.3665-3670

D. Debanne, S. Boudkkazi, E. Campanac, R. H. Cudmore, P. Giraud et al., Paired-recordings from synaptically coupled cortical and hippocampal neurons in acute and cultured brain slices, Nat Protoc, vol.3, issue.10, pp.1559-1568, 2008.
URL : https://hal.archives-ouvertes.fr/inserm-00484944

J. Y. Lin, S. B. Sann, K. Zhou, S. Nabavi, C. D. Proulx et al., Optogenetic inhibition of synaptic release with chromophore-assisted light inactivation (CALI), Neuron, vol.79, issue.2, pp.241-253, 2013.

K. L. Meerbrey, G. Hu, J. D. Kessler, K. Roarty, M. Z. Li et al., The pINDUCER lentiviral toolkit for inducible RNA interference in vitro and in vivo, Proc Natl Acad Sci U S A, vol.108, issue.9, pp.3665-3670, 2011.

M. Israel, N. Morel, B. Lesbats, S. Birman, and R. Manaranche, Purification of a presynaptic membrane protein that mediates a calcium-dependent translocation of acetylcholine, Proc Natl Acad Sci U S A, vol.83, issue.23, pp.9226-9230, 1986.

J. Falk-vairant, F. M. Meunier, B. Lesbats, P. Correges, L. Eder-colli et al., Cell lines expressing an acetylcholine release mechanism; correction of a releasedeficient cell by mediatophore transfection, J Neurosci Res, vol.45, issue.3, p.1, 1996.

J. Falk-vairant, P. Correges, L. Eder-colli, N. Salem, E. Roulet et al., Quantal acetylcholine release induced by mediatophore transfection, Proc Natl Acad Sci U S A, vol.93, issue.11, pp.5203-5207, 1996.

J. Falk-vairant, P. Correges, L. Eder-colli, N. Salem, F. M. Meunier et al., Evoked acetylcholine release expressed in neuroblastoma cells by transfection of mediatophore cDNA, J Neurochem, vol.66, issue.3, pp.1322-1325, 1996.

C. Peters, M. J. Bayer, S. Buhler, J. S. Andersen, M. Mann et al., Trans-complex formation by proteolipid channels in the terminal phase of membrane fusion, Nature, vol.409, issue.6820, pp.581-588, 2001.

M. J. Bayer, C. Reese, S. Buhler, C. Peters, and A. Mayer, Vacuole membrane fusion: V0 functions after trans-SNARE pairing and is coupled to the Ca2+-releasing channel, J Cell Biol, vol.162, issue.2, pp.211-222, 2003.

P. R. Hiesinger, A. Fayyazuddin, S. Q. Mehta, T. Rosenmund, K. L. Schulze et al., The v-ATPase V0 subunit a1 is required for a late step in synaptic vesicle exocytosis in Drosophila, Cell, vol.121, issue.4, pp.607-620, 2005.

D. Wang, D. Epstein, O. Khalaf, S. Srinivasan, W. R. Williamson et al., Ca2+-Calmodulin regulates SNARE assembly and spontaneous neurotransmitter release via v-ATPase subunit V0a1, J Cell Biol, vol.205, issue.1, pp.21-31, 2014.

G. H. Sun-wada, T. Toyomura, Y. Murata, A. Yamamoto, M. Futai et al., The a3 isoform of V-ATPase regulates insulin secretion from pancreatic beta-cells, J Cell Sci, vol.119, pp.4531-4540, 2006.

F. Peri and C. Nusslein-volhard, Live imaging of neuronal degradation by microglia reveals a role for v0-ATPase a1 in phagosomal fusion in vivo, Cell, vol.133, issue.5, pp.916-927, 2008.

S. Liegeois, A. Benedetto, J. M. Garnier, Y. Schwab, and M. Labouesse, The V0-ATPase mediates apical secretion of exosomes containing Hedgehog-related proteins in Caenorhabditis elegans, J Cell Biol, vol.173, issue.6, pp.949-961, 2006.
URL : https://hal.archives-ouvertes.fr/hal-00188024

S. Poea-guyon, M. Amar, P. Fossier, and N. Morel, Alternative splicing controls neuronal expression of v-ATPase subunit a1 and sorting to nerve terminals, J Biol Chem, vol.281, issue.25, pp.17164-17172, 2006.
URL : https://hal.archives-ouvertes.fr/hal-00103592

M. R. Baldwin and J. T. Barbieri, Association of botulinum neurotoxin serotypes a and B with synaptic vesicle protein complexes, Biochemistry, vol.46, issue.11, pp.3200-3210, 2007.

T. Galli, P. S. Mcpherson, D. Camilli, and P. , The V0 sector of the V-ATPase, synaptobrevin, and synaptophysin are associated on synaptic vesicles in a Triton X-100-resistant, freeze-thawing sensitive, complex, J Biol Chem, vol.271, issue.4, pp.2193-2198, 1996.

H. Y. Sroussi, J. Berline, and J. M. Palefsky, Oxidation of methionine 63 and 83 regulates the effect of S100A9 on the migration of neutrophils in vitro, J Leukoc Biol, vol.81, issue.3, pp.818-824, 2007.

P. C. Jones, M. A. Harrison, Y. I. Kim, M. E. Finbow, and J. Findlay, The first putative transmembrane helix of the 16 kDa proteolipid lines a pore in the V<sub>o</sub> sector of the vacuolar H<sup>+</sup>-ATPase, Biochemical Journal, vol.312, issue.3, pp.739-747, 1995.

Z. Zhang, K. T. Nguyen, E. F. Barrett, G. David, and . Vesicular, ATPase Inserted into the Plasma Membrane of Motor Terminals by Exocytosis Alkalinizes Cytosolic pH and Facilitates Endocytosis, Neuron, vol.68, issue.6, pp.1097-1108