The membrane domain of vacuolar HATPase: a crucial player in neurotransmitter exocytotic release
Cellular and Molecular Life Sciences, ISSN: 1420-9071, Vol: 72, Issue: 13, Page: 2561-2573
2015
- 29Citations
- 55Captures
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
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Metrics Details
- Citations29
- Citation Indexes29
- 29
- CrossRef20
- Captures55
- Readers55
- 55
Review Description
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.
Bibliographic Details
http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=84930540208&origin=inward; http://dx.doi.org/10.1007/s00018-015-1886-2; http://www.ncbi.nlm.nih.gov/pubmed/25795337; http://link.springer.com/10.1007/s00018-015-1886-2; https://dx.doi.org/10.1007/s00018-015-1886-2; https://link.springer.com/article/10.1007/s00018-015-1886-2
Springer Science and Business Media LLC
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