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  Clathrin coat controls synaptic vesicle acidification by blocking vacuolar ATPase activity.

Farsi, Z., Gowrisankaran, S., Krunic, M., Rammner, B., Woehler, A., Lafer, E. M., et al. (2018). Clathrin coat controls synaptic vesicle acidification by blocking vacuolar ATPase activity. eLife, 7: e32569. doi:10.7554/eLife.32569.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0001-270F-4 Version Permalink: http://hdl.handle.net/21.11116/0000-0003-4F6E-B
Genre: Journal Article

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Farsi, Z.1, Author              
Gowrisankaran, S., Author
Krunic, M., Author
Rammner, B., Author
Woehler, A., Author
Lafer, E. M., Author
Mim, C., Author
Jahn, R.1, Author              
Milosevic, I., Author
Affiliations:
1Department of Neurobiology, MPI for biophysical chemistry, Max Planck Society, ou_578595              

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Free keywords: E. coli; human; mouse; neuroscience
 Abstract: Newly-formed synaptic vesicles (SVs) are rapidly acidified by vacuolar adenosine triphosphatases (vATPases), generating a proton electrochemical gradient that drives neurotransmitter loading. Clathrin-mediated endocytosis is needed for the formation of new SVs, yet it is unclear when endocytosed vesicles acidify and refill at the synapse. Here, we isolated clathrin-coated vesicles (CCVs) from mouse brain to measure their acidification directly at the single vesicle level. We observed that the ATP-induced acidification of CCVs was strikingly reduced in comparison to SVs. Remarkably, when the coat was removed from CCVs, uncoated vesicles regained ATP-dependent acidification, demonstrating that CCVs contain the functional vATPase, yet its function is inhibited by the clathrin coat. Considering the known structures of the vATPase and clathrin coat, we propose a model in which the formation of the coat surrounds the vATPase and blocks its activity. Such inhibition is likely fundamental for the proper timing of SV refilling.

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Language(s): eng - English
 Dates: 2018-04-13
 Publication Status: Published online
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 Rev. Method: Peer
 Identifiers: DOI: 10.7554/eLife.32569
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Title: eLife
Source Genre: Journal
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Pages: 18 Volume / Issue: 7 Sequence Number: e32569 Start / End Page: - Identifier: -