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

Farsi, Z.; Gowrisankaran, S.; Krunic, M.; Rammner, B.; woehler, A.; Lafer, E. M.; Mim, C.; Jahn, R.; Milosevic, I.

doi:10.1016/j.bpj.2017.11.1611

Item

ITEM ACTIONSEXPORT

Add to Basket

Local TagsRelease HistoryDetailsSummary

Released

Conference Paper

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

MPS-Authors

/persons/resource/persons59362

Farsi, Z.
Department of Neurobiology, MPI for biophysical chemistry, Max Planck Society;

/persons/resource/persons15266

Jahn, R.
Department of Neurobiology, MPI for biophysical chemistry, Max Planck Society;

External Resource

No external resources are shared

Fulltext (restricted access)

There are currently no full texts shared for your IP range.

Fulltext (public)

2581643.pdf
(Publisher version), 44KB

Supplementary Material (public)

There is no public supplementary material available

Citation

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. Biophysical Journal, 114(3), 280a-280a. doi:10.1016/j.bpj.2017.11.1611.

Cite as: https://hdl.handle.net/21.11116/0000-0001-31CD-1

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.