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Clathrin coat controls synaptic vesicle acidification by blocking vacuolar ATPase activity
Max Planck Inst Biophys Chem, Dept Neurobiol, Gottingen, Germany.;Max Delbruck Ctr Mol Med, Berlin Inst Med Syst Biol, Berlin, Germany..
Univ Med Ctr Gottingen, European Neurosci Inst, Synapt Vesicle Dynam Grp, Gottingen, Germany..
Univ Med Ctr Gottingen, European Neurosci Inst, Synapt Vesicle Dynam Grp, Gottingen, Germany..
Sciloop, Hamburg, Germany..
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2018 (English)In: eLIFE, E-ISSN 2050-084X, Vol. 7, article id e32569Article in journal (Refereed) Published
Abstract [en]

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.

Place, publisher, year, edition, pages
ELIFE SCIENCES PUBLICATIONS LTD , 2018. Vol. 7, article id e32569
National Category
Biophysics
Identifiers
URN: urn:nbn:se:kth:diva-227777DOI: 10.7554/eLife.32569ISI: 000431395100001PubMedID: 29652249Scopus ID: 2-s2.0-85048847378OAI: oai:DiVA.org:kth-227777DiVA, id: diva2:1205409
Funder
EU, FP7, Seventh Framework Programme, 605544
Note

QC 20180514

Available from: 2018-05-14 Created: 2018-05-14 Last updated: 2018-10-16Bibliographically approved

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CiteExportLink to record
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