Evidence map›Paper›PMID 29652249›Full record

ArticleeLife2018

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

Zohreh Farsi, Sindhuja Gowrisankaran, Matija Krunic, Burkhard Rammner, Andrew Woehler, Eileen M Lafer, Carsten Mim, Reinhard Jahn, Ira Milosevic

Abstract read
In one paragraph

Article in eLife, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

31 citing papers in PubMed.

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  12. Molecular architecture of synaptic vesicles.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  13. Article
  14. Review
  15. Possible Compensatory Role of ASICs in Glutamatergic Synapses.International journal of molecular sciences · 2023
    Article
  16. Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

9 authors.

Zohreh FarsiDepartment of Neurobiology, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.
Sindhuja Gowrisankaran *Synaptic Vesicle Dynamics Group, European Neuroscience Institute, University Medical Center Göttingen, Göttingen, Germany.
Matija Krunic *Synaptic Vesicle Dynamics Group, European Neuroscience Institute, University Medical Center Göttingen, Göttingen, Germany.
Burkhard RammnerSciloop, Hamburg, Germany.
Andrew WoehlerBerlin Institute for Medical Systems Biology, Max Delbrück Center for Molecular Medicine, Berlin, Germany.
Eileen M LaferDepartment of Biochemistry and Structural Biology, University of Texas Health Science Center at San Antonio, San Antonio, United States.
Carsten MimDepartment for Biomedical Engineering and Health Solutions, Kungliga Tekniska Högskolan, Huddinge, Sweden.
Reinhard JahnDepartment of Neurobiology, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.ORCID http://orcid.org/0000-0003-1542-3498
Ira MilosevicSynaptic Vesicle Dynamics Group, European Neuroscience Institute, University Medical Center Göttingen, Göttingen, Germany.ORCID http://orcid.org/0000-0001-6440-3763

Funding

Chaperone Mechanisms in Clathrin Mediated Neuronal Vesicle TraffickingR01GM118933 · NIGMS · UNIVERSITY OF TEXAS HLTH SCIENCE CENTER · PI LAFER, EILEEN M., SOUSA, RUI J. · 2016 to 2019
$1.7M
NIGMS NIH HHS R01 GM118933NIH HHS GM118933
6 · The paper itself

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.

Indexed as

Adenosine TriphosphateAnimalsBrainClathrinClathrin-Coated VesiclesHydrolysisMiceSynaptic VesiclesVacuolar Proton-Translocating ATPasesAdenosine TriphosphateClathrinVacuolar Proton-Translocating ATPasesacidificationclathrin coatE. coliendocytosishumanmouseneuroscienceproton pumpsynaptic vesiclevATPase

Identifiers

PMID29652249
PMCPMC5935483

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.