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Structure and topography of the synaptic V-ATPase–synaptophysin complex
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Structure and topography of the synaptic V-ATPase–synaptophysin complex
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Journal Article
Structure and topography of the synaptic V-ATPase–synaptophysin complex
2024
Overview
Synaptic vesicles are organelles with a precisely defined protein and lipid composition
1
,
2
, yet the molecular mechanisms for the biogenesis of synaptic vesicles are mainly unknown. Here we discovered a well-defined interface between the synaptic vesicle V-ATPase and synaptophysin by in situ cryo-electron tomography and single-particle cryo-electron microscopy of functional synaptic vesicles isolated from mouse brains
3
. The synaptic vesicle V-ATPase is an ATP-dependent proton pump that establishes the proton gradient across the synaptic vesicle, which in turn drives the uptake of neurotransmitters
4
,
5
. Synaptophysin
6
and its paralogues synaptoporin
7
and synaptogyrin
8
belong to a family of abundant synaptic vesicle proteins whose function is still unclear. We performed structural and functional studies of synaptophysin-knockout mice, confirming the identity of synaptophysin as an interaction partner with the V-ATPase. Although there is little change in the conformation of the V-ATPase upon interaction with synaptophysin, the presence of synaptophysin in synaptic vesicles profoundly affects the copy number of V-ATPases. This effect on the topography of synaptic vesicles suggests that synaptophysin assists in their biogenesis. In support of this model, we observed that synaptophysin-knockout mice exhibit severe seizure susceptibility, suggesting an imbalance of neurotransmitter release as a physiological consequence of the absence of synaptophysin.
Using cryo-electron tomography and single-particle cryo-electron microscopy of functional synaptic vesicles, a V-ATPase–synaptophysin interface was found to regulate synaptic vesicle biogenesis and alter seizure susceptibility.
Publisher
Nature Publishing Group UK,Nature Publishing Group
Subject
/ 101/58
/ 13
/ 13/1
/ 64/60
/ Animals
/ Electron Microscope Tomography
/ Humanities and Social Sciences
/ Lipids
/ Male
/ Mice
/ Neurotransmitter Agents - metabolism
/ Proteins
/ Protons
/ Science
/ Seizures
/ Structure-function relationships
/ Synaptic Vesicles - chemistry
/ Synaptic Vesicles - enzymology
/ Synaptic Vesicles - ultrastructure
/ Synaptophysin - ultrastructure
/ Vacuolar Proton-Translocating ATPases - analysis
/ Vacuolar Proton-Translocating ATPases - chemistry
/ Vacuolar Proton-Translocating ATPases - metabolism
/ Vacuolar Proton-Translocating ATPases - ultrastructure
/ Vesicles
