@misc{10481/68079,
year = {2021},
url = {http://hdl.handle.net/10481/68079},
abstract = {Synaptic vesicles are storage organelles for neurotransmitters. They pass through a trafficking cycle and fuse with the pre-synaptic membrane when an action potential arrives at the
nerve terminal. While molecular components and biophysical parameters of synaptic vesicles
have been determined, our knowledge on the protein interactions in their membranes is
limited. Here, we apply cross-linking mass spectrometry to study interactions of synaptic
vesicle proteins in an unbiased approach without the need for specific antibodies or
detergent-solubilisation. Our large-scale analysis delivers a protein network of vesicle subpopulations and functional assemblies including an active and an inactive conformation of the
vesicular ATPase complex as well as non-conventional arrangements of the luminal loops of
SV2A, Synaptophysin and structurally related proteins. Based on this network, we specifically
target Synaptobrevin-2, which connects with many proteins, in different approaches. Our
results allow distinction of interactions caused by ‘crowding’ in the vesicle membrane from
stable interaction modules.},
organization = {Projekt DEAL},
publisher = {NATURE RESEARCH},
title = {Cross-linking mass spectrometry uncovers protein interactions and functional assemblies in synaptic vesicle membranes},
doi = {10.1038/s41467-021-21102-w},
author = {Wittig, Sabine and Pérez Lara, Francisco Ángel},
}