Cross-linking mass spectrometry uncovers protein interactions and functional assemblies in synaptic vesicle membranes

Sabine Wittig, Marcelo Ganzella, Marie Barth, Susann Kostmann, Dietmar Riedel, Ángel Pérez-Lara, Reinhard Jahn and Carla Schmidt ()
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Sabine Wittig: Martin Luther University Halle-Wittenberg
Marcelo Ganzella: Max Planck Institute for Biophysical Chemistry
Marie Barth: Martin Luther University Halle-Wittenberg
Susann Kostmann: Martin Luther University Halle-Wittenberg
Dietmar Riedel: Max Planck Institute for Biophysical Chemistry
Ángel Pérez-Lara: Max Planck Institute for Biophysical Chemistry
Reinhard Jahn: Max Planck Institute for Biophysical Chemistry
Carla Schmidt: Martin Luther University Halle-Wittenberg

Nature Communications, 2021, vol. 12, issue 1, 1-14

Abstract: 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 sub-populations 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.

Date: 2021
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DOI: 10.1038/s41467-021-21102-w

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