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

Wittig, S., Ganzella, M., Kostmann, S., Barth, M., Riedel, D., Perez-Lara, A., et al. (2021). Cross-linking mass spectrometry uncovers protein interactions and functional assemblies in synaptic vesicle membranes. Nature Communications, 12: 858. doi:10.1038/s41467-021-21102-w.

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Wittig, S., Author
Ganzella, M.1, Author              
Kostmann, S., Author
Barth, M., Author
Riedel, D.2, Author              
Perez-Lara, A., Author
Jahn, R.3, Author              
Schmidt, C., Author
Affiliations:
1Laboratory of Neurobiology, MPI for Biophysical Chemistry, Max Planck Society, ou_3049887              
2Facility for Electron Microscopy, MPI for biophysical chemistry, Max Planck Society, ou_578615              
3Laboratory of Neurobiology, Max Planck Institute for Biophysical Chemistry, Max Planck Society, ou_3049887              

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Free keywords: Protein–protein interaction networks; Structural biology
 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.

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Language(s): eng - English
 Dates: 2021-02-08
 Publication Status: Published online
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 Rev. Type: Peer
 Identifiers: DOI: 10.1038/s41467-021-21102-w
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Title: Nature Communications
Source Genre: Journal
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Pages: - Volume / Issue: 12 Sequence Number: 858 Start / End Page: - Identifier: -