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  Protein phosphorylation in depolarized synaptosomes: Dissecting primary effects of calcium from synaptic vesicle cycling

Silbern, I., Pan, K. T., Fiosins, M., Bonn, S., Rizzoli, S. O., Fornasiero, E. F., et al. (2021). Protein phosphorylation in depolarized synaptosomes: Dissecting primary effects of calcium from synaptic vesicle cycling. Molecular and Cellular Proteomics, 20: 100061. doi:10.1016/j.mcpro.2021.100061.

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Silbern, I.1, Author              
Pan, K. T.1, Author              
Fiosins, M., Author
Bonn, S., Author
Rizzoli, S. O., Author
Fornasiero, E. F., Author
Urlaub, H.2, Author              
Jahn, R.3, Author              
Affiliations:
1Research Group of Bioanalytical Mass Spectrometry, MPI for Biophysical Chemistry, Max Planck Society, ou_578613              
2Research Group of Bioanalytical Mass Spectrometry, MPI for biophysical chemistry, Max Planck Society, ou_578613              
3Laboratory of Neurobiology, Max Planck Institute for Biophysical Chemistry, Max Planck Society, ou_3049887              

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Free keywords: Endocytosis; exocytosis; phosphorylation; synapse; SNARE; botulinum neurotoxins; phosphomimetic studies; synaptobrevin; syntaxin; cannabinoid receptor
 Abstract: Synaptic transmission is mediated by the regulated exocytosis of synaptic vesicles. When the presynaptic membrane is depolarized by an incoming action potential, voltage-gated calcium channels open, resulting in the influx of calcium ions that triggers the fusion of synaptic vesicles (SVs) with the plasma membrane. SVs are recycled by endocytosis. Phosphorylation of synaptic proteins plays a major role in these processes, and several studies have shown that the synaptic phosphoproteome changes rapidly in response to depolarization. However, it is unclear which of these changes are directly linked to SV cycling and which might regulate other presynaptic functions that are also controlled by calcium-dependent kinases and phosphatases. To address this question, we analyzed changes in the phosphoproteome using rat synaptosomes in which exocytosis was blocked with botulinum neurotoxins (BoNTs) while depolarization-induced calcium influx remained unchanged. BoNT-treatment significantly alters the response of the synaptic phoshoproteome to depolarization and results in reduced phosphorylation levels when compared with stimulation of synaptosomes by depolarization with KCl alone. We dissect the primary Ca2+-dependent phosphorylation from SV-cycling-dependent phosphorylation and confirm an effect of such SV-cycling-dependent phosphorylation events on syntaxin-1a-T21/T23, synaptobrevin-S75, and cannabinoid receptor-1-S314/T322 on exo- and endocytosis in cultured hippocampal neurons.

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Language(s): eng - English
 Dates: 2021-02-122021
 Publication Status: Published in print
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 Rev. Type: Peer
 Identifiers: DOI: 10.1016/j.mcpro.2021.100061
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Title: Molecular and Cellular Proteomics
Source Genre: Journal
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Pages: 20 Volume / Issue: 20 Sequence Number: 100061 Start / End Page: - Identifier: -