Home > Publications Database > Protein Phosphorylation in Depolarized Synaptosomes: Dissecting Primary Effects of Calcium from Synaptic Vesicle Cycling. > print

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024 7 _ |a 10.1016/j.mcpro.2021.100061
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037 _ _ |a DZNE-2021-00764
041 _ _ |a English
082 _ _ |a 610
100 1 _ |a Silbern, Ivan
|b 0
245 _ _ |a Protein Phosphorylation in Depolarized Synaptosomes: Dissecting Primary Effects of Calcium from Synaptic Vesicle Cycling.
260 _ _ |a Bethesda, Md.
|c 2021
|b The American Society for Biochemistry and Molecular Biology
336 7 _ |a article
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520 _ _ |a 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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650 _ 7 |a Endocytosis
|2 Other
650 _ 7 |a SNARE
|2 Other
650 _ 7 |a botulinum neurotoxins
|2 Other
650 _ 7 |a cannabinoid receptor
|2 Other
650 _ 7 |a exocytosis
|2 Other
650 _ 7 |a phosphomimetic studies
|2 Other
650 _ 7 |a phosphorylation
|2 Other
650 _ 7 |a synapse
|2 Other
650 _ 7 |a synaptobrevin
|2 Other
650 _ 7 |a syntaxin
|2 Other
650 _ 2 |a Animals
|2 MeSH
650 _ 2 |a Botulinum Toxins: pharmacology
|2 MeSH
650 _ 2 |a Calcium: metabolism
|2 MeSH
650 _ 2 |a Clostridium botulinum
|2 MeSH
650 _ 2 |a Glutamic Acid: metabolism
|2 MeSH
650 _ 2 |a HeLa Cells
|2 MeSH
650 _ 2 |a Hippocampus: cytology
|2 MeSH
650 _ 2 |a Humans
|2 MeSH
650 _ 2 |a Neurons: metabolism
|2 MeSH
650 _ 2 |a Neurotoxins: pharmacology
|2 MeSH
650 _ 2 |a Phosphoproteins: metabolism
|2 MeSH
650 _ 2 |a Phosphorylation
|2 MeSH
650 _ 2 |a Proteome
|2 MeSH
650 _ 2 |a R-SNARE Proteins: metabolism
|2 MeSH
650 _ 2 |a Rats, Wistar
|2 MeSH
650 _ 2 |a Receptor, Cannabinoid, CB1: metabolism
|2 MeSH
650 _ 2 |a Synaptic Vesicles: metabolism
|2 MeSH
650 _ 2 |a Synaptosomes: metabolism
|2 MeSH
650 _ 2 |a Syntaxin 1: metabolism
|2 MeSH
700 1 _ |a Pan, Kuan-Ting
|b 1
700 1 _ |a Fiosins, Maksims
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700 1 _ |a Bonn, Stefan
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700 1 _ |a Rizzoli, Silvio O
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700 1 _ |a Fornasiero, Eugenio F
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700 1 _ |a Urlaub, Henning
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700 1 _ |a Jahn, Reinhard
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773 _ _ |a 10.1016/j.mcpro.2021.100061
|g Vol. 20, p. 100061 -
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|t Molecular & cellular proteomics
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856 4 _ |u https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7995663/
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