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@ARTICLE{Silbern:155596,
      author       = {Silbern, Ivan and Pan, Kuan-Ting and Fiosins, Maksims and
                      Bonn, Stefan and Rizzoli, Silvio O and Fornasiero, Eugenio F
                      and Urlaub, Henning and Jahn, Reinhard},
      title        = {{P}rotein {P}hosphorylation in {D}epolarized
                      {S}ynaptosomes: {D}issecting {P}rimary {E}ffects of
                      {C}alcium from {S}ynaptic {V}esicle {C}ycling.},
      journal      = {Molecular $\&$ cellular proteomics},
      volume       = {20},
      issn         = {1535-9476},
      address      = {Bethesda, Md.},
      publisher    = {The American Society for Biochemistry and Molecular
                      Biology},
      reportid     = {DZNE-2021-00764},
      pages        = {100061},
      year         = {2021},
      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.},
      keywords     = {Animals / Botulinum Toxins: pharmacology / Calcium:
                      metabolism / Clostridium botulinum / Glutamic Acid:
                      metabolism / HeLa Cells / Hippocampus: cytology / Humans /
                      Neurons: metabolism / Neurotoxins: pharmacology /
                      Phosphoproteins: metabolism / Phosphorylation / Proteome /
                      R-SNARE Proteins: metabolism / Rats, Wistar / Receptor,
                      Cannabinoid, CB1: metabolism / Synaptic Vesicles: metabolism
                      / Synaptosomes: metabolism / Syntaxin 1: metabolism /
                      Endocytosis (Other) / SNARE (Other) / botulinum neurotoxins
                      (Other) / cannabinoid receptor (Other) / exocytosis (Other)
                      / phosphomimetic studies (Other) / phosphorylation (Other) /
                      synapse (Other) / synaptobrevin (Other) / syntaxin (Other)},
      cin          = {AG Heutink},
      ddc          = {610},
      cid          = {I:(DE-2719)1210002},
      pnm          = {354 - Disease Prevention and Healthy Aging (POF4-354)},
      pid          = {G:(DE-HGF)POF4-354},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:33582301},
      pmc          = {pmc:PMC7995663},
      doi          = {10.1016/j.mcpro.2021.100061},
      url          = {https://pub.dzne.de/record/155596},
}