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000155596 0247_ $$2doi$$a10.1016/j.mcpro.2021.100061
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000155596 037__ $$aDZNE-2021-00764
000155596 041__ $$aEnglish
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000155596 1001_ $$aSilbern, Ivan$$b0
000155596 245__ $$aProtein Phosphorylation in Depolarized Synaptosomes: Dissecting Primary Effects of Calcium from Synaptic Vesicle Cycling.
000155596 260__ $$aBethesda, Md.$$bThe American Society for Biochemistry and Molecular Biology$$c2021
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000155596 520__ $$aSynaptic transmission is mediated by the regulated exocytosis of synaptic vesicles. When the presynaptic membrane is depolarized by an incoming action potential, voltage-gated calcium channels open, resulting in the influx of calcium ions that triggers the fusion of synaptic vesicles (SVs) with the plasma membrane. SVs are recycled by endocytosis. Phosphorylation of synaptic proteins plays a major role in these processes, and several studies have shown that the synaptic phosphoproteome changes rapidly in response to depolarization. However, it is unclear which of these changes are directly linked to SV cycling and which might regulate other presynaptic functions that are also controlled by calcium-dependent kinases and phosphatases. To address this question, we analyzed changes in the phosphoproteome using rat synaptosomes in which exocytosis was blocked with botulinum neurotoxins (BoNTs) while depolarization-induced calcium influx remained unchanged. BoNT-treatment significantly alters the response of the synaptic phoshoproteome to depolarization and results in reduced phosphorylation levels when compared with stimulation of synaptosomes by depolarization with KCl alone. We dissect the primary Ca2+-dependent phosphorylation from SV-cycling-dependent phosphorylation and confirm an effect of such SV-cycling-dependent phosphorylation events on syntaxin-1a-T21/T23, synaptobrevin-S75, and cannabinoid receptor-1-S314/T322 on exo- and endocytosis in cultured hippocampal neurons.
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000155596 650_7 $$2Other$$aEndocytosis
000155596 650_7 $$2Other$$aSNARE
000155596 650_7 $$2Other$$abotulinum neurotoxins
000155596 650_7 $$2Other$$acannabinoid receptor
000155596 650_7 $$2Other$$aexocytosis
000155596 650_7 $$2Other$$aphosphomimetic studies
000155596 650_7 $$2Other$$aphosphorylation
000155596 650_7 $$2Other$$asynapse
000155596 650_7 $$2Other$$asynaptobrevin
000155596 650_7 $$2Other$$asyntaxin
000155596 650_2 $$2MeSH$$aAnimals
000155596 650_2 $$2MeSH$$aBotulinum Toxins: pharmacology
000155596 650_2 $$2MeSH$$aCalcium: metabolism
000155596 650_2 $$2MeSH$$aClostridium botulinum
000155596 650_2 $$2MeSH$$aGlutamic Acid: metabolism
000155596 650_2 $$2MeSH$$aHeLa Cells
000155596 650_2 $$2MeSH$$aHippocampus: cytology
000155596 650_2 $$2MeSH$$aHumans
000155596 650_2 $$2MeSH$$aNeurons: metabolism
000155596 650_2 $$2MeSH$$aNeurotoxins: pharmacology
000155596 650_2 $$2MeSH$$aPhosphoproteins: metabolism
000155596 650_2 $$2MeSH$$aPhosphorylation
000155596 650_2 $$2MeSH$$aProteome
000155596 650_2 $$2MeSH$$aR-SNARE Proteins: metabolism
000155596 650_2 $$2MeSH$$aRats, Wistar
000155596 650_2 $$2MeSH$$aReceptor, Cannabinoid, CB1: metabolism
000155596 650_2 $$2MeSH$$aSynaptic Vesicles: metabolism
000155596 650_2 $$2MeSH$$aSynaptosomes: metabolism
000155596 650_2 $$2MeSH$$aSyntaxin 1: metabolism
000155596 7001_ $$aPan, Kuan-Ting$$b1
000155596 7001_ $$0P:(DE-2719)2811935$$aFiosins, Maksims$$b2$$udzne
000155596 7001_ $$0P:(DE-2719)2810547$$aBonn, Stefan$$b3$$udzne
000155596 7001_ $$aRizzoli, Silvio O$$b4
000155596 7001_ $$0P:(DE-HGF)0$$aFornasiero, Eugenio F$$b5$$eCorresponding author
000155596 7001_ $$0P:(DE-HGF)0$$aUrlaub, Henning$$b6$$eCorresponding author
000155596 7001_ $$0P:(DE-HGF)0$$aJahn, Reinhard$$b7$$eCorresponding author
000155596 773__ $$0PERI:(DE-600)2071375-7$$a10.1016/j.mcpro.2021.100061$$gVol. 20, p. 100061 -$$p100061$$tMolecular & cellular proteomics$$v20$$x1535-9476$$y2021
000155596 8564_ $$uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC7995663/
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