Phosphorylation of VAMP/synaptobrevin in synaptic vesicles by endogenous protein kinases

Autor: Giampietro Schiavo, Flavia Valtorta, Paul Greengard, Cesare Montecucco, Fabio Benfenati, H. B. Nielander, Franco Onofri
Přispěvatelé: Nielander, H. B, Onofri, F, Valtorta, Flavia, Schiavo, G, Montecucco, C, Greengard, P, Benfenati, F.
Jazyk: angličtina
Rok vydání: 1995
Předmět:
Botulinum Toxins
Synaptobrevin
Protein Kinase
Molecular Sequence Data
Nerve Tissue Proteins
Botulinum Toxin
Calcium-Calmodulin-Dependent Protein Kinase
Protein Serine-Threonine Kinases
Protein-Serine-Threonine Kinase
Biology
Biochemistry
Synaptic vesicle
R-SNARE Proteins
Cellular and Molecular Neuroscience
chemistry.chemical_compound
R-SNARE Protein
Ca2+/calmodulin-dependent protein kinase
Animals
Electrophoresis
Gel
Two-Dimensional
Amino Acid Sequence
Amino Acids
Phosphorylation
Casein Kinase II
Protein kinase A
Neurotransmitter
Membrane Protein
Protein Kinase C
Animal
Kinase
Membrane Proteins
Rats
Cell biology
Amino Acid
chemistry
Calcium-Calmodulin-Dependent Protein Kinases
Nerve Tissue Protein
Rat
Synaptic Vesicles
Casein kinase 2
Calcium-Calmodulin-Dependent Protein Kinase Type 2
Protein Kinases
Zdroj: Scopus-Elsevier
Europe PubMed Central
Popis: VAMP/synaptobrevin (SYB), an integral membrane protein of small synaptic vesicles, is specifically cleaved by tetanus neurotoxin and botulinum neurotoxins B, D, F, and G is thought to play an important role in the docking and/or fusion of synaptic vesicles with the presynaptic membrane. Potential phosphorylation sites for various kinases are present in SYB sequence. We have studied whether SYB is a substrate for protein kinases that are present in nerve terminals and known to modulate neurotransmitter release. SYB can be phosphorylated within the same vesicle by endogenous Ca2+/calmodulin-dependent protein kinase II (CaMKII) associated with synaptic vesicles. This phosphorylation reaction occurs rapidly and involves serine and threonine residues in the cytoplasmic region of SYB. Similarly to CaMKII, a casein kinase II (CasKII) activity copurifying with synaptic vesicles is able to phosphorylate SYB selectively on serine residues of the cytoplasmic region. This phosphorylation reaction is markedly stimulated by sphingosine, a sphingolipid known to activate CasKII and to inhibit CaMKII and protein kinase C. The results show that SYB is a potential substrate for protein kinases involved in the regulation of neurotransmitter release and open the possibility that phosphorylation of SYB plays a role in modulating the molecular interactions between synaptic vesicles and the presynaptic membrane.
Databáze: OpenAIRE
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