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Synapsin I from human brain. Phosphorylation by Ca2+, phospholipid-dependent protein kinase
S E Severin1, E L Moskvitina, E V Bykova
1M.V. Lomonosov Institute of Fine Chemical Technology, Moscow, USSR.
FEBS Letters
|December 4, 1989
Summary
Human brain synapsin I phosphorylation by protein kinase C is inhibited by calmodulin. Non-esterified fatty acids and acidic phospholipids also inhibit synapsin I phosphorylation by Ca2+, calmodulin-dependent protein kinase II.
Area of Science:
- Neuroscience
- Molecular Biology
- Biochemistry
Background:
- Synapsin I is a crucial neuronal phosphoprotein involved in regulating neurotransmitter release.
- Protein kinases play key roles in modulating synaptic function through protein phosphorylation.
Purpose of the Study:
- To investigate the phosphorylation of human brain synapsin I by Ca2+, phospholipid-dependent protein kinase (protein kinase C).
- To examine the regulatory effects of calmodulin, fatty acids, and phospholipids on synapsin I phosphorylation.
Main Methods:
- Rapid and efficient purification of synapsin I from human brain tissue.
- In vitro kinase assays to study synapsin I phosphorylation by protein kinase C and Ca2+, calmodulin-dependent protein kinase II.
Main Results:
- Calmodulin was found to inhibit the phosphorylation of synapsin I by protein kinase C.
- Non-esterified fatty acids and acidic phospholipids demonstrated inhibitory effects on synapsin I phosphorylation mediated by Ca2+, calmodulin-dependent protein kinase II.
Conclusions:
- Synapsin I phosphorylation is subject to complex regulation by various cellular factors.
- Calmodulin, fatty acids, and phospholipids act as negative regulators in specific synapsin I phosphorylation pathways.