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Synapsin phosphorylation by SRC tyrosine kinase enhances SRC activity in synaptic vesicles
Franco Onofri1, Mirko Messa, Vittoria Matafora
1Department of Experimental Medicine, University of Genova, 16132 Genova, Italy.
The Journal of Biological Chemistry
|April 3, 2007
Summary
Synapsins activate Src kinase on synaptic vesicles, influencing neurotransmitter release. This interaction is crucial for regulating synaptic vesicle-associated Src activity and downstream signaling.
Area of Science:
- Neuroscience
- Molecular Biology
- Cell Biology
Background:
- Synapsins are key phosphoproteins regulating neurotransmitter release.
- Synapsin I binds to c-Src's SH3 domain, stimulating its activity on synaptic vesicles.
Purpose of the Study:
- To investigate the mechanism and role of synapsin-mediated Src activation on synaptic vesicles.
- To elucidate how synapsin regulates Src activity and its impact on neurotransmitter release.
Main Methods:
- In vitro and intact synaptic vesicle phosphorylation assays.
- Mass spectrometry to identify phosphorylation sites.
- Synaptosome assays with Src domain internalization.
- Studies using synapsin null mice.
Main Results:
- Synapsin is tyrosine phosphorylated by c-Src at Tyr(301), a conserved site.
- Synapsin tyrosine phosphorylation enhances binding to Src SH2 domains.
- Vesicle-associated synapsin levels control Src activity.
- Reduced synapsin or disrupted Src-synapsin interaction impairs Src activity and alters neurotransmitter release.
Conclusions:
- Synapsin acts as both a substrate and activator of synaptic vesicle-associated c-Src.
- Regulation of Src activity by synapsin on synaptic vesicles is integral to neurotransmitter release control.
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