Phospho-Synapsin I (S603) Antibody Summary
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Detection of Phospho-Synapsin I (S603) by Western Blot. Western blot of rat brain lysate showing specific immunolabeling of the ~78 kDa Synapsin I phosphorylated at S603 (Control). The phosphospecificity of this labeling is demonstrated by treatment with 1200 U of lambda Phosphatase ( lambda PPase) for 30 minutes before being exposed to the Anti-Phospho-Synapsin I (S603). The immunolabeling is completely eliminated by treatment with lambda PPase.
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Background: Synapsin I
Synapsin I is an 85 kDa neuron-specific, O-GlcNAcylated phosphoprotein that interacts with synaptic vesicles and regulates neurotransmitter release. It is concentrated in presynaptic terminals where it anchors synaptic vesicles to the underlying cytoskeleton. Phosphorylation at various sites reduces Synapsin I binding to neurosecretory vesicles, making them available for neurotransmitter release. Rat Synapsin I is 704 amino acids (aa) in length and contains five domains, named A-E/F. Domains A‑D lie between aa 1‑655, while E and F are alternate splice forms. Domain A (28 aa) regulates neurotransmitter release in a phosphorylation-dependent manner. Domains C (328 aa) and E (49 aa) anchor to actin in the synaptic region. Domains B (84 aa) and D (235 aa) promote actin and secretory vesicle interaction, and actin nucleation. Phosphorylation of S603 and S566 in domain D, and S9 in domain A, reduces the affinity of Synapsin I for actin and secretory vesicles.
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- Cole, R.N. and G.W. Hart (1999) J. Neurochem. 73:418.
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