Stress-induced phosphorylation of SNAP-25

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Abstract

Synaptosomal-associated protein of 25kDa (SNAP-25), a t-SNARE protein, plays a crucial role in neurotransmitter release by exocytosis. Protein kinase C phosphorylates SNAP-25 at Ser187, however the physiological significance of this phosphorylation event in brain function remains unclear. In the present study, we found that SNAP-25 phosphorylation increased rapidly in the mouse brain following cold-water restraint stress. Both basal and stress-induced phosphorylation of SNAP-25 were high in stress-related brain regions, including the cerebral cortex, hippocampus, and amygdala, and the extent of phosphorylation increased with increasing amounts of stress. Intravenous administration of adrenaline increased SNAP-25 phosphorylation, although stress-induced phosphorylation was still observed in adrenalectomized mice. These results indicate that SNAP-25 phosphorylation is regulated in a stress-dependent manner through both central and peripheral mechanisms. © 2013 Elsevier Ireland Ltd.

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Yamamori, S., Sugaya, D., Iida, Y., Kokubo, H., Itakura, M., Suzuki, E., … Takahashi, M. (2014). Stress-induced phosphorylation of SNAP-25. Neuroscience Letters, 561, 182–187. https://doi.org/10.1016/j.neulet.2013.12.044

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