Stress-induced phosphorylation of SNAP-25

Citations of this article
Mendeley users who have this article in their library.


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.




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.

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free