@article{oai:soar-ir.repo.nii.ac.jp:00012409,
 author = {Kataoka,  Masakazu and Yamamori,  Saori and Suzuki,  Eiji and Watanabe,  Shigeru and Sato,  Taku and Miyaoka,  Hitoshi and Azuma,  Sadahiro and Ikegami,  Shiro and Kuwahara,  Reiko and Suzuki-Migishima,  Rika and Nakahara,  Yohko and Nihonmatsu,  Itsuko and Inokuchi,  Kaoru and Katoh-Fukui,  Yuko and Yokoyama,  Minesuke and Takahashi,  Masami},
 issue = {9},
 journal = {PLOS ONE},
 month = {Sep},
 note = {Synaptosomal-associated protein of 25 kDa (SNAP-25) is a presynaptic protein essential for neurotransmitter release. Previously, we demonstrate that protein kinase C (PKC) phosphorylates Ser(187) of SNAP-25, and enhances neurotransmitter release by recruiting secretory vesicles near to the plasma membrane. As PKC is abundant in the brain and SNAP-25 is essential for synaptic transmission, SNAP-25 phosphorylation is likely to play a crucial role in the central nervous system. We therefore generated a mutant mouse, substituting Ser(187) of SNAP-25 with Ala using "knock-in" technology. The most striking effect of the mutation was observed in their behavior. The homozygous mutant mice froze readily in response to environmental change, and showed strong anxiety-related behavior in general activity and light and dark preference tests. In addition, the mutant mice sometimes exhibited spontaneously occurring convulsive seizures. Microdialysis measurements revealed that serotonin and dopamine release were markedly reduced in amygdala. These results clearly indicate that PKC-dependent SNAP-25 phosphorylation plays a critical role in the regulation of emotional behavior as well as the suppression of epileptic seizures, and the lack of enhancement of monoamine release is one of the possible mechanisms underlying these defects., Article, PLOS ONE. 6(9):e25158 (2011)},
 title = {A Single Amino Acid Mutation in SNAP-25 Induces Anxiety-Related Behavior in Mouse},
 volume = {6},
 year = {2011}
}