Interaction of Synaptosomal-Associated Protein 25 with Neutral Sphingomyelinase 2: Functional Impact on the Sphingomyelin Pathway
- Authors
- Won, Jong Hoon; Jeon, Hyung Jun; Kim, Seok Kyun; Shin, In Chul; Jang, Ji Min; Ha, Hae Chan; Back, Moon Jung; Kim, Dae Kyong
- Issue Date
- 10-Feb-2020
- Publisher
- PERGAMON-ELSEVIER SCIENCE LTD
- Keywords
- synaptosomal-associated protein 25; ceramide; neutral sphingomyelinase 2; dopamine; neurotransmission
- Citation
- NEUROSCIENCE, v.427, pp 1 - 15
- Pages
- 15
- Journal Title
- NEUROSCIENCE
- Volume
- 427
- Start Page
- 1
- End Page
- 15
- URI
- https://scholarworks.bwise.kr/cau/handle/2019.sw.cau/38175
- DOI
- 10.1016/j.neuroscience.2019.08.015
- ISSN
- 0306-4522
1873-7544
- Abstract
- Neurotransmitter release is mediated by ceramide, which is generated by sphingomyelin hydrolysis. In the present study, we examined whether synaptosomal-associated protein 25 (SNAP-25) is involved in ceramide production and exocytosis. Neutral sphingomyelinase 2 (nSMase2) was partially purified from bovine brain and we found that SNAP-25 was enriched in the nSMase2-containing fractions. In rat synaptosomes and PC12 cells, the immunoprecipitation pellet of anti-SNAP-25 antibody showed higher nSMase activity than the immunoprecipitation pellet of anti-nSMase2 antibody. In PC12 cells, SNAP-25 was colocalized with nSMase2. Transfection of SNAP-25 small interfering RNA (siRNA) significantly inhibited nSMase2 translocation to the plasma membrane. A23187-induced ceramide production was concomitantly reduced in SNAP-25 siRNA-transfected PC12 cells compared with that in scrambled siRNA-transfected cells. Moreover, transfection of SNAP-25 siRNA inhibited dopamine release, whereas addition of C-6-ceramide to the siRNA-treated cells moderately reversed this inhibition. Additionally, nSMase2 inhibition reduced dopamine release. Collectively, our results indicate that SNAP-25 interacts with nSMase2 during ceramide production, which mediates exocytosis and neurotransmitter release. (C) 2019 Published by Elsevier Ltd on behalf of IBRO.
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