TY - JOUR
T1 - The SNARE proteins SNAP25 and synaptobrevin are involved in endocytosis at hippocampal synapses
AU - Zhang, Zhen
AU - Wang, Dongsheng
AU - Sun, Tao
AU - Xu, Jianhua
AU - Chiang, Hsueh Cheng
AU - Shin, Wonchul
AU - Wu, Ling Gang
PY - 2013/5/22
Y1 - 2013/5/22
N2 - SNAP25, an essential component of the soluble NSF (N-ethylmaleimide-sensitive factor) attachment protein receptor (SNARE) complex that mediates exocytosis, is not considered to play a role in endocytosis, which couples to exocytosis by retrieving a similar amount of exocytosed vesicles. By knocking down SNAP25 and imaging slow endocytosis at a conventional synapse, the rat cultured hippocampal synapse, we found that SNAP25 is involved in slow, clathrin-dependent endocytosis. With similar techniques, we found that not only SNAP25, but also synaptobrevin is involved in slow endocytosis. These results provide the first evidence showing the dual role of SNAP25 and synaptobrevin in both exocytosis and slow endocytosis at conventional synapses. Such a dual role may contribute to mediate the coupling between exocytosis and clathrin-dependent endocytosis at conventional synapses, a mechanism critical for the maintenance of synaptic transmission and the normal structure of nerve terminals.
AB - SNAP25, an essential component of the soluble NSF (N-ethylmaleimide-sensitive factor) attachment protein receptor (SNARE) complex that mediates exocytosis, is not considered to play a role in endocytosis, which couples to exocytosis by retrieving a similar amount of exocytosed vesicles. By knocking down SNAP25 and imaging slow endocytosis at a conventional synapse, the rat cultured hippocampal synapse, we found that SNAP25 is involved in slow, clathrin-dependent endocytosis. With similar techniques, we found that not only SNAP25, but also synaptobrevin is involved in slow endocytosis. These results provide the first evidence showing the dual role of SNAP25 and synaptobrevin in both exocytosis and slow endocytosis at conventional synapses. Such a dual role may contribute to mediate the coupling between exocytosis and clathrin-dependent endocytosis at conventional synapses, a mechanism critical for the maintenance of synaptic transmission and the normal structure of nerve terminals.
UR - http://www.scopus.com/inward/record.url?scp=84877976648&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84877976648&partnerID=8YFLogxK
U2 - 10.1523/JNEUROSCI.0301-13.2013
DO - 10.1523/JNEUROSCI.0301-13.2013
M3 - Article
C2 - 23699527
AN - SCOPUS:84877976648
SN - 0270-6474
VL - 33
SP - 9169
EP - 9175
JO - Journal of Neuroscience
JF - Journal of Neuroscience
IS - 21
ER -