MISC

2007年6月

Truncations of amphiphysin I by calpain inhibit vesicle endocytosis during neural hyperexcitation

EMBO JOURNAL
  • Yumei Wu
  • ,
  • Shuang Liang
  • ,
  • Yoshiya Oda
  • ,
  • Iori Ohmori
  • ,
  • Tei-Ichi Nishiki
  • ,
  • Kohji Takei
  • ,
  • Hideki Matsui
  • ,
  • Kazuhito Tomizawa

26
12
開始ページ
2981
終了ページ
2990
記述言語
英語
掲載種別
DOI
10.1038/sj.emboj.7601741
出版者・発行元
NATURE PUBLISHING GROUP

Under normal physiological conditions, synaptic vesicle endocytosis is regulated by phosphorylation and Ca2+-dependent dephosphorylation of endocytic proteins such as amphiphysin and dynamin. To investigate the regulatory mechanisms that may occur under the conditions of excessive presynaptic Ca2+ influx observed preceding neural hyperexcitation, we examined hippocampal slices following high-potassium or high-frequency electrical stimulation (HFS). In both cases, three truncated forms of amphiphysin I resulted from cleavage by the protease calpain. In vitro, the binding of truncated amphiphysin I to dynamin I and copolymerization into rings with dynamin I were inhibited, but its interaction with liposomes was not affected. Moreover, overexpression of the truncated form of amphiphysin I inhibited endocytosis of transferrin and synaptic vesicles. Inhibiting calpain prevented HFS-induced depression of presynaptic transmission. Finally, calpain-dependent amphiphysin I cleavage attenuated kainate-induced seizures. These results suggest that calpain-dependent cleavage of amphiphysin I inhibits synaptic vesicle endocytosis during neural hyperexcitation and demonstrate a novel post-translational regulation of endocytosis.


リンク情報
DOI
https://doi.org/10.1038/sj.emboj.7601741
Web of Science
https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000248038200015&DestApp=WOS_CPL
ID情報
  • DOI : 10.1038/sj.emboj.7601741
  • ISSN : 0261-4189
  • Web of Science ID : WOS:000248038200015

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