2003年11月
Cophosphorylation of amphiphysin 1 and dynamin 1 by Cdk5 regulates clathrin-mediated endocytosis of synaptic vesicles
JOURNAL OF CELL BIOLOGY
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- 巻
- 163
- 号
- 4
- 開始ページ
- 813
- 終了ページ
- 824
- 記述言語
- 英語
- 掲載種別
- DOI
- 10.1083/jcb.200308110
- 出版者・発行元
- ROCKEFELLER UNIV PRESS
It has been thought that clathrin-mediated endocytosis is regulated by phosphorylation and dephosphorylation of many endocytic proteins, including amphiphysin I and dynamin I. Here, we show that Cdk5/p35-dependent cophosphorylation of amphiphysin I and dynamin I plays a critical role in such processes. Cdk5 inhibitors enhanced the electric stimulation-induced endocytosis in hippocampal neurons, and the endocytosis was also enhanced in the neurons of p35-deficient mice. Cdk5 phosphorylated the proline-rich domain of both amphiphysin I and dynamin I in vitro and in vivo. Cdk5-dependent phosphorylation of amphiphysin I inhibited the association with P-adaptin. Furthermore, the phosphorylation of dynamin I blocked its binding to amphiphysin I. The phosphorylation of each protein reduced the copolymerization into a ring formation in a cell-free system. Moreover, the phosphorylation of both proteins completely disrupted the copolymerization into a ring formation. Finally, phosphorylation of both proteins was undetectable in p35-deficient mice.
- リンク情報
- ID情報
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- DOI : 10.1083/jcb.200308110
- ISSN : 0021-9525
- Web of Science ID : WOS:000186849800014