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- Title
Cophosphorylation of amphiphysin I and dynamin I by Cdk5 regulates clathrin-mediated endocytosis of synaptic vesicles.
- Authors
Tomizawa, Kazuhito; Sunada, Satoshi; Yun-Fei Lu, Satoshi; Oda, Yoshiya; Kinuta, Masahiro; Ohshima, Toshio; Saito, Taro; Fan-Yan Wei, Taro; Matsushita, Masayuki; Li, Sheng-Tian; Tsutsui, Kimiko; Hisanaga, Shin-ichi; Mikoshiba, Katsuhiko; Takei, Kohji; Matysui, Hideki
- Abstract
It has been thought that clathrin-mediated endocytosis is regulated by phosphorytation 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. CdkS 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 β-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.
- Subjects
ENDOCYTOSIS; PHOSPHORYLATION; PROTEINS; NEURONS; CELL physiology
- Publication
Journal of Cell Biology, 2003, Vol 163, Issue 4, p813
- ISSN
0021-9525
- Publication type
Article
- DOI
10.1083/jcb.200308110