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Cophosphorylation of amphiphysin I and dynamin I by Cdk5 regulates clathrin-mediated endocytosis of synaptic vesicles
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 process...
Autores principales: | , , , , , , , , , , , , , , |
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Formato: | Texto |
Lenguaje: | English |
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The Rockefeller University Press
2003
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2173686/ https://www.ncbi.nlm.nih.gov/pubmed/14623869 http://dx.doi.org/10.1083/jcb.200308110 |
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author | Tomizawa, Kazuhito Sunada, Satoshi Lu, Yun-Fei Oda, Yoshiya Kinuta, Masahiro Ohshima, Toshio Saito, Taro Wei, Fan-Yan Matsushita, Masayuki Li, Sheng-Tian Tsutsui, Kimiko Hisanaga, Shin-ichi Mikoshiba, Katsuhiko Takei, Kohji Matsui, Hideki |
author_facet | Tomizawa, Kazuhito Sunada, Satoshi Lu, Yun-Fei Oda, Yoshiya Kinuta, Masahiro Ohshima, Toshio Saito, Taro Wei, Fan-Yan Matsushita, Masayuki Li, Sheng-Tian Tsutsui, Kimiko Hisanaga, Shin-ichi Mikoshiba, Katsuhiko Takei, Kohji Matsui, Hideki |
author_sort | Tomizawa, Kazuhito |
collection | PubMed |
description | 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 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. |
format | Text |
id | pubmed-2173686 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2003 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-21736862008-05-01 Cophosphorylation of amphiphysin I and dynamin I by Cdk5 regulates clathrin-mediated endocytosis of synaptic vesicles Tomizawa, Kazuhito Sunada, Satoshi Lu, Yun-Fei Oda, Yoshiya Kinuta, Masahiro Ohshima, Toshio Saito, Taro Wei, Fan-Yan Matsushita, Masayuki Li, Sheng-Tian Tsutsui, Kimiko Hisanaga, Shin-ichi Mikoshiba, Katsuhiko Takei, Kohji Matsui, Hideki J Cell Biol Article 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 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. The Rockefeller University Press 2003-11-24 /pmc/articles/PMC2173686/ /pubmed/14623869 http://dx.doi.org/10.1083/jcb.200308110 Text en Copyright © 2003, The Rockefeller University Press This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/). |
spellingShingle | Article Tomizawa, Kazuhito Sunada, Satoshi Lu, Yun-Fei Oda, Yoshiya Kinuta, Masahiro Ohshima, Toshio Saito, Taro Wei, Fan-Yan Matsushita, Masayuki Li, Sheng-Tian Tsutsui, Kimiko Hisanaga, Shin-ichi Mikoshiba, Katsuhiko Takei, Kohji Matsui, Hideki Cophosphorylation of amphiphysin I and dynamin I by Cdk5 regulates clathrin-mediated endocytosis of synaptic vesicles |
title | Cophosphorylation of amphiphysin I and dynamin I by Cdk5 regulates clathrin-mediated endocytosis of synaptic vesicles |
title_full | Cophosphorylation of amphiphysin I and dynamin I by Cdk5 regulates clathrin-mediated endocytosis of synaptic vesicles |
title_fullStr | Cophosphorylation of amphiphysin I and dynamin I by Cdk5 regulates clathrin-mediated endocytosis of synaptic vesicles |
title_full_unstemmed | Cophosphorylation of amphiphysin I and dynamin I by Cdk5 regulates clathrin-mediated endocytosis of synaptic vesicles |
title_short | Cophosphorylation of amphiphysin I and dynamin I by Cdk5 regulates clathrin-mediated endocytosis of synaptic vesicles |
title_sort | cophosphorylation of amphiphysin i and dynamin i by cdk5 regulates clathrin-mediated endocytosis of synaptic vesicles |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2173686/ https://www.ncbi.nlm.nih.gov/pubmed/14623869 http://dx.doi.org/10.1083/jcb.200308110 |
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