AMPK controls the speed of microtubule polymerization and directional cell migration through CLIP-170 phosphorylation

被引：0

作者：

Atsushi Nakano

Hisakazu Kato

Takashi Watanabe

Kyung-Duk Min

Satoru Yamazaki

Yoshihiro Asano

Osamu Seguchi

Shuichiro Higo

Yasunori Shintani

Hiroshi Asanuma

Masanori Asakura

Tetsuo Minamino

Kozo Kaibuchi

Naoki Mochizuki

Masafumi Kitakaze

Seiji Takashima

机构：

[1] National Cardiovascular Center Research Institute Suita,Division of Cardiovascular Medicine

[2] National Cardiovascular Center,Department of Structural Analysis

[3] Research Institute Suita,Department of Cardiovascular Medicine

[4] Osaka University Graduate School of Medicine Suita,Department of Molecular Cardiology

[5] Osaka University Graduate School of Medicine Suita,Department of Cell Pharmacology

[6] Institute for Advanced Research,undefined

[7] Nagoya University Graduate School of Medicine,undefined

[8] Nagoya University Graduate School of Medicine,undefined

来源：

Nature Cell Biology | 2010年 / 12卷

关键词：

D O I：

暂无

中图分类号：

学科分类号：

摘要：

The microtubule plus end protein CLIP-170 has been shown to be an AMP activated protein kinase (AMPK) substrate. AMPK-mediated phosphorylation of CLIP-170 regulates microtubule polarization and directional cell migration.

引用

页码：583 / 590

页数：7

共 26 条

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