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
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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.
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页码：583 / 590
页数：7
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