Exercise and Insulin: Convergence or Divergence at AS160 and TBC1D1?

被引：59

作者：

Cartee, Gregory D. ^{[1
,2
]}

Funai, Katsuhiko ^{[1
]}

机构：

[1] Univ Michigan, Sch Kinesiol, Muscle Biol Lab, Ann Arbor, MI 48109 USA

[2] Univ Michigan, Dept Mol & Integrat Physiol, Ann Arbor, MI 48109 USA

来源：

EXERCISE AND SPORT SCIENCES REVIEWS | 2009年 / 37卷 / 04期

关键词：

glucose transport; skeletal muscle; TBC1D4; AMP-activated protein kinase; protein kinase B; contraction; GLUT4; RAT SKELETAL-MUSCLE; STIMULATED GLUCOSE-TRANSPORT; 160 KDA AS160; GLUT4; TRANSLOCATION; AKT SUBSTRATE; RESISTANCE EXERCISE; REGULATE AS160; 14-3-3; BINDING; PHOSPHORYLATION; CONTRACTION;

D O I：

10.1097/JES.0b013e3181b7b7c5

中图分类号：

Q4 [生理学];

学科分类号：

071003 [生理学];

摘要：

CARTEE, G.D. and K. FUNAL Exercise and Insulin: Convergence or Divergence atAS160 and TBC1D1? Exerc. Sport Sci. Rev., Vol. 37, No. 4, pp. 188-195, 2009. Akt substrate of 160 kDa (called AS160 or TBC1D4) and TBC1D1, Rab GTPase-activating proteins that regulate glucose transport, become phosphorylated with exercise or insulin stimulation. Evidence suggests that this convergence may prove to be imperfect, and each stimulus will produce a unique phosphosignature, providing a plausible mechanism for their apparently unique and overlapping roles in exercise- and insulin-stimulated glucose transport.

引用

页码：188 / 195

页数：8

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