在3T3-L1脂肪细胞中，胰岛素刺激的GLUT4囊泡与质膜的融合依赖于渥曼青霉素敏感的胰岛素信号通路。
Insulin-stimulated fusion of GLUT4 vesicles to plasma membrane is dependent on wortmannin-sensitive insulin signaling pathway in 3T3-L1 adipocytes.
作者信息
Kawaguchi Takayuki, Tamori Yoshikazu, Yoshikawa Mari, Kanda Hajime, Kasuga Masato
机构信息
Division of Diabetes, Metabolism, and Endocrinology, Department of Internal Medicine, Kobe University Graduate School of Medicine, Chuo-ku, Kobe 650-0017, Japan.
出版信息
Kobe J Med Sci. 2008 Oct 30;54(4):E209-16.
It is established that wortmannin which completely inhibits class IA PI 3-kinase activation abrogated the insulin-dependent translocation of GLUT4 to the plasma membrane in adipocytes and skeletal muscle. However, it was not clear which steps wortmannin inhibited during the whole translocation process of GLUT4. We have now dissected the each steps of the GLUT4 trafficking in 3T3-L1 adipocytes using exogenously-expressed GLUT4 reporter in combination with plasma membrane lawn assay. We showed that 100 nM wortmannin inhibited the fusion of GLUT4 vesicles to the plasma membrane without affecting the movement and the subsequent tethering/docking event of GLUT4 vesicles to the membrane in 3T3-L1 adipocytes. These results suggest that wortmannin-sensitive insulin signaling pathway plays a crucial role in the fusion step of GLUT4 vesicles to the plasma membrane in 3T3-L1 adipocytes.
已证实，完全抑制IA类磷脂酰肌醇-3激酶（PI 3-激酶）激活的渥曼青霉素可消除脂肪细胞和骨骼肌中胰岛素依赖性葡萄糖转运蛋白4（GLUT4）向质膜的转位。然而，在GLUT4的整个转位过程中，渥曼青霉素抑制哪些步骤尚不清楚。我们现在利用外源性表达的GLUT4报告基因结合质膜平铺分析，剖析了3T3-L1脂肪细胞中GLUT4转运的各个步骤。我们发现，100 nM的渥曼青霉素抑制了GLUT4囊泡与质膜的融合，而不影响3T3-L1脂肪细胞中GLUT4囊泡向膜的移动以及随后的拴系/对接事件。这些结果表明，渥曼青霉素敏感的胰岛素信号通路在3T3-L1脂肪细胞中GLUT4囊泡与质膜的融合步骤中起关键作用。
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