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80K-H在完整活细胞中作为蛋白激酶Cζ(PKCζ)与葡萄糖转运蛋白4(GLUT4)转位调节因子Munc18c之间的信号传导桥梁。

80K-H acts as a signaling bridge in intact living cells between PKCzeta and the GLUT4 translocation regulator Munc18c.

作者信息

Smithers Natalie P, Hodgkinson Conrad P, Cuttle Matt, Sale Graham J

机构信息

School of Biological Sciences, University of Southampton, Southampton, United Kingdom.

出版信息

J Recept Signal Transduct Res. 2008;28(6):581-9. doi: 10.1080/10799890802598571.

Abstract

Insulin triggers the translocation of glucose transporter GLUT4 to the plasma membrane. To understand the nature of the missing links between upstream insulin activated kinases and proteins of the GLUT4 translocation apparatus, the role of 80K-H was examined to test if it was one such missing link in live cells. Fluorescence correlation spectroscopy showed that the mobility of 80K-H was significantly decreased by insulin stimulation. This was dependent on the presence of PKCzeta and an intact binding site for PKCzeta. Insulin also increased the mobility of munc18c in an 80K-H- and PKCzeta dependent manner. These results indicate that insulin induces dynamic associations between PKCzeta, 80K-H, and munc18c and that 80K-H may act as a key signaling link between PKCzeta and munc18c in live cells.

摘要

胰岛素触发葡萄糖转运蛋白GLUT4向质膜的转位。为了了解上游胰岛素激活激酶与GLUT4转位装置蛋白之间缺失环节的本质,研究了80K-H的作用,以测试其是否为活细胞中此类缺失环节之一。荧光相关光谱显示,胰岛素刺激显著降低了80K-H的流动性。这依赖于PKCzeta的存在和PKCzeta的完整结合位点。胰岛素还以依赖于80K-H和PKCzeta的方式增加了munc18c的流动性。这些结果表明,胰岛素诱导PKCzeta、80K-H和munc18c之间的动态关联,并且80K-H可能在活细胞中作为PKCzeta和munc18c之间的关键信号连接。

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