In fat and muscle cells, insulin-stimulated glucose uptake is mainly mediated by glucose transporter 4 （GLUT4）, which translocates from intracellular compartments to the cell surface in response to insulin stimulati...In fat and muscle cells, insulin-stimulated glucose uptake is mainly mediated by glucose transporter 4 （GLUT4）, which translocates from intracellular compartments to the cell surface in response to insulin stimulation. AS160 is one of the substrates of Akt and plays important roles in insulin-regulated GLUT4 translocation. In this study, RuvB- like protein 2 （RUVBL2） is identified as a new AS160-binding protein using mammalian tandem affinity purification （TAP） combined with mass spectrometry. In 3T3-L1 adipocytes, RUVBL2 is highly expressed and is mainly distrib- uted in the cytosol. Depletion of RUVBL2 in adipocytes inhibits insulin-stimulated GLUT4 translocation and glucose uptake through reducing insulin-stimulated ASI60 phosphorylation. However, introduction of human RUVBL2 can reverse this inhibitory effect. These data suggest that RUVBL2 plays an important role in insulin-stimulated GLUT4 translocation through its interaction with AS160.展开更多
基金Acknowledgments We would like to thank our colleagues, Prof Hong Tang for providing pCTAP-A expression vector and Dr Li Zheng for valuable discussion. This work is supported by the National Natural Science Foundation of China （NO. 30630020）, the National Basic Research Program of China （2004CB720000）, and the CAS Proj- ect （KSCX 1-YW-02-1）.
文摘In fat and muscle cells, insulin-stimulated glucose uptake is mainly mediated by glucose transporter 4 （GLUT4）, which translocates from intracellular compartments to the cell surface in response to insulin stimulation. AS160 is one of the substrates of Akt and plays important roles in insulin-regulated GLUT4 translocation. In this study, RuvB- like protein 2 （RUVBL2） is identified as a new AS160-binding protein using mammalian tandem affinity purification （TAP） combined with mass spectrometry. In 3T3-L1 adipocytes, RUVBL2 is highly expressed and is mainly distrib- uted in the cytosol. Depletion of RUVBL2 in adipocytes inhibits insulin-stimulated GLUT4 translocation and glucose uptake through reducing insulin-stimulated ASI60 phosphorylation. However, introduction of human RUVBL2 can reverse this inhibitory effect. These data suggest that RUVBL2 plays an important role in insulin-stimulated GLUT4 translocation through its interaction with AS160.
