Volume 19, No 9, Sep 2009
ISSN: 1001-0602
EISSN: 1748-7838 2018
impact factor 17.848*
(Clarivate Analytics, 2019)
Volume 19 Issue 9, September 2009: 1090-1097
ORIGINAL ARTICLES
RUVBL2, a novel AS160-binding protein, regulates insulin-stimulated GLUT4 translocation
Xiangyang Xie1,2,*, Yu Chen1,2,*, Peng Xue1, Yong Fan1,2, Yongqiang Deng1,2, Gong Peng1,2, Fuquan Yang1 and Tao Xu1
1National Key Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China
2Graduate School of the Chinese Academy of Sciences, Beijing 100101, China
Correspondence: Tao Xu, Fuquan Yang,(xutao@ibp.ac.cn; fqyang@ibp.ac.cn)
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 distributed in the cytosol. Depletion of RUVBL2 in adipocytes inhibits insulin-stimulated GLUT4 translocation and glucose uptake through reducing insulin-stimulated AS160 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.
Cell Research (2009) 19:1090-1097. doi: 10.1038/cr.2009.96 published online 16 June 2009
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