ORIGINAL ARTICLE

Cell Research (2009): 1-8
© 2009 IBCB, SIBS, CAS All rights reserved 1001-0602/06 $ 30.00
www.nature.com/cr

RUVBL2, a novel AS160-binding protein, regulates insulin-stimulated GLUT4 translocation

Xiangyang Xie^1,2,*, Yu Chen^1,2,*, Peng Xue¹, Yong Fan^1,2, Yongqiang Deng^1,2, Gong Peng^1,2, Fuquan Yang¹ and Tao Xu¹

Correspondence: Tao Xu, E-mail: xutao@ibp.ac.cn; Fuquan Yang, E-mail: fqyang@ibp.ac.cn *These two authors contribute equally to this work.

Download as printable (PDF) file Full Text (html)file Search Medline for articles by: Xiangyang Xie

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 advance online publication 16 June 2009; doi: 10.1038/cr.2009.68

Keywords: GLUT4, AS160, RUVBL2, tandem affinity purification (TAP), adipocytes, insulin