GDI-1 preferably interacts with Rab10 in insulin-stimulated GLUT4 translocation

Biochem J. 2009 Aug 13;422(2):229-35. doi: 10.1042/BJ20090624.

Abstract

Insulin stimulates GLUT4 (glucose transporter 4) translocation in adipocytes and muscles. An emerging picture is that Rab10 could bridge the gap between the insulin signalling cascade and GLUT4 translocation in adipocytes. In the present study, two potential effectors of Rab10, GDI (guanine-nucleotide-dissociation inhibitor)-1 and GDI-2, are characterized in respect to their roles in insulin-stimulated GLUT4 translocation. It is shown that both GDI-1 and GDI-2 exhibit similar distribution to GLUT4 and Rab10 at the TGN (trans-Golgi network) and periphery structures. Meanwhile, GDI-1 clearly interacts with Rab10 with higher affinity, as shown by both immunoprecipitation and in vivo FRET (fluorescence resonance energy transfer). In addition, the participation of GDIs in GLUT4 translocation is illustrated when overexpression of either GDI inhibits insulin-stimulated GLUT4 translocation in 3T3-L1 adipocytes. Taken together, we propose that GDI-1 is preferentially involved in insulin-stimulated GLUT4 translocation through facilitating Rab10 recycling.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adipocytes / drug effects
  • Adipocytes / metabolism
  • Animals
  • Cell Line
  • Glucose Transporter Type 4 / metabolism*
  • Guanine Nucleotide Dissociation Inhibitors / metabolism*
  • Guanine Nucleotide Dissociation Inhibitors / physiology
  • Humans
  • Insulin / pharmacology*
  • Mice
  • NIH 3T3 Cells
  • Protein Binding / drug effects
  • Protein Binding / physiology
  • Protein Transport
  • rab GTP-Binding Proteins / metabolism*

Substances

  • GDP dissociation inhibitor 1
  • Glucose Transporter Type 4
  • Guanine Nucleotide Dissociation Inhibitors
  • Insulin
  • Rab10 protein, human
  • rab GTP-Binding Proteins