Glucose-induced translocation of coronin 3 regulates the retrograde transport of the secretory membrane in the pancreatic beta-cells

Biochem Biophys Res Commun. 2010 May 7;395(3):318-23. doi: 10.1016/j.bbrc.2010.03.173. Epub 2010 Apr 1.

Abstract

GTP-Rab27a is known to regulate insulin exocytosis. We have recently reported that coronin 3, which paradoxically binds GDP-Rab27a, participates in endocytosis of the insulin secretory membrane. Here, we demonstrate that glucose stimulation caused redistribution of coronin 3 in the vicinity of the plasma membrane, which was mimicked by overexpression of the GDP-Rab27a mutant or the Rab27a GAP. Glucose-induced translocation of coronin 3 was inhibited by Rab27a knock-down. The internalized phogrin, an insulin granule associated protein, located near the plasma membrane by the dominant-negative coronin 3, but the protein at the outer surface of the plasma membrane was decreased. These results indicate that glucose recruits coronin 3 near the plasma membrane, and that it regulates the retrograde transport of the secretory membrane in pancreatic beta-cells.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cell Line
  • Cell Membrane / drug effects
  • Cell Membrane / metabolism*
  • Glucose / metabolism*
  • Glucose / pharmacology
  • Insulin-Secreting Cells / drug effects
  • Insulin-Secreting Cells / metabolism*
  • Mice
  • Microfilament Proteins / metabolism*
  • Protein Transport
  • rab GTP-Binding Proteins / genetics
  • rab GTP-Binding Proteins / metabolism
  • rab27 GTP-Binding Proteins

Substances

  • Microfilament Proteins
  • rab27 GTP-Binding Proteins
  • coronin proteins
  • Rab27a protein, mouse
  • rab GTP-Binding Proteins
  • Glucose