Actin assembly controlled by GDP-Rab27a is essential for endocytosis of the insulin secretory membrane

Arch Biochem Biophys. 2010 Apr 1;496(1):33-7. doi: 10.1016/j.abb.2010.01.017. Epub 2010 Feb 4.

Abstract

We have recently reported that GDP-bound Rab27a regulates endocytosis of the insulin secretory membrane via its binding to coronin 3, an actin-binding protein. The aim of this study was to examine the participation of actin assembly in the Rab27a-dependent regulation of endocytosis using a pancreatic beta cell line, MIN6. Coronin 3 promoted F-actin bundling only in the presence of GDP-Rab27a. This effect was independent of coronin-3-binding to the actin-related proteins 2 and 3 (Arp2/3). Uptake of anti-phogrin-lumen antibody into MIN6 was inhibited by anti-coronin-3-C antibody which recognizes the actin-binding site. This inhibition was also observed with coronin-3-R28D, which lacks in actin binding. These results suggest that coronin 3 is a genuine GDP-Rab27a effector, and that controls endocytosis of the secretory membrane via modulating actin assembly in pancreatic beta-cells.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Actins / chemistry
  • Actins / metabolism*
  • Animals
  • Binding Sites
  • COS Cells
  • Cell Membrane / metabolism*
  • Chlorocebus aethiops
  • Endocytosis*
  • Guanosine Diphosphate / metabolism*
  • Insulin / metabolism*
  • Insulin Secretion
  • Mice
  • Microfilament Proteins / metabolism
  • Protein Binding
  • Protein Multimerization
  • Protein Structure, Quaternary
  • rab GTP-Binding Proteins / metabolism*
  • rab27 GTP-Binding Proteins

Substances

  • Actins
  • Insulin
  • Microfilament Proteins
  • rab27 GTP-Binding Proteins
  • coronin proteins
  • Guanosine Diphosphate
  • Rab27a protein, mouse
  • rab GTP-Binding Proteins