| First Author | Kimura T | Year | 2010 |
| Journal | Arch Biochem Biophys | Volume | 496 |
| Issue | 1 | Pages | 33-7 |
| PubMed ID | 20138020 | Mgi Jnum | J:158634 |
| Mgi Id | MGI:4439251 | Doi | 10.1016/j.abb.2010.01.017 |
| Citation | Kimura T, et al. (2010) Actin assembly controlled by GDP-Rab27a is essential for endocytosis of the insulin secretory membrane. Arch Biochem Biophys 496(1):33-7 |
| abstractText | 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. |
