Actin assembly controlled by GDP-Rab27a is essential for endocytosis of the insulin secretory membrane |
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Authors: | Toshihide Kimura |
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Institution: | Department of Pharmacology, Oita University Faculty of Medicine at Oita, Japan |
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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 β-cells. |
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Keywords: | Rab27 Coronin Endocytosis Insulin granule Actin Small GTPase |
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