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

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.

journal_name

Arch Biochem Biophys

journal_title

Archives of biochemistry and biophysics

authors

Kimura T,Taniguchi S,Niki I

doi

10.1016/j.abb.2010.01.017

subject

Has Abstract

pub_date

2010-04-01 00:00:00

pages

33-7

issue

1

eissn

0003-9861

issn

1096-0384

pii

S0003-9861(10)00041-X

journal_volume

496

pub_type

杂志文章

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