A redistribution of actin and myosin IIA accompanies Ca2+-dependent insulin secretion

被引：44

作者：

Wilson, JR

Ludowyke, RI

Biden, TJ

机构：

[1] St Vincents Hosp, Garvan Inst Med Res, Darlinghurst, NSW 2010, Australia

[2] St Vincents Hosp, Ctr Immunol, Sydney, NSW 2010, Australia

来源：

FEBS LETTERS | 2001年 / 492卷 / 1-2期

关键词：

exocytosis; cytoskeleton; pancreatic beta-cell; myosin heavy chain; jasplakinolide;

D O I：

10.1016/S0014-5793(01)02241-4

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The study addressed the functional link between remodelling of the actomyosin cytoskeleton in pancreatic beta -cells and the regulation of insulin secretion. Confocal microscopy revealed that myosin heavy chain (MHC) IIA co-localized very well with filamentous (F)-actin in RINm5F cells but MHCIIB did not. Subcellular localization of MHCIIB was not altered by stimulation with 30 mM KCl (which evokes Ca2+-dependent insulin secretion). In contrast MHCIIA redistributed in a manner similar to F-actin, especially towards the apical surface, but also away from peripheral regions towards cell contact points on the basal surface. Finally, Ca2+-dependent insulin secretion was inhibited by stabilization of actin filaments with jasplakinolide, The results support a role for the MHCIIA/actin cytoskeleton in regulating insulin secretion. (C) 2001 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.

引用

页码：101 / +

页数：7

共 29 条

[1] Threonine phosphorylations induced by RX-871024 and insulin secretagogues in βTC6-F7 cells [J].