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

FEBS Letters

Wilson, Justine R.²  Biden, Trevor J.²  Ludowyke, Russell I.¹ 

[1] Centre for Immunology, St. Vincent's Hospital, Sydney 2010, Australia;Garvan Institute of Medical Research, 384 Victoria St., Darlinghurst 2010, Australia

关键词: Exocytosis;    Cytoskeleton;    Pancreatic β-cell;    Myosin heavy chain;    Jasplakinolide;    MHC;    myosin heavy chain;    RLC;    regulatory light chain;    KRB;    Krebs–Ringer bicarbonate buffer;    FITC;    fluorescein isothiocyanate;    F-actin;    filamentous actin;    PBS;    phosphate-buffered saline;   

DOI  :  10.1016/S0014-5793(01)02241-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The study addressed the functional link between remodelling of the actomyosin cytoskeleton in pancreatic β-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.

【 授权许可】

Unknown