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A redistribution of actin and myosin IIA accompanies Ca 2+ ‐dependent insulin secretion
Author(s) -
Wilson Justine R.,
Ludowyke Russell I.,
Biden Trevor J.
Publication year - 2001
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(01)02241-4
Subject(s) - actin , microbiology and biotechnology , cytoskeleton , secretion , myosin , actin cytoskeleton , insulin , actin remodeling , cytoplasm , biology , chemistry , endocrinology , cell , biochemistry
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 Ca 2+ ‐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, Ca 2+ ‐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.