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Submitted on September 25, 2002
Accepted on January 10, 2003
1 Department of Biochemistry & Molecular Biology, Center for Diabetes Research, Indiana University School of Medicine, Indianapolis, IN 46202; Department of Physiology & Biophysics, The University of Iowa, Iowa City, IA 52242; Laboratoires Jeantet, University Medical Center, Geneva, Switzerland
* To whom correspondence should be addressed. E-mail: dthurmon{at}iupui.edu.
The actin monomer sequestering agent latrunculin B depolymerized beta cell cortical actin which resulted in increased glucose-stimulated insulin secretion in both cultured MIN6 beta cells and isolated rat islet cells. In perifused islets, latrunculin B treatment increased both first and second phase glucose-stimulated insulin secretion without any significant effect on total insulin content. This increase in secretion was independent of calcium regulation, since latrunculin B also potentiated calcium-stimulated insulin secretion in permeabilized MIN6 cells. Confocal immunofluorescent microscopy revealed a redistribution of insulin granules to the cell periphery in response to glucose or latrunculin B, which correlated with a reduction in phalloidin staining of cortical actin. Moreover, the t-SNARE proteins Syntaxin 1 and SNAP-25 co-immunoprecipitated polymerized actin from unstimulated MIN6 cells. Glucose stimulation transiently decreased the amount of actin co-immunoprecipitated with Syntaxin 1 and SNAP-25, and latrunculin B treatment fully ablated the co-immunoprecipitation. In contrast, the actin stabilizing agent jasplakinolide increased the amount of actin co-immunoprecipitated with the t-SNARE complex and prevented its dissociation after glucose stimulation. These data suggest a mechanism whereby glucose modulates beta cell cortical actin organization and disrupts the interaction of polymerized actin with the plasma membrane t-SNARE complex at a distal regulatory step in the exocytosis of insulin granules.
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