Myosin Va transports dense core secretory vesicles in pancreatic MIN6 beta-cells.
Ontology highlight
ABSTRACT: The role of unconventional myosins in neuroendocrine cells is not fully understood, with involvement suggested in the movement of both secretory vesicles and mitochondria. Here, we demonstrate colocalization of myosin Va (MyoVa) with insulin in pancreatic beta-cells and show that MyoVa copurifies with insulin in density gradients and with the vesicle marker phogrin-enhanced green fluorescent protein upon fluorescence-activated sorting of vesicles. By contrast, MyoVa immunoreactivity was poorly colocalized with mitochondrial or other markers. Demonstrating an important role for MyoVa in the recruitment of secretory vesicles to the cell surface, a reduction of MyoVa protein levels achieved by RNA interference caused a significant decrease in glucose- or depolarization-stimulated insulin secr
SUBMITTER: Varadi A
PROVIDER: S-EPMC1142415 | biostudies-literature | 2005 Jun
REPOSITORIES: biostudies-literature
ACCESS DATA