The role of G proteins in regulation of non-voltage-gated Na+ channels in human myeloid leukemia K562 cells was studied by inside-out patch-clamp method. Na+ channels were activated by non-hydrolyzable analog of guanosine triphosphate (GTP), GTPgammaS, known to activate both heterotrimeric and small G proteins. Channel activity was not affected by aluminum fluoride that indiscriminately activates heterotrimeric G proteins. The effect of GTPgammaS was prevented by phalloidin and by G-actin, both interfering with actin disassembly, which indicates that GTPgammaS-induced channel activation was likely due to microfilament disruption. GTPgammaS-activated channels were inactivated by polymerizing actin. These data show, for the first time, that small G proteins can regulate Na+ channels, and an intracellular mechanism mediating their effect involves actin cytoskeleton rearrangements.
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