Non-hydrolyzable analog of GTP induces activity of Na+channels via disassembly of cortical actin cytoskeleton

  • Shumilina E
  • Khaitlina S
  • Morachevskaya E
 et al. 
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Abstract

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), GTPγS, 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 GTPγS was prevented by phalloidin and by G-actin, both interfering with actin disassembly, which indicates that GTPγS-induced channel activation was likely due to microfilament disruption. GTPγS-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. © 2003 Published by Elsevier Science B.V. on behalf of the Federation of European Biochemical Societies.

Author-supplied keywords

  • Actin cytoskeleton
  • G protein
  • Guanosine 5′-[γ-thio]triphosphate
  • Leukemia cell
  • Na+channel
  • Patch-clamp

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