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FEBS Lett. 2003 Jul 17;547(1-3):27-31.

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

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1
Institute of Cytology RAS, 4 Tikhoretsky Ave., 194064, St. Petersburg, Russia.

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), 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.

PMID:
12860381
DOI:
10.1016/s0014-5793(03)00663-x
[Indexed for MEDLINE]
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