Premium
Non‐hydrolyzable analog of GTP induces activity of Na + channels via disassembly of cortical actin cytoskeleton
Author(s) -
Shumilina Ekaterina V,
Khaitlina Sofia Yu,
Morachevskaya Elena A,
Negulyaev Yuri A
Publication year - 2003
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(03)00663-x
Subject(s) - gtpgammas , heterotrimeric g protein , chemistry , microbiology and biotechnology , biophysics , g protein , actin cytoskeleton , actin , cytoskeleton , biochemistry , biology , signal transduction , cell
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.