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We have recently shown that the rat brain Kv1.1 (RCK1)
voltage-gated K
Volume 270,
Number 24,
Issue of June 16, pp. 14611-14618, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
channel is partially phosphorylated in
its basal state in Xenopus oocytes and can be further
phosphorylated upon treatment for a short time with a cAMP analog
(Ivanina, T., Perts, T., Thornhill, W. B., Levin, G., Dascal, N., and
Lotan, I.(1994) Biochemistry 33, 8786-8792). In this
study, we show, by two-electrode voltage clamp analysis, that whereas
treatments for a short time with various cAMP analogs do not affect the
channel function, prolonged treatment with 8-bromoadenosine
3`,5`-cyclic monophosphorothioate
((S
)-8-Br-cAMPS), a membrane-permeant cAMP analog,
enhances the current amplitude. It also enhances the current amplitude
through a mutant channel that cannot be phosphorylated by protein
kinase A activation. The enhancement is inhibited in the presence of (R)-8-Br-cAMPS, a membrane-permeant protein kinase
A inhibitor. Concomitant SDS-polyacrylamide gel electrophoresis
analysis reveals that this treatment not only brings about
phosphorylation of the wild-type channel, but also increases the
amounts of both wild-type and mutant channel proteins; the latter
effect can be inhibited by cycloheximide, a protein synthesis
inhibitor. In the presence of cycloheximide, the (Sp)-8-Br-cAMPS
treatment enhances only the wild-type current amplitudes and induces
accumulation of wild-type channels in the plasma membrane of the
oocyte. In summary, prolonged treatment with (S)-8-Br-cAMPS regulates RCK1 function via two
pathways, a pathway leading to enhanced channel synthesis and a pathway
involving channel phosphorylation that directs channels to the plasma
membrane.
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