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J. Biol. Chem., Vol. 277, Issue 7, 5426-5432, February 15, 2002
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From the Department of Physiology, Semmelweis University,
H-1444 Budapest, Hungary
The potassium channels in the two-pore
domain family are widely expressed and regulate the excitability of
neurons and other excitable cells. These channels have been shown to
function as dimers, but heteromerization between the various channel
subunits has not yet been reported. Here we demonstrate that two
members of the TASK subfamily of potassium channels, TASK-1 and TASK-3, can form functional heterodimers when expressed in Xenopus
laevis oocytes. To recognize the two TASK channel types, we took
advantage of the higher sensitivity of TASK-1 over TASK-3 to
physiological pH changes and the discriminating sensitivity of TASK-3
to the cationic dye ruthenium red. These features were clearly observed when the channels were expressed individually. However, when TASK-1 and
TASK-3 were expressed together, the resulting current showed intermediate pH sensitivity and ruthenium red insensitivity
(characteristic of TASK-1), indicating the formation of TASK-1/TASK-3
heterodimers. Expression of a tandem construct in which TASK-3 and
TASK-1 were linked together yielded currents with features very similar
to those observed when coexpressing the two channels. The tandem construct also responded to AT1a angiotensin II receptor
stimulation with an inhibition that was weaker than the inhibition of
homodimeric TASK-1 and greater than that shown by TASK-3. Expression of
epitope-tagged channels in mammalian cells showed their primary
presence in the plasma membrane consistent with their function in this
location. Heteromerization of two-pore domain potassium channels may
provide a greater functional diversity and additional means by which
they can be regulated in their native tissues.
To whom correspondence should be addressed: Dept. of Physiology,
Semmelweis University, P.O. Box 259, H-1444 Budapest, Hungary. Tel.:
36-1-266-2755, Ext. 4079; Fax: 36-1-266-6504; E-mail:
enyedi@puskin.sote.hu.
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