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XB-ART-17017
FEBS Lett 1997 Jan 27;4021:28-32.
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The structure, function and distribution of the mouse TWIK-1 K+ channel.

Lesage F , Lauritzen I , Duprat F , Reyes R , Fink M , Heurteaux C , Lazdunski M .


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The two P domain K+ channel mTWIK-1 has been cloned from mouse brain. In Xenopus oocytes, mTWIK-1 currents are K+-selective, instantaneous, and weakly inward rectifying. These currents are blocked by Ba2+ and quinine, decreased by protein kinase C and increased by internal acidification. The apparent molecular weight of mTWIK-1 in brain is 81 kDa. A 40 kDa form is revealed after treatment with a reducing agent, strongly suggesting that native mTWIK-1 subunits dimerize via a disulfide bridge. TWIK-1 mRNA is expressed abundantly in brain and at lower levels in lung, kidney, and skeletal muscle. In situ hybridization shows that mTWIK-1 expression is restricted to a few brain regions, with the highest levels in cerebellar granule cells, brainstem, hippocampus and cerebral cortex.

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Species referenced: Xenopus
Genes referenced: kcnk1