1. The structure, function and distribution of the mouse TWIK-1 K+ channel
- Author
-
Michel Fink, Inger Lauritzen, Catherine Heurteaux, Roberto V. Reyes, Florian Lesage, Fabrice Duprat, and Michel Lazdunski
- Subjects
DNA, Complementary ,Potassium Channels ,Xenopus ,Blotting, Western ,Molecular Sequence Data ,Biophysics ,In situ hybridization ,Biology ,Biochemistry ,Membrane Potentials ,Mice ,Potassium Channels, Tandem Pore Domain ,Structural Biology ,Genetics ,medicine ,Animals ,Amino Acid Sequence ,RNA, Messenger ,Molecular Biology ,Protein kinase C ,In Situ Hybridization ,Messenger RNA ,Base Sequence ,Quinine ,Skeletal muscle ,Brain ,Cell Biology ,biology.organism_classification ,Molecular biology ,Potassium channel ,Cell biology ,Molecular Weight ,medicine.anatomical_structure ,Cerebral cortex ,Barium ,Two P domains ,Oocytes ,Heterologous expression ,Xenopus oocyte ,Dimerization - Abstract
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.
- Published
- 1997