The structure, function and distribution of the mouse TWIK-1 K+ channel

FEBS Lett. 1997 Jan 27;402(1):28-32. doi: 10.1016/s0014-5793(96)01491-3.


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Barium / pharmacology
  • Base Sequence
  • Blotting, Western
  • Brain / metabolism*
  • DNA, Complementary / genetics
  • Dimerization
  • In Situ Hybridization
  • Membrane Potentials
  • Mice
  • Molecular Sequence Data
  • Molecular Weight
  • Oocytes
  • Potassium Channels / chemistry*
  • Potassium Channels / genetics
  • Potassium Channels / metabolism
  • Potassium Channels, Tandem Pore Domain*
  • Quinine / pharmacology
  • RNA, Messenger / genetics
  • RNA, Messenger / metabolism
  • Xenopus


  • DNA, Complementary
  • Kcnk1 protein, mouse
  • Potassium Channels
  • Potassium Channels, Tandem Pore Domain
  • RNA, Messenger
  • Barium
  • Quinine

Associated data

  • GENBANK/AF033017