A mammalian two pore domain mechano-gated S-like K+ channel

EMBO J. 1998 Aug 3;17(15):4283-90. doi: 10.1093/emboj/17.15.4283.

Abstract

Aplysia S-type K+ channels of sensory neurons play a dominant role in presynaptic facilitation and behavioural sensitization. They are closed by serotonin via cAMP-dependent phosphorylation, whereas they are opened by arachidonic acid, volatile general anaesthetics and mechanical stimulation. We have identified a cloned mammalian two P domain K+ channel sharing the properties of the S channel. In addition, the recombinant channel is opened by lipid bilayer amphipathic crenators, while it is closed by cup-formers. The cytoplasmic C-terminus contains a charged region critical for chemical and mechanical activation, as well as a phosphorylation site required for cAMP inhibition.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Aplysia
  • Arachidonic Acid / pharmacology
  • COS Cells
  • Cyclic AMP-Dependent Protein Kinases / metabolism
  • Humans
  • Invertebrate Hormones / chemistry
  • Invertebrate Hormones / physiology
  • Ion Channel Gating / drug effects
  • Ion Channel Gating / physiology*
  • Molecular Sequence Data
  • Phosphorylation
  • Potassium Channels / chemistry*
  • Potassium Channels / drug effects
  • Potassium Channels / metabolism
  • Potassium Channels / physiology*
  • Potassium Channels, Tandem Pore Domain*
  • Protein Structure, Tertiary
  • Shab Potassium Channels

Substances

  • Invertebrate Hormones
  • KCNK1 protein, human
  • Potassium Channels
  • Potassium Channels, Tandem Pore Domain
  • Shab Potassium Channels
  • Shab protein, Aplysia
  • potassium channel protein TREK-1
  • Arachidonic Acid
  • Cyclic AMP-Dependent Protein Kinases