Mode-switching of a voltage-gated cation channel is mediated by a protein kinase A-regulated tyrosine phosphatase

Nature. 1993 Dec 2;366(6454):433-8. doi: 10.1038/366433a0.


Tyrosine kinases and tyrosine phosphatases are abundant in central nervous system tissue, yet the role of these enzymes in the modulation of neuronal excitability is unknown. Patch-clamp studies of an Aplysia voltage-gated cation channel now demonstrate that a tyrosine phosphatase endogenous to excised patches determines both the gating mode of the channel and the response of the channel to protein kinase A. Moreover, a switch in gating modes similar to that triggered by the phosphatase occurs at the onset of a prolonged change in the excitability of Aplysia bag cell neurons.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Aplysia
  • Cations / metabolism*
  • Conotoxins*
  • Cyclic AMP-Dependent Protein Kinases / metabolism*
  • Ion Channel Gating*
  • Mollusk Venoms / pharmacology
  • Neurons / metabolism*
  • Nitrophenols / pharmacology
  • Organophosphorus Compounds / pharmacology
  • Phosphorylation
  • Protein Tyrosine Phosphatases / antagonists & inhibitors
  • Protein Tyrosine Phosphatases / metabolism*
  • Tyrosine / metabolism
  • Vanadates / pharmacology


  • Cations
  • Conotoxins
  • Conus textile toxin
  • Mollusk Venoms
  • Nitrophenols
  • Organophosphorus Compounds
  • nitrophenylphosphate
  • Vanadates
  • Tyrosine
  • Cyclic AMP-Dependent Protein Kinases
  • Protein Tyrosine Phosphatases