A cytoskeletal mechanism for Ca2+ channel metabolic dependence and inactivation by intracellular Ca2+

Neuron. 1993 May;10(5):797-804. doi: 10.1016/0896-6273(93)90196-x.


Many different types of voltage-dependent Ca2+ channels inactivate when intracellular ATP declines or intracellular Ca2+ rises. An inside-out, patch-clamp technique was applied to the Ca2+ channels of Lymnaea neurons to determine the mechanism(s) underlying these two phenomena. Although no evidence was found for a phosphorylation mechanism, agents that act on the cytoskeleton were found to alter Ca2+ channel activity. The cytoskeletal disrupters colchicine and cytochalasin B were found to speed Ca2+ channel decline in ATP, whereas the cytoskeletal stabilizers taxol and phalloidin were found to prolong Ca2+ channel activity without ATP. In addition, cytoskeletal stabilizers reduced Ca(2+)-dependent channel inactivation, suggesting that both channel metabolic dependence and Ca(2+)-dependent inactivation result from a cytoskeletal interaction.

Publication types

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

MeSH terms

  • Actins / pharmacology
  • Adenosine Triphosphate / metabolism
  • Animals
  • Barium / metabolism
  • Calcium / pharmacology*
  • Calcium Channels / drug effects
  • Calcium Channels / metabolism*
  • Colchicine / pharmacology
  • Cytochalasin B / pharmacology
  • Cytoskeleton / drug effects
  • Cytoskeleton / physiology*
  • Electric Conductivity
  • Lymnaea
  • Paclitaxel / pharmacology
  • Phalloidine / pharmacology
  • Phosphorylation
  • Tubulin / pharmacology


  • Actins
  • Calcium Channels
  • Tubulin
  • Phalloidine
  • Barium
  • Cytochalasin B
  • Adenosine Triphosphate
  • Paclitaxel
  • Colchicine
  • Calcium