Store-operated Ca2+ entry: evidence for a secretion-like coupling model

Cell. 1999 Aug 20;98(4):487-99. doi: 10.1016/s0092-8674(00)81977-7.

Abstract

The elusive coupling between endoplasmic reticulum (ER) Ca2+ stores and plasma membrane (PM) "store-operated" Ca2+ entry channels was probed through a novel combination of cytoskeletal modifications. Whereas coupling was unaffected by disassembly of the actin cytoskeleton, in situ redistribution of F-actin into a tight cortical layer subjacent to the PM displaced cortical ER and prevented coupling between ER and PM Ca2+ entry channels, while not affecting inositol 1,4,5-trisphosphate-mediated store release. Importantly, disassembly of the induced cortical actin layer allowed ER to regain access to the PM and reestablish coupling of Ca2+ entry channels to Ca2+ store depletion. Coupling is concluded to be mediated by a physical "secretion-like" mechanism involving close but reversible interactions between the ER and the PM.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Actins / physiology
  • Animals
  • Calcium / metabolism*
  • Calcium Channels / metabolism*
  • Calcium Signaling / physiology*
  • Cell Line, Transformed
  • Cell Membrane / metabolism*
  • Cell Membrane / ultrastructure
  • Cells, Cultured
  • Cytochalasin D / pharmacology
  • Cytoskeleton / drug effects
  • Cytoskeleton / physiology
  • Cytoskeleton / ultrastructure
  • Endoplasmic Reticulum / metabolism*
  • Inositol 1,4,5-Trisphosphate / metabolism
  • Ion Channel Gating / physiology*
  • Ion Transport
  • Microscopy, Fluorescence
  • Muscle, Smooth, Vascular / drug effects
  • Muscle, Smooth, Vascular / metabolism
  • Muscle, Smooth, Vascular / ultrastructure
  • Okadaic Acid / pharmacology
  • Oxazoles / pharmacology
  • Phosphoprotein Phosphatases / antagonists & inhibitors
  • Phosphoprotein Phosphatases / physiology
  • Rats

Substances

  • Actins
  • Calcium Channels
  • Oxazoles
  • Okadaic Acid
  • Cytochalasin D
  • calyculin A
  • Inositol 1,4,5-Trisphosphate
  • Phosphoprotein Phosphatases
  • Calcium