Caveolin-3 is adjacent to a group of extradyadic ryanodine receptors

Biophys J. 2005 Sep;89(3):1893-901. doi: 10.1529/biophysj.105.064212. Epub 2005 Jun 24.


Caveolae are present in almost all cells and concentrate a wide variety of signaling molecules, receptors, transporters, and ion pumps. We have investigated the distribution of the ryanodine receptor, the Na(+)/Ca(2+) exchanger, the predominant Na(+) channel isoform rH1, and the L-type calcium channel, Ca(v)1.2, relative to the muscle-specific caveolin isoform, caveolin-3, in adult rat ventricular myocytes. Three-dimensional immunofluorescence images were deconvolved and analyzed. Caveolin-3 colocalizes with all of these molecules at the surface of the cell, but there is no significant colocalization between caveolin-3 and either the Na(+)/Ca(2+) exchanger or the Na(+) channel in the cell interior. The distribution of the surface colocalization indicates that the caveolae that colocalize with each molecule form distinct populations. This organization indicates that there are multiple populations of caveolae separable by location and occupants. In the interior of the cell, caveolin-3 shows a marked colocalization with a population of ryanodine receptors that are separate from those within the dyad. Because of their location, the signaling molecules contained within these caveolae may have preferred access to the neighboring nondyadic ryanodine receptors.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Algorithms
  • Animals
  • Arabidopsis Proteins
  • Calcium Channels, L-Type / chemistry
  • Caveolin 3 / chemistry
  • Caveolin 3 / metabolism
  • Caveolin 3 / physiology*
  • Caveolins / chemistry
  • Cell Membrane / metabolism
  • Cells, Cultured
  • Heart Ventricles / cytology
  • Image Processing, Computer-Assisted
  • Ions / chemistry
  • Male
  • Microscopy, Fluorescence
  • Monte Carlo Method
  • Muscle Cells / metabolism
  • Myocardial Contraction
  • Myocytes, Cardiac / cytology
  • Protein Binding
  • Protein Isoforms
  • Rats
  • Rats, Wistar
  • Ryanodine Receptor Calcium Release Channel / chemistry*
  • Signal Transduction
  • Sodium-Calcium Exchanger / chemistry*
  • Sodium-Calcium Exchanger / metabolism


  • Arabidopsis Proteins
  • Calcium Channels, L-Type
  • Caveolin 3
  • Caveolins
  • Ions
  • L-type calcium channel alpha(1C)
  • PHOT2 protein, Arabidopsis
  • Protein Isoforms
  • Ryanodine Receptor Calcium Release Channel
  • Sodium-Calcium Exchanger