Structure and function of ryanodine receptors

Am J Physiol. 1994 Jun;266(6 Pt 1):C1485-504. doi: 10.1152/ajpcell.1994.266.6.C1485.


Membrane depolarization, neurotransmitters, and hormones evoke a release of Ca2+ from intracellular Ca(2+)-storing organelles like the endoplasmic reticulum and, in muscle, the sarcoplasmic reticulum (SR). In turn, the released Ca2+ serves to trigger a variety of cellular responses. The presence of Ca2+ pumps to replenish intracellular stores was described more than 20 years ago. The presence of Ca2+ channels, like the ryanodine receptor, which suddenly release the organelle-stored Ca2+, is a more recent finding. This review describes the progress made in the last five years on the structure, function, and regulation of the ryanodine receptor. Numerous reports have described the response of ryanodine receptors to cellular ions and metabolites, kinases and other proteins, and pharmacological agents. In many cases, comparative measurements have been made using Ca2+ fluxes in SR vesicles, single-channel recordings in planar bilayers, and radioligand binding assays using [3H]ryanodine. These techniques have helped to relate the activity of single ryanodine receptors to global changes in the SR Ca2+ permeability. Molecular information on functional domains within the primary structure of the ryanodine receptor is also available. There are at least three ryanodine receptor isoforms in various tissues. Some cells, such as amphibian muscle cells, express more than a single isoform. The diversity of ligands known to modulate gating and the diversity of tissues known to express the protein suggest that the ryanodine receptor has the potential to participate in many types of cell stimulus-Ca(2+)-release coupling mechanisms.

Publication types

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

MeSH terms

  • Animals
  • Calcium / metabolism
  • Calcium Channels / chemistry*
  • Calcium Channels / isolation & purification
  • Calcium Channels / metabolism*
  • Cloning, Molecular
  • Humans
  • Ion Channel Gating
  • Muscle Proteins / chemistry*
  • Muscle Proteins / isolation & purification
  • Muscle Proteins / metabolism*
  • Phosphorylation
  • Ryanodine Receptor Calcium Release Channel
  • Sarcoplasmic Reticulum / metabolism
  • Structure-Activity Relationship
  • Tissue Distribution


  • Calcium Channels
  • Muscle Proteins
  • Ryanodine Receptor Calcium Release Channel
  • Calcium