[Frontiers in Bioscience 7, d2072-2080, November 1, 2002]
REGULATION OF MAMMALIAN RYANODINE RECEPTORS
Department of Biochemistry and Biophysics, University of North Carolina, Chapel Hill, NC 27599-7260
TABLE OF CONTENTS
1. Abstract
2. Introduction
3. Regulation of RyRs by Ca2+
4. Modulation of Ca2+ RyR activities by monovalent ions
5. Effects by divalent cations in the absence of adenine nucleotides
6. Regulation of RyRs in the presence of adenine nucleotides
7. Modulation of RyRs by calmodulin
8. Oxidation of RyRs
9. S-Nitrosylation of RyRs
10. Phosphorylation of RyRs
11. Conclusion
12. Acknowledgement
13. References
1. ABSTRACT
Ryanodine receptors (RyRs) are large, high conductance Ca2+ channels that control the level of intracellular Ca2+ by releasing Ca2+ from an intracellular compartment, the sarco/endoplasmic reticulum. Mammalian tissues express 3 closely related ryanodine receptors (RyRs) known as skeletal muscle (RyR1), cardiac muscle (RyR2) and brain (RyR3) . The RyRs are isolated as 30S protein complexes comprised of four 560 kDa RyR2 subunits and four 12.6 kDa FK506 binding protein (FKBP12.6) subunits. Multiple endogenous effector molecules and posttranslational modifications regulate the RyRs. This chapter reviews the regulation of the mammalian RyRs by endogenous effector molecules.