Proteins of the Triad Junction of Skeletal Muscle

  • Anthony H. Caswell
  • Neil R. Brandt
  • Shu-Rong Wen
  • Jane A. Talvenheimo
Part of the Series of the Centro de Estudios Científicos de Santiago book series (SCEC)


The basic mechanism of excitation-contraction coupling in skeletal muscle is still not understood despite many years of active research on both the physiology and the biochemistry of the process. Several years ago we embarked on a project of identifying the constituents of the triad junction with the view that this junctional region represents not only the point of physical contact between the external and internal organelle but also the point of dynamic transmission in muscle excitation.(1,2) In 1986 we described the isolation of a protein of approximate subunit molecular weight 300,000 which spanned the gap between the transverse (T) tubule and the terminal cisternae, and therefore represented a portion of the junctional feet(3) Later work by others has demonstrated that this protein is identical to the ryanodine receptor protein and contains Ca2+ -channel activity. (4–8) This then suggests that the process of Ca2+ release from the sarcoplasmic reticulum (SR) takes place at the level of the junctional foot. What is still not clear, however, is the relationship between the T-tubule and the junctional foot. The experiments described in this chapter represent an approach to the understanding of the constituents of the T-tubule and of the junction which forms the full triadic junctional structure.


Sarcoplasmic Reticulum Ryanodine Receptor Inositol Trisphosphate Dihydropyridine Receptor Calcium Release Channel 
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  1. 1.
    Cadwell, J. J. S., and Caswell, A. H., 1982, Identification of a constituent of the junctional feet linking terminal cistemae to transverse tubules in skeletal muscle, J. Cell. Biol. 93: 543–550.PubMedCrossRefGoogle Scholar
  2. 2.
    Caswell, A. H., and Brunschwig, J-P., 1984, Identification and extraction of proteins which compose the triad junction of skeletal muscle, J. Cell Biol 99: 929–939.PubMedCrossRefGoogle Scholar
  3. 3.
    Kawamoto, R. M., Brunschwig, J-P., Kim, K. C., and Caswell, A. H., 1986, Isolation, characterization, and localization of the spanning protein from skeletal muscle triads, J. Cell Biol 103: 1405–1414.PubMedCrossRefGoogle Scholar
  4. 4.
    Inui, M., Saito, A., and Fleischer, S., 1987, Purification of the ryanodine receptor and identity with feet structures of junctional terminal cisternae of sarcoplasmic reticulum from fast skeletal muscle, J. Biol Chem. 262: 1740–1747.PubMedGoogle Scholar
  5. 5.
    Lai, F. A., Erickson, H., Block, B. A., and Meissner, G., 1987, Evidence for a Ca2+ -channel within the ryanodine receptor complex from cardiac sarcoplasmic reticulum, Biochem. Biophys. Res. Commun. 143: 704–709.PubMedCrossRefGoogle Scholar
  6. 6.
    Campbell, K. P., Knudson, C. M., Imagawa, T., Leung, A. T., Sutko, J. L., Kahl, S. D., Raab, C. R., and Madson, L., 1987, Identification and characterization of the high-affinity [3H]-ryanodine receptor of the junctional sarcoplasmic reticulum calcium release channel, J. Biol. Chem. 262: 6460–6463.PubMedGoogle Scholar
  7. 7.
    Imagawa, T., Smith, J. S., Coronado, R., and Campbell, K. P., 1987, Purified ryanodine receptor from skeletal muscle sarcoplasmic reticulum is the Ca2+ -permeable pore of the calcium release channel, J. Biol. Chem. 262: 16636–16643.PubMedGoogle Scholar
  8. 8.
    Lai, F. A., Erickson, H. P., Rousseau, E., Liu, Q-Y., and Meissner, G., 1988, Purification and reconstitution of the calcium release channel from skeletal muscle, Nature 331: 315–319.PubMedCrossRefGoogle Scholar
  9. 9.
    Corbett, A. M., Caswell, A. H., Brandt, N. R., and Brunschwig, J-P., 1985, Determinants of triad junction reformation: Isolation and identification of an endogenous promoter of junction reformation in skeletal muscle, J. Membrane Biol. 86: 267–276.CrossRefGoogle Scholar
  10. 10.
    Caswell, A. H., and Corbett, A. M., 1985, Interaction of glyceraldehyde-3-phosphate dehydrogenase with isolated microsomal subfractions of skeletal muscle, J. Biol. Chem. 260: 6892–6898.PubMedGoogle Scholar
  11. 11.
    Rios, E., and Brum, G., 1987, Involvement of dihydropyridine receptors in excitation-contraction coupling in skeletal muscle, Nature 325: 717–720.PubMedCrossRefGoogle Scholar

Copyright information

© Plenum Press, New York 1990

Authors and Affiliations

  • Anthony H. Caswell
    • 1
  • Neil R. Brandt
    • 1
  • Shu-Rong Wen
    • 1
    • 2
  • Jane A. Talvenheimo
    • 1
  1. 1.Department of PharmacologyUniversity of Miami School of MedicineMiamiUSA
  2. 2.Department of PharmacologyBeijing Medical UniversityBeijingPeople’s Republic of China

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