Core skeletal muscle ryanodine receptor calcium release complex

Marco Casarotto, Lan Wei-LaPierre, Nicole BEARD

    Research output: Contribution to journalArticle

    12 Citations (Scopus)

    Abstract

    The core skeletal muscle ryanodine receptor (RyR1) calcium release complex extends through three compartments of the muscle fibre, linking the extracellular environment through the cytoplasmic junctional gap to the lumen of the internal sarcoplasmic reticulum (SR) calcium store. The protein complex is essential for skeletal excitation-contraction (EC)-coupling and skeletal muscle function. Its importance is highlighted by perinatal death if any one of the EC-coupling components are missing and by myopathies associated with mutation of any of the proteins. The proteins essential for EC-coupling include the DHPR a1S subunit in the transverse tubule membrane, the DHPR ß1a subunit in the cytosol and the RyR1 ion channel in the SR membrane. The other core proteins are triadin and junctin and calsequestrin, associated mainly with SR. These SR proteins are not essential for survival but exert structural and functional influences that modify the gain of EC-coupling and maintain normal muscle function. This review summarises our current knowledge of the individual protein/protein interactions within the core complex and their overall contribution to EC-coupling. We highlight significant areas that provide a continuing challenge for the field. Additional important components of the Ca2+ release complex, such as FKBP12, calmodulin, S100A1 and Stac3 are identified and reviewed elsewhere.
    Original languageEnglish
    Pages (from-to)3-12
    Number of pages10
    JournalClinical and Experimental Pharmacology and Physiology
    Volume44
    Issue number1
    DOIs
    Publication statusPublished - 2017

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    Ryanodine Receptor Calcium Release Channel
    Excitation Contraction Coupling
    Skeletal Muscle
    Sarcoplasmic Reticulum
    Proteins
    Tacrolimus Binding Protein 1A
    Calsequestrin
    Calcium
    Muscles
    Membranes
    Muscular Diseases
    Calmodulin
    Ion Channels
    Cytosol
    Mutation

    Cite this

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    title = "Core skeletal muscle ryanodine receptor calcium release complex",
    abstract = "The core skeletal muscle ryanodine receptor (RyR1) calcium release complex extends through three compartments of the muscle fibre, linking the extracellular environment through the cytoplasmic junctional gap to the lumen of the internal sarcoplasmic reticulum (SR) calcium store. The protein complex is essential for skeletal excitation-contraction (EC)-coupling and skeletal muscle function. Its importance is highlighted by perinatal death if any one of the EC-coupling components are missing and by myopathies associated with mutation of any of the proteins. The proteins essential for EC-coupling include the DHPR a1S subunit in the transverse tubule membrane, the DHPR {\ss}1a subunit in the cytosol and the RyR1 ion channel in the SR membrane. The other core proteins are triadin and junctin and calsequestrin, associated mainly with SR. These SR proteins are not essential for survival but exert structural and functional influences that modify the gain of EC-coupling and maintain normal muscle function. This review summarises our current knowledge of the individual protein/protein interactions within the core complex and their overall contribution to EC-coupling. We highlight significant areas that provide a continuing challenge for the field. Additional important components of the Ca2+ release complex, such as FKBP12, calmodulin, S100A1 and Stac3 are identified and reviewed elsewhere.",
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    Core skeletal muscle ryanodine receptor calcium release complex. / Casarotto, Marco; Wei-LaPierre, Lan; BEARD, Nicole.

    In: Clinical and Experimental Pharmacology and Physiology, Vol. 44, No. 1, 2017, p. 3-12.

    Research output: Contribution to journalArticle

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    AU - Wei-LaPierre, Lan

    AU - BEARD, Nicole

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    AB - The core skeletal muscle ryanodine receptor (RyR1) calcium release complex extends through three compartments of the muscle fibre, linking the extracellular environment through the cytoplasmic junctional gap to the lumen of the internal sarcoplasmic reticulum (SR) calcium store. The protein complex is essential for skeletal excitation-contraction (EC)-coupling and skeletal muscle function. Its importance is highlighted by perinatal death if any one of the EC-coupling components are missing and by myopathies associated with mutation of any of the proteins. The proteins essential for EC-coupling include the DHPR a1S subunit in the transverse tubule membrane, the DHPR ß1a subunit in the cytosol and the RyR1 ion channel in the SR membrane. The other core proteins are triadin and junctin and calsequestrin, associated mainly with SR. These SR proteins are not essential for survival but exert structural and functional influences that modify the gain of EC-coupling and maintain normal muscle function. This review summarises our current knowledge of the individual protein/protein interactions within the core complex and their overall contribution to EC-coupling. We highlight significant areas that provide a continuing challenge for the field. Additional important components of the Ca2+ release complex, such as FKBP12, calmodulin, S100A1 and Stac3 are identified and reviewed elsewhere.

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