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The amino-terminal disease hotspot of ryanodine receptors forms a cytoplasmic vestibule

Author

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  • Ching-Chieh Tung

    (University of British Columbia, Vancouver, British Columbia V6T 1Z3, Canada)

  • Paolo A. Lobo

    (University of British Columbia, Vancouver, British Columbia V6T 1Z3, Canada)

  • Lynn Kimlicka

    (University of British Columbia, Vancouver, British Columbia V6T 1Z3, Canada)

  • Filip Van Petegem

    (University of British Columbia, Vancouver, British Columbia V6T 1Z3, Canada)

Abstract

Muscle disease link to ryanodine Ryanodine receptors are large ion channels that mediate the release of Ca2+ from the endoplasmic or sarcoplasmic reticulum, and mutations in these receptors can lead to severe genetic conditions in both cardiac and skeletal muscles. The X-ray crystal structure of a type 1 ryanodine receptor is now reported. The exact locations of more than 50 disease-related mutations have been found in the full-length receptor. The disease mutations seem to cause misfolding of an individual domain, to destabilize interactions between the three N-terminal domains, or to otherwise affect one of the other domain interfaces.

Suggested Citation

  • Ching-Chieh Tung & Paolo A. Lobo & Lynn Kimlicka & Filip Van Petegem, 2010. "The amino-terminal disease hotspot of ryanodine receptors forms a cytoplasmic vestibule," Nature, Nature, vol. 468(7323), pages 585-588, November.
    • Handle: RePEc:nat:nature:v:468:y:2010:i:7323:d:10.1038_nature09471
    DOI: 10.1038/nature09471
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    Cited by:

    1. Yu Seby Chen & Maricela Garcia-Castañeda & Maria Charalambous & Daniela Rossi & Vincenzo Sorrentino & Filip Van Petegem, 2024. "Cryo-EM investigation of ryanodine receptor type 3," Nature Communications, Nature, vol. 15(1), pages 1-12, December.
    2. Roman Nikolaienko & Elisa Bovo & Daniel Kahn & Ryan Gracia & Thomas Jamrozik & Aleksey V. Zima, 2023. "Cysteines 1078 and 2991 cross-linking plays a critical role in redox regulation of cardiac ryanodine receptor (RyR)," Nature Communications, Nature, vol. 14(1), pages 1-11, December.

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