Journal
JOURNAL OF MUSCLE RESEARCH AND CELL MOTILITY
Volume 42, Issue 2, Pages 291-304Publisher
SPRINGER
DOI: 10.1007/s10974-020-09575-6
Keywords
Excitation-contraction coupling; Ryanodine receptor; Ca2+ release channel; Sarcoplasmic reticulum; Skeletal muscle; Structural biology; Molecular dynamics
Categories
Funding
- Japan Society for the Promotion of Sciences KAKENHI [JP16H04748, 19K07105, 19K07306, 19H03198, 19H03404]
- Platform Project for Supporting Drug Discovery and Life Science Research [Basis for Supporting Innovative Drug Discovery and Life Science Research (BINDS)] [JP17am0101080j0001]
- Practical Research Project for Rare/Intractable Diseases from the Japan Agency for Medical Research and Development (AMED) [19ek0109202]
- Intramural Research Grant for Neurological and Psychiatric Disorders of NCNP [29-4]
- Grants-in-Aid for Scientific Research [19H03198, 19H03404, 19K07306, 19K07105] Funding Source: KAKEN
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Recent advancements in cryo-electron microscopy have provided near-atomic structures of RyRs, leading to a better understanding of their architecture and mechanisms, including gating, regulation and disease-causing mutations.
Ryanodine receptors (RyRs) are huge homotetrameric Ca2+ release channels localized to the sarcoplasmic reticulum. RyRs are responsible for the release of Ca2+ from the SR during excitation-contraction coupling in striated muscle cells. Recent revolutionary advancements in cryo-electron microscopy have provided a number of near-atomic structures of RyRs, which have enabled us to better understand the architecture of RyRs. Thus, we are now in a new era understanding the gating, regulatory and disease-causing mechanisms of RyRs. Here we review recent advances in the elucidation of the structures of RyRs, especially RyR1 in skeletal muscle, and their mechanisms of regulation by small molecules, associated proteins and disease-causing mutations.
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