{"title":"ryanodine受体/Ca2+释放通道的调控机制及其结构研究进展","authors":"Haruo Ogawa, Nagomi Kurebayashi, Toshiko Yamazawa, Takashi Murayama","doi":"10.1007/s10974-020-09575-6","DOIUrl":null,"url":null,"abstract":"<p><p>Ryanodine receptors (RyRs) are huge homotetrameric Ca<sup>2+</sup> release channels localized to the sarcoplasmic reticulum. RyRs are responsible for the release of Ca<sup>2+</sup> 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.</p>","PeriodicalId":16422,"journal":{"name":"Journal of Muscle Research and Cell Motility","volume":"42 2","pages":"291-304"},"PeriodicalIF":1.8000,"publicationDate":"2021-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1007/s10974-020-09575-6","citationCount":"26","resultStr":"{\"title\":\"Regulatory mechanisms of ryanodine receptor/Ca<sup>2+</sup> release channel revealed by recent advancements in structural studies.\",\"authors\":\"Haruo Ogawa, Nagomi Kurebayashi, Toshiko Yamazawa, Takashi Murayama\",\"doi\":\"10.1007/s10974-020-09575-6\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>Ryanodine receptors (RyRs) are huge homotetrameric Ca<sup>2+</sup> release channels localized to the sarcoplasmic reticulum. RyRs are responsible for the release of Ca<sup>2+</sup> 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.</p>\",\"PeriodicalId\":16422,\"journal\":{\"name\":\"Journal of Muscle Research and Cell Motility\",\"volume\":\"42 2\",\"pages\":\"291-304\"},\"PeriodicalIF\":1.8000,\"publicationDate\":\"2021-06-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1007/s10974-020-09575-6\",\"citationCount\":\"26\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Journal of Muscle Research and Cell Motility\",\"FirstCategoryId\":\"99\",\"ListUrlMain\":\"https://doi.org/10.1007/s10974-020-09575-6\",\"RegionNum\":3,\"RegionCategory\":\"生物学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"2020/2/10 0:00:00\",\"PubModel\":\"Epub\",\"JCR\":\"Q4\",\"JCRName\":\"CELL BIOLOGY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Journal of Muscle Research and Cell Motility","FirstCategoryId":"99","ListUrlMain":"https://doi.org/10.1007/s10974-020-09575-6","RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"2020/2/10 0:00:00","PubModel":"Epub","JCR":"Q4","JCRName":"CELL BIOLOGY","Score":null,"Total":0}
Regulatory mechanisms of ryanodine receptor/Ca2+ release channel revealed by recent advancements in structural studies.
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.
期刊介绍：
The Journal of Muscle Research and Cell Motility has as its main aim the publication of original research which bears on either the excitation and contraction of muscle, the analysis of any one of the processes involved therein, the processes underlying contractility and motility of animal and plant cells, the toxicology and pharmacology related to contractility, or the formation, dynamics and turnover of contractile structures in muscle and non-muscle cells. Studies describing the impact of pathogenic mutations in genes encoding components of contractile structures in humans or animals are welcome, provided they offer mechanistic insight into the disease process or the underlying gene function. The policy of the Journal is to encourage any form of novel practical study whatever its specialist interest, as long as it falls within this broad field. Theoretical essays are welcome provided that they are concise and suggest practical ways in which they may be tested. Manuscripts reporting new mutations in known disease genes without validation and mechanistic insight will not be considered. It is the policy of the journal that cells lines, hybridomas and DNA clones should be made available by the developers to any qualified investigator. Submission of a manuscript for publication constitutes an agreement of the authors to abide by this principle.
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