Home > Browse Issues > Vol.37 No.1
Ryanodine Receptors: Functional Structure and Their Regulatory Factors
Fan Juan1, Yang Jin1, Zhou Xin1, Dong Zhilong2, Wang Liyang1, MengMeng Xu3, Mu Yulian4, Miyuki Nishi5,Williams Isaacs6, An Shucheng1, Hiroshi Takeshima5, Jianjie Ma7, Xu Xuehong1*
1College of Life Science, Shaanxi Normal University, Xi’an 710062, China; 22nd Hospital, Lanzhou University, Lanzhou 730030, China; 3Medical Scientist Training Program, Duke University Medical Center, Durham, NC 27705, USA; 4Institute of Animal Sciences, Chinese Academy of Agricultural Sciences, Beijing 100093, China; 5School of Pharmacology, Kyoto University, Kyoto 606-8501, Japan; 6School of Medicine, Johns Hopkins University, Baltimore, MD 21287, USA; 7School of Medicine, Ohio State University, Columbia, OH 43210, USA
Abstract: Ryanodine receptor (RyR)， located on the sarcoplasmic/endoplasmic reticulum membrane， is known as one of the few Calcium channels in charge of Calcium release within the cell. The functional RyR is a homotetramer with a total molecular mass in excess of 2 MDa and each subunit is larger than 550 kDa. There are three known mammalian isoforms of RyR each distributed in different areas of the body， RyR1 in skeletal muscle， RyR2 in cardiac muscles， and RyR3 in brain. RyR plays vital roles in many physiological functions as gated calcium channels guarding the wealth of intracellular calcium in sarcoplasmic reticulum. RyR is responsible for myocyte contractility， synaptic transmission， hormone secretion， protein folding， and programmed apoptotic/necrotic death. The fundamental role and structure of RyR were discussed in this review. Their regulatory networks through DHPR， calmodulin， calsequestrin， FKBPs and small molecular regulators， including ions ryanodine and caffeine， were discussed. The current importance of RyR in medical and pharmaceutical development was also summarized in this review.
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