Recent advances in understanding the ryanodine receptor calcium release channels and their role in calcium signalling.

作者: Angela F. Dulhunty , Nicole A. Beard , Marco G. Casarotto

DOI: 10.12688/F1000RESEARCH.16434.1

关键词: Ion channelSkeletal muscleCalciumCytoplasmFunction (biology)Ryanodine receptorCell biologyCalcium signalingIon Channel ProteinChemistry

摘要: The ryanodine receptor calcium release channel is central to cytoplasmic Ca 2+ signalling in skeletal muscle, the heart, and many other tissues, including nervous system, lymphocytes, stomach, kidney, adrenal glands, ovaries, testes, thymus, lungs. ion protein massive (more than 2.2 MDa) has a structure that defied detailed determination until recent developments cryo-electron microscopy revealed much of its at near-atomic resolution. availability this high-resolution provided most significant advances understanding function past 30 years. We can now visualise molecular environment individual amino acid residues form binding sites for essential modulators determine role signalling. Importantly, structural deletions point mutations disrupt cardiac myopathies neuropathies. implications are vital importance our basis channel’s design therapies counteract effects receptor-associated disorders.

参考文章(44)
D.R. Witcher, P.S. McPherson, S.D. Kahl, T. Lewis, P. Bentley, M.J. Mullinnix, J.D. Windass, K.P. Campbell, Photoaffinity labeling of the ryanodine receptor/Ca2+ release channel with an azido derivative of ryanodine. Journal of Biological Chemistry. ,vol. 269, pp. 13076- 13079 ,(1994) , 10.1016/S0021-9258(17)36799-6
C. Callaway, A. Seryshev, J.P. Wang, K.J. Slavik, D.H. Needleman, C. Cantu, Y. Wu, T. Jayaraman, A.R. Marks, S.L. Hamilton, Localization of the high and low affinity [3H]ryanodine binding sites on the skeletal muscle Ca2+ release channel Journal of Biological Chemistry. ,vol. 269, pp. 15876- 15884 ,(1994) , 10.1016/S0021-9258(17)40762-9
Kishani M. Ranatunga, S. R. Wayne Chen, Luc Ruest, William Welch, Alan J. Williams, Quantification of the effects of a ryanodine receptor channel mutation on interaction with a ryanoid Molecular Membrane Biology. ,vol. 24, pp. 185- 193 ,(2007) , 10.1080/09687860601076522
Zhen Yan, Xiao-chen Bai, Chuangye Yan, Jianping Wu, Zhangqiang Li, Tian Xie, Wei Peng, Chang-cheng Yin, Xueming Li, Sjors H. W. Scheres, Yigong Shi, Nieng Yan, Structure of the rabbit ryanodine receptor RyR1 at near-atomic resolution Nature. ,vol. 517, pp. 50- 55 ,(2015) , 10.1038/NATURE14063
E SOBIE, S GUATIMOSIM, L GOMEZVIQUEZ, L SONG, H HARTMANN, M SALEETJAFRI, W LEDERER, The Ca2+ leak paradox and “rogue ryanodine receptors”: SR Ca2+ efflux theory and practice Progress in Biophysics & Molecular Biology. ,vol. 90, pp. 172- 185 ,(2006) , 10.1016/J.PBIOMOLBIO.2005.06.010
AF Dulhunty, Excitation-contraction coupling from the 1950s into the new millennium. Clinical and Experimental Pharmacology and Physiology. ,vol. 33, pp. 763- 772 ,(2006) , 10.1111/J.1440-1681.2006.04441.X
D. Jiang, B. Xiao, D. Yang, R. Wang, P. Choi, L. Zhang, H. Cheng, S. R. W. Chen, RyR2 mutations linked to ventricular tachycardia and sudden death reduce the threshold for store-overload-induced Ca2+ release (SOICR) Proceedings of the National Academy of Sciences of the United States of America. ,vol. 101, pp. 13062- 13067 ,(2004) , 10.1073/PNAS.0402388101
Rouslan G. Efremov, Alexander Leitner, Ruedi Aebersold, Stefan Raunser, Architecture and conformational switch mechanism of the ryanodine receptor Nature. ,vol. 517, pp. 39- 43 ,(2015) , 10.1038/NATURE13916
Takeshi Yamamoto, Roque El-Hayek, Noriaki Ikemoto, Postulated Role of Interdomain Interaction within the Ryanodine Receptor in Ca2+ Channel Regulation Journal of Biological Chemistry. ,vol. 275, pp. 11618- 11625 ,(2000) , 10.1074/JBC.275.16.11618
Sanjeewa A. Goonasekera, Nicole A. Beard, Linda Groom, Takashi Kimura, Alla D. Lyfenko, Andrew Rosenfeld, Isabelle Marty, Angela F. Dulhunty, Robert T. Dirksen, Triadin binding to the C-terminal luminal loop of the ryanodine receptor is important for skeletal muscle excitation contraction coupling. The Journal of General Physiology. ,vol. 130, pp. 365- 378 ,(2007) , 10.1085/JGP.200709790