메뉴 건너뛰기




Volumn 26, Issue 9, 2016, Pages 995-1006

The Central domain of RyR1 is the transducer for long-range allosteric gating of channel opening

Author keywords

calcium channel; excitation contraction coupling; membrane transport; RyR1; voltage gated calcium channels

Indexed keywords

RYANODINE RECEPTOR;

EID: 84980015412     PISSN: 10010602     EISSN: 17487838     Source Type: Journal    
DOI: 10.1038/cr.2016.89     Document Type: Article
Times cited : (89)

References (48)
  • 1
    • 0022395442 scopus 로고
    • The calcium-ryanodine receptor complex of skeletal and cardiac muscle
    • Pessah IN, Waterhouse AL, Casida JE. The calcium-ryanodine receptor complex of skeletal and cardiac muscle. Biochem Biophys Res Commun 1985; 128: 449-456
    • (1985) Biochem Biophys Res Commun , vol.128 , pp. 449-456
    • Pessah, I.N.1    Waterhouse, A.L.2    Casida, J.E.3
  • 2
    • 0023644484 scopus 로고
    • Purification of the ryanodine receptor and identity with feet structures of junctional terminal cisternae of sarcoplasmic reticulum from fast skeletal muscle
    • Inui M, Saito A, Fleischer S. Purification of the ryanodine receptor and identity with feet structures of junctional terminal cisternae of sarcoplasmic reticulum from fast skeletal muscle. J Biol Chem 1987; 262: 1740-1747
    • (1987) J Biol Chem , vol.262 , pp. 1740-1747
    • Inui, M.1    Saito, A.2    Fleischer, S.3
  • 3
    • 0023903046 scopus 로고
    • Purification and reconstitution of the calcium release channel from skeletal muscle
    • Lai FA, Erickson HP, Rousseau E, Liu QY, Meissner G. Purification and reconstitution of the calcium release channel from skeletal muscle. Nature 1988; 331: 315-319
    • (1988) Nature , vol.331 , pp. 315-319
    • Lai, F.A.1    Erickson, H.P.2    Rousseau, E.3    Liu, Q.Y.4    Meissner, G.5
  • 4
    • 79952478406 scopus 로고    scopus 로고
    • Ryanodine receptors: Structure, expression, molecular details, and function in calcium release
    • Lanner JT, Georgiou DK, Joshi AD, Hamilton SL. Ryanodine receptors: structure, expression, molecular details, and function in calcium release. Cold Spring Harb Perspect Biol 2010; 2: a003996
    • (2010) Cold Spring Harb Perspect Biol , vol.2 , pp. a003996
    • Lanner, J.T.1    Georgiou, D.K.2    Joshi, A.D.3    Hamilton, S.L.4
  • 5
    • 0024318429 scopus 로고
    • Primary structure and expression from complementary DNA of skeletal muscle ryanodine receptor
    • Takeshima H, Nishimura S, Matsumoto T, et al. Primary structure and expression from complementary DNA of skeletal muscle ryanodine receptor. Nature 1989; 339: 439-445
    • (1989) Nature , vol.339 , pp. 439-445
    • Takeshima, H.1    Nishimura, S.2    Matsumoto, T.3
  • 6
    • 0036877140 scopus 로고    scopus 로고
    • Molecular genetics of ryanodine receptors Ca2+-release channels
    • Rossi D, Sorrentino V. Molecular genetics of ryanodine receptors Ca2+-release channels. Cell Calcium 2002; 32: 307-319
    • (2002) Cell Calcium , vol.32 , pp. 307-319
    • Rossi, D.1    Sorrentino, V.2
  • 7
    • 0025171580 scopus 로고
    • Molecular cloning of cDNA encoding the Ca2+release channel (ryanodine receptor) of rabbit cardiac muscle sarcoplasmic reticulum
    • Otsu K, Willard HF, Khanna VK, Zorzato F, Green NM, MacLennan DH. Molecular cloning of cDNA encoding the Ca2+release channel (ryanodine receptor) of rabbit cardiac muscle sarcoplasmic reticulum. J Biol Chem 1990; 265: 13472-13483
    • (1990) J Biol Chem , vol.265 , pp. 13472-13483
    • Otsu, K.1    Willard, H.F.2    Khanna, V.K.3    Zorzato, F.4    Green, N.M.5    MacLennan, D.H.6
  • 8
    • 0025123804 scopus 로고
    • Primary structure and functional expression from cDNA of the cardiac ryanodine receptor/calcium release channel
    • Nakai J, Imagawa T, Hakamat Y, Shigekawa M, Takeshima H, Numa S. Primary structure and functional expression from cDNA of the cardiac ryanodine receptor/calcium release channel. FEBS Lett 1990; 271: 169-177
    • (1990) FEBS Lett , vol.271 , pp. 169-177
    • Nakai, J.1    Imagawa, T.2    Hakamat, Y.3    Shigekawa, M.4    Takeshima, H.5    Numa, S.6
  • 9
    • 0026471048 scopus 로고
    • Primary structure and distribution of a novel ryanodine receptor/calcium release channel from rabbit brain
    • Hakamata Y, Nakai J, Takeshima H, Imoto K. Primary structure and distribution of a novel ryanodine receptor/calcium release channel from rabbit brain. FEBS Lett 1992; 312: 229-235
    • (1992) FEBS Lett , vol.312 , pp. 229-235
    • Hakamata, Y.1    Nakai, J.2    Takeshima, H.3    Imoto, K.4
  • 10
    • 0026589932 scopus 로고
    • Cryo-EM of the native structure of the calcium release channel/ryanodine receptor from sarcoplasmic reticulum
    • Radermacher M, Wagenknecht T, Grassucci R, et al. Cryo-EM of the native structure of the calcium release channel/ryanodine receptor from sarcoplasmic reticulum. Biophys J 1992; 61: 936-940
    • (1992) Biophys J , vol.61 , pp. 936-940
    • Radermacher, M.1    Wagenknecht, T.2    Grassucci, R.3
  • 11
    • 0028004249 scopus 로고
    • Cryo-electron microscopy and three-dimensional reconstruction of the calcium release channel/ryanodine receptor from skeletal muscle
    • Radermacher M, Rao V, Grassucci R, et al. Cryo-electron microscopy and three-dimensional reconstruction of the calcium release channel/ryanodine receptor from skeletal muscle. J Cell Biol 1994; 127: 411-423
    • (1994) J Cell Biol , vol.127 , pp. 411-423
    • Radermacher, M.1    Rao, V.2    Grassucci, R.3
  • 12
    • 22444444618 scopus 로고    scopus 로고
    • Internal structure and visualization of transmembrane domains of the RyR1 calcium release channel by cryo-EM
    • Samso M, Wagenknecht T, Allen PD. Internal structure and visualization of transmembrane domains of the RyR1 calcium release channel by cryo-EM. Nat Struct Mol Biol 2005; 12: 539-544
    • (2005) Nat Struct Mol Biol , vol.12 , pp. 539-544
    • Samso, M.1    Wagenknecht, T.2    Allen, P.D.3
  • 13
    • 47749109511 scopus 로고    scopus 로고
    • Subnanometer-resolution electron cryomicroscopy-based domain models for the cytoplasmic region of skeletal muscle RyR channel
    • Serysheva, II, Ludtke SJ, Baker ML, et al. Subnanometer-resolution electron cryomicroscopy-based domain models for the cytoplasmic region of skeletal muscle RyR channel. Proc Natl Acad Sci USA 2008; 105: 9610-9615
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 9610-9615
    • Serysheva, I.I.1    Ludtke, S.J.2    Baker, M.L.3
  • 14
    • 67649637588 scopus 로고    scopus 로고
    • Coordinated movement of cytoplasmic and transmembrane domains of RyR1 upon gating
    • Samso M, Feng W, Pessah IN, Allen PD. Coordinated movement of cytoplasmic and transmembrane domains of RyR1 upon gating. PLoS Biol 2009; 7: e85
    • (2009) PLoS Biol , vol.7 , pp. e85
    • Samso, M.1    Feng, W.2    Pessah, I.N.3    Allen, P.D.4
  • 15
    • 0141532146 scopus 로고    scopus 로고
    • Stoichiometric phosphorylation of cardiac ryanodine receptor on serine 2809 by calmodulin-dependent kinase II and protein kinase A
    • Rodriguez P, Bhogal MS, Colyer J. Stoichiometric phosphorylation of cardiac ryanodine receptor on serine 2809 by calmodulin-dependent kinase II and protein kinase A. J Biol Chem 2003; 278: 38593-38600
    • (2003) J Biol Chem , vol.278 , pp. 38593-38600
    • Rodriguez, P.1    Bhogal, M.S.2    Colyer, J.3
  • 16
    • 3042763171 scopus 로고    scopus 로고
    • Ca2+/calmodulin-dependent protein kinase II phosphorylation regulates the cardiac ryanodine receptor
    • Wehrens XH, Lehnart SE, Reiken SR, Marks AR. Ca2+/calmodulin-dependent protein kinase II phosphorylation regulates the cardiac ryanodine receptor. Circ Res 2004; 94: e61-e70
    • (2004) Circ Res , vol.94 , pp. e61-e70
    • Wehrens, X.H.1    Lehnart, S.E.2    Reiken, S.R.3    Marks, A.R.4
  • 17
    • 34548644786 scopus 로고    scopus 로고
    • Modulation of the ryanodine receptor and intracellular calcium
    • Zalk R, Lehnart SE, Marks AR. Modulation of the ryanodine receptor and intracellular calcium. Annu Rev Biochem 2007; 76: 367-385
    • (2007) Annu Rev Biochem , vol.76 , pp. 367-385
    • Zalk, R.1    Lehnart, S.E.2    Marks, A.R.3
  • 18
    • 84866395344 scopus 로고    scopus 로고
    • Ryanodine receptors: Structure and function
    • Van Petegem F. Ryanodine receptors: structure and function. J Biol Chem 2012; 287: 31624-31632
    • (2012) J Biol Chem , vol.287 , pp. 31624-31632
    • Van Petegem, F.1
  • 19
    • 0031035586 scopus 로고    scopus 로고
    • Regulation of skeletal muscle Ca2+ release channel (ryanodine receptor) by Ca2+ and monovalent cations and anions
    • Meissner G, Rios E, Tripathy A, Pasek DA. Regulation of skeletal muscle Ca2+ release channel (ryanodine receptor) by Ca2+ and monovalent cations and anions. J Biol Chem 1997; 272: 1628-1638
    • (1997) J Biol Chem , vol.272 , pp. 1628-1638
    • Meissner, G.1    Rios, E.2    Tripathy, A.3    Pasek, D.A.4
  • 20
    • 0035893823 scopus 로고    scopus 로고
    • Regulation of the calcium release channel from rabbit skeletal muscle by the nucleotides ATP, AMP, IMP and adenosine
    • Laver DR, Lenz GK, Lamb GD. Regulation of the calcium release channel from rabbit skeletal muscle by the nucleotides ATP, AMP, IMP and adenosine. J Physiol 2001; 537: 763-778
    • (2001) J Physiol , vol.537 , pp. 763-778
    • Laver, D.R.1    Lenz, G.K.2    Lamb, G.D.3
  • 21
    • 0024580990 scopus 로고
    • Positive cooperativity of ryanodine binding to the calcium release channel of sarcoplasmic reticulum from heart and skeletal muscle
    • McGrew SG, Wolleben C, Siegl P, Inui M, Fleischer S. Positive cooperativity of ryanodine binding to the calcium release channel of sarcoplasmic reticulum from heart and skeletal muscle. Biochemistry 1989; 28: 1686-1691
    • (1989) Biochemistry , vol.28 , pp. 1686-1691
    • McGrew, S.G.1    Wolleben, C.2    Siegl, P.3    Inui, M.4    Fleischer, S.5
  • 23
    • 84922479751 scopus 로고    scopus 로고
    • Structure of the rabbit ryanodine receptor RyR1 at near-Atomic resolution
    • Yan Z, Bai XC, Yan C, et al. Structure of the rabbit ryanodine receptor RyR1 at near-Atomic resolution. Nature 2015; 517: 50-55
    • (2015) Nature , vol.517 , pp. 50-55
    • Yan, Z.1    Bai, X.C.2    Yan, C.3
  • 24
    • 77955335145 scopus 로고    scopus 로고
    • Armadillo-repeat protein functions: Questions for little creatures
    • Tewari R, Bailes E, Bunting KA, Coates JC. Armadillo-repeat protein functions: questions for little creatures. Trends Cell Biol 2010; 20: 470-481
    • (2010) Trends Cell Biol , vol.20 , pp. 470-481
    • Tewari, R.1    Bailes, E.2    Bunting, K.A.3    Coates, J.C.4
  • 25
    • 84922481432 scopus 로고    scopus 로고
    • Architecture and conformational switch mechanism of the ryanodine receptor
    • Efremov RG, Leitner A, Aebersold R, Raunser S. Architecture and conformational switch mechanism of the ryanodine receptor. Nature 2015; 517: 39-43
    • (2015) Nature , vol.517 , pp. 39-43
    • Efremov, R.G.1    Leitner, A.2    Aebersold, R.3    Raunser, S.4
  • 26
    • 84940100060 scopus 로고    scopus 로고
    • Channel gating dependence on pore lining helix glycine residues in skeletal muscle ryanodine receptor
    • Mei Y, Xu L, Mowrey DD, et al. Channel gating dependence on pore lining helix glycine residues in skeletal muscle ryanodine receptor. J Biol Chem 2015; 290: 17535-17545
    • (2015) J Biol Chem , vol.290 , pp. 17535-17545
    • Mei, Y.1    Xu, L.2    Mowrey, D.D.3
  • 27
    • 0023113884 scopus 로고
    • Involvement of dihydropyridine receptors in excitation-contraction coupling in skeletal muscle
    • Rios E, Brum G. Involvement of dihydropyridine receptors in excitation-contraction coupling in skeletal muscle. Nature 1987; 325: 717-720
    • (1987) Nature , vol.325 , pp. 717-720
    • Rios, E.1    Brum, G.2
  • 28
    • 0025288735 scopus 로고
    • Regions of the skeletal muscle dihydropyridine receptor critical for excitation-contraction coupling
    • Tanabe T, Beam KG, Adams BA, Niidome T, Numa S. Regions of the skeletal muscle dihydropyridine receptor critical for excitation-contraction coupling. Nature 1990; 346: 567-569
    • (1990) Nature , vol.346 , pp. 567-569
    • Tanabe, T.1    Beam, K.G.2    Adams, B.A.3    Niidome, T.4    Numa, S.5
  • 29
    • 0032839459 scopus 로고    scopus 로고
    • Shape, size, and distribution of Ca(2+) release units and couplons in skeletal and cardiac muscles
    • Franzini-Armstrong C, Protasi F, Ramesh V. Shape, size, and distribution of Ca(2+) release units and couplons in skeletal and cardiac muscles. Biophys J 1999; 77: 1528-1539
    • (1999) Biophys J , vol.77 , pp. 1528-1539
    • Franzini-Armstrong, C.1    Protasi, F.2    Ramesh, V.3
  • 30
    • 0030912648 scopus 로고    scopus 로고
    • Coordinated incorporation of skeletal muscle dihydropyridine receptors and ryanodine receptors in peripheral couplings of BC3H1 cells
    • Protasi F, Franzini-Armstrong C, Flucher BE. Coordinated incorporation of skeletal muscle dihydropyridine receptors and ryanodine receptors in peripheral couplings of BC3H1 cells. J Cell Biol 1997; 137: 859-870
    • (1997) J Cell Biol , vol.137 , pp. 859-870
    • Protasi, F.1    Franzini-Armstrong, C.2    Flucher, B.E.3
  • 31
    • 0032559585 scopus 로고    scopus 로고
    • Role of ryanodine receptors in the assembly of calcium release units in skeletal muscle
    • Protasi F, Franzini-Armstrong C, Allen PD. Role of ryanodine receptors in the assembly of calcium release units in skeletal muscle. J Cell Biol 1998; 140: 831-842
    • (1998) J Cell Biol , vol.140 , pp. 831-842
    • Protasi, F.1    Franzini-Armstrong, C.2    Allen, P.D.3
  • 32
    • 41149098918 scopus 로고    scopus 로고
    • Ryanodine receptor arrays: Not just a pretty pattern?
    • Yin CC, D'Cruz LG, Lai FA. Ryanodine receptor arrays: not just a pretty pattern? Trends Cell Biol 2008; 18: 149-156
    • (2008) Trends Cell Biol , vol.18 , pp. 149-156
    • Yin, C.C.1    D'Cruz, L.G.2    Lai, F.A.3
  • 33
    • 0141994822 scopus 로고    scopus 로고
    • Amino acids 1-1, 680 of ryanodine receptor type 1 hold critical determinants of skeletal type for excitation-contraction coupling Role of divergence domain D2
    • Perez CF, Mukherjee S, Allen PD. Amino acids 1-1, 680 of ryanodine receptor type 1 hold critical determinants of skeletal type for excitation-contraction coupling. Role of divergence domain D2. J Biol Chem 2003; 278: 39644-39652
    • (2003) J Biol Chem , vol.278 , pp. 39644-39652
    • Perez, C.F.1    Mukherjee, S.2    Allen, P.D.3
  • 34
    • 84950282257 scopus 로고    scopus 로고
    • Structure of the voltage-gated calcium channel Cav1.1 complex
    • Wu J, Yan Z, Li Z, et al. Structure of the voltage-gated calcium channel Cav1.1 complex. Science 2015; 350: aad2395
    • (2015) Science , vol.350 , pp. aad2395
    • Wu, J.1    Yan, Z.2    Li, Z.3
  • 35
    • 84955307962 scopus 로고    scopus 로고
    • Sampling the conformational space of the catalytic subunit of human gamma-secretase
    • Bai XC, Rajendra E, Yang G, Shi Y, Scheres SH. Sampling the conformational space of the catalytic subunit of human gamma-secretase. eLife 2015; 4: e11182
    • (2015) ELife , vol.4 , pp. e11182
    • Bai, X.C.1    Rajendra, E.2    Yang, G.3    Shi, Y.4    Scheres, S.H.5
  • 36
    • 0038441501 scopus 로고    scopus 로고
    • Accurate determination of local defocus and specimen tilt in electron microscopy
    • Mindell JA, Grigorieff N. Accurate determination of local defocus and specimen tilt in electron microscopy. J Struct Biol 2003; 142: 334-347
    • (2003) J Struct Biol , vol.142 , pp. 334-347
    • Mindell, J.A.1    Grigorieff, N.2
  • 37
    • 84868444740 scopus 로고    scopus 로고
    • RELION: Implementation of a Bayesian approach to cryo-EM structure determination
    • Scheres SH. RELION: implementation of a Bayesian approach to cryo-EM structure determination. J Struct Biol 2012; 180: 519-530
    • (2012) J Struct Biol , vol.180 , pp. 519-530
    • Scheres, S.H.1
  • 38
    • 84922727036 scopus 로고    scopus 로고
    • Semi-Automated selection of cryo-EM particles in RELION-1.3
    • Scheres SH. Semi-Automated selection of cryo-EM particles in RELION-1.3. J Struct Biol 2015; 189: 114-122
    • (2015) J Struct Biol , vol.189 , pp. 114-122
    • Scheres, S.H.1
  • 39
    • 84880607763 scopus 로고    scopus 로고
    • High-resolution noise substitution to measure overfitting and validate resolution in 3D structure determination by single particle electron cryomicroscopy
    • Chen S, McMullan G, Faruqi AR, et al. High-resolution noise substitution to measure overfitting and validate resolution in 3D structure determination by single particle electron cryomicroscopy. Ultramicroscopy 2013; 135: 24-35
    • (2013) Ultramicroscopy , vol.135 , pp. 24-35
    • Chen, S.1    McMullan, G.2    Faruqi, A.R.3
  • 40
    • 84866078359 scopus 로고    scopus 로고
    • Prevention of overfitting in cryo-EM structure determination
    • Scheres SH, Chen S. Prevention of overfitting in cryo-EM structure determination. Nat Methods 2012; 9: 853-854
    • (2012) Nat Methods , vol.9 , pp. 853-854
    • Scheres, S.H.1    Chen, S.2
  • 41
    • 0142042865 scopus 로고    scopus 로고
    • Optimal determination of particle orientation, absolute hand, and contrast loss in single-particle electron cryomicroscopy
    • Rosenthal PB, Henderson R. Optimal determination of particle orientation, absolute hand, and contrast loss in single-particle electron cryomicroscopy. J Mol Biol 2003; 333: 721-745
    • (2003) J Mol Biol , vol.333 , pp. 721-745
    • Rosenthal, P.B.1    Henderson, R.2
  • 42
    • 84862863609 scopus 로고    scopus 로고
    • Real-space refinement with DireX: From global fitting to side-chain improvements
    • Wang Z, Schroder GF. Real-space refinement with DireX: from global fitting to side-chain improvements. Biopolymers 2012; 97: 687-697
    • (2012) Biopolymers , vol.97 , pp. 687-697
    • Wang, Z.1    Schroder, G.F.2
  • 46
    • 84900435661 scopus 로고    scopus 로고
    • Initiation of translation by cricket paralysis virus IRES requires its translocation in the ribosome
    • Fernandez IS, Bai XC, Murshudov G, Scheres SH, Ramakrishnan V. Initiation of translation by cricket paralysis virus IRES requires its translocation in the ribosome. Cell 2014; 157: 823-831
    • (2014) Cell , vol.157 , pp. 823-831
    • Fernandez, I.S.1    Bai, X.C.2    Murshudov, G.3    Scheres, S.H.4    Ramakrishnan, V.5
  • 47
    • 4444221565 scopus 로고    scopus 로고
    • UCSF chimera-A visualization system for exploratory research and analysis
    • Pettersen EF, Goddard TD, Huang CC, et al. UCSF chimera-A visualization system for exploratory research and analysis. J Comput Chem 2004; 25: 1605-1612
    • (2004) J Comput Chem , vol.25 , pp. 1605-1612
    • Pettersen, E.F.1    Goddard, T.D.2    Huang, C.C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.