메뉴 건너뛰기




Volumn 48, Issue 1, 2014, Pages 28-38

Skeletal muscle excitation-contraction coupling: Who are the dancing partners?

Author keywords

Dihydropyridine receptor; Excitation contraction coupling; Ryanodine receptor; Sarcoplasmic reticulum; Skeletal muscle

Indexed keywords

1,4 DIHYDROPYRIDINE RECEPTOR; BINDING PROTEIN; CALSEQUESTRIN; HISTIDINE RICH CALCIUM BINDING PROTEIN; JP 45 PROTEIN; JUNCTATE; JUNCTIN; JUNCTOPHILIN; MITSUGUMIN 29; PROTEIN; RYANODINE RECEPTOR; STAC3 PROTEIN; TRIADIN; UNCLASSIFIED DRUG; CALCIUM BINDING PROTEIN; CALCIUM RELEASE ACTIVATED CALCIUM CHANNEL 1; GUANYLATE KINASE; HISTIDINE; MUSCLE PROTEIN; TIGHT JUNCTION PROTEIN;

EID: 84892653310     PISSN: 13572725     EISSN: 18785875     Source Type: Journal    
DOI: 10.1016/j.biocel.2013.12.001     Document Type: Review
Times cited : (74)

References (126)
  • 2
    • 83455220173 scopus 로고    scopus 로고
    • Dual role of junctin in the regulation of ryanodine receptors and calcium release in cardiac ventricular myocytes
    • B.A. Altschafl, D.A. Arvanitis, O. Fuentes, Q. Yuan, E.G. Kranias, and H.H. Valdivia Dual role of junctin in the regulation of ryanodine receptors and calcium release in cardiac ventricular myocytes Journal of Physiology 589 2011 6063 6080
    • (2011) Journal of Physiology , vol.589 , pp. 6063-6080
    • Altschafl, B.A.1    Arvanitis, D.A.2    Fuentes, O.3    Yuan, Q.4    Kranias, E.G.5    Valdivia, H.H.6
  • 4
    • 0141994764 scopus 로고    scopus 로고
    • The novel skeletal muscle sarcoplasmic reticulum JP-45 protein. Molecular cloning, tissue distribution, developmental expression, and interaction with α1.1 subunit of the voltage-gated calcium channel
    • DOI 10.1074/jbc.M305016200
    • A.A. Anderson, S. Treves, D. Biral, R. Betto, D. Sandona, and M. Ronjat et al. The novel skeletal muscle sarcoplasmic reticulum JP-45 protein. Molecular cloning, tissue distribution, developmental expression, and interaction with alpha 1.1 subunit of the voltage-gated calcium channel Journal of Biological Chemistry 278 2003 39987 39992 (Pubitemid 37248563)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.41 , pp. 39987-39992
    • Anderson, A.A.1    Treves, S.2    Biral, D.3    Betto, R.4    Sandona, D.5    Ronjat, M.6    Zorzato, F.7
  • 5
    • 54149104117 scopus 로고    scopus 로고
    • The Ser96Ala variant in histidine-rich calcium-binding protein is associated with life-threatening ventricular arrhythmias in idiopathic dilated cardiomyopathy
    • D.A. Arvanitis, D. Sanoudou, F. Kolokathis, E. Vafiadaki, V. Papalouka, and A. Kontrogianni-Konstantopoulos et al. The Ser96Ala variant in histidine-rich calcium-binding protein is associated with life-threatening ventricular arrhythmias in idiopathic dilated cardiomyopathy European Heart Journal 29 2008 2514 2525
    • (2008) European Heart Journal , vol.29 , pp. 2514-2525
    • Arvanitis, D.A.1    Sanoudou, D.2    Kolokathis, F.3    Vafiadaki, E.4    Papalouka, V.5    Kontrogianni-Konstantopoulos, A.6
  • 7
    • 35748948363 scopus 로고    scopus 로고
    • Bridging the myoplasmic gap: Recent developments in skeletal muscle excitation-contraction coupling
    • DOI 10.1007/s10974-007-9118-5
    • R.A. Bannister Bridging the myoplasmic gap: recent developments in skeletal muscle excitation-contraction coupling Journal of Muscle Research and Cell Motility 28 2007 275 283 (Pubitemid 350043630)
    • (2007) Journal of Muscle Research and Cell Motility , vol.28 , Issue.4-5 , pp. 275-283
    • Bannister, R.A.1
  • 8
    • 67649951484 scopus 로고    scopus 로고
    • Effects of inserting fluorescent proteins into the alpha1S II-III loop: Insights into excitation-contraction coupling
    • R.A. Bannister, S. Papadopoulos, C.S. Haarmann, and K.G. Beam Effects of inserting fluorescent proteins into the alpha1S II-III loop: insights into excitation-contraction coupling Journal of General Physiology 134 2009 35 51
    • (2009) Journal of General Physiology , vol.134 , pp. 35-51
    • Bannister, R.A.1    Papadopoulos, S.2    Haarmann, C.S.3    Beam, K.G.4
  • 9
    • 77954346809 scopus 로고    scopus 로고
    • Looking for answers to EC coupling's persistent questions
    • K.G. Beam, and R.A. Bannister Looking for answers to EC coupling's persistent questions Journal of General Physiology 136 2010 7 12
    • (2010) Journal of General Physiology , vol.136 , pp. 7-12
    • Beam, K.G.1    Bannister, R.A.2
  • 10
    • 0032763538 scopus 로고    scopus 로고
    • Involvement of the carboxy-terminus region of the dihydropyridine receptor beta1a subunit in excitation-contraction coupling of skeletal muscle
    • M. Beurg, C.A. Ahern, P. Vallejo, M.W. Conklin, P.A. Powers, and R.G. Gregg et al. Involvement of the carboxy-terminus region of the dihydropyridine receptor beta1a subunit in excitation-contraction coupling of skeletal muscle Biophysical Journal 77 1999 2953 2967
    • (1999) Biophysical Journal , vol.77 , pp. 2953-2967
    • Beurg, M.1    Ahern, C.A.2    Vallejo, P.3    Conklin, M.W.4    Powers, P.A.5    Gregg, R.G.6
  • 11
    • 0024245148 scopus 로고
    • Structural evidence for direct interaction between the molecular components of the transverse tubule/sarcoplasmic reticulum junction in skeletal muscle
    • DOI 10.1083/jcb.107.6.2587
    • B.A. Block, T. Imagawa, K.P. Campbell, and C. Franzini-Armstrong Structural evidence for direct interaction between the molecular components of the transverse tubule/sarcoplasmic reticulum junction in skeletal muscle Journal of Cell Biology 107 1988 2587 2600 (Pubitemid 19019400)
    • (1988) Journal of Cell Biology , vol.107 , Issue.6 , pp. 2587-2600
    • Block, B.A.1    Imagawa, T.2    Campbell, K.P.3    Franzini-Armstrong, C.4
  • 12
    • 84863622589 scopus 로고    scopus 로고
    • Triadin/junctin double null mouse reveals a differential role for triadin and junctin in anchoring CASQ to the jSR and regulating Ca(2+) homeostasis
    • S. Boncompagni, M. Thomas, J.R. Lopez, P.D. Allen, Q. Yuan, and E.G. Kranias et al. Triadin/junctin double null mouse reveals a differential role for triadin and junctin in anchoring CASQ to the jSR and regulating Ca(2+) homeostasis PLoS ONE 7 2012 e39962
    • (2012) PLoS ONE , vol.7 , pp. 39962
    • Boncompagni, S.1    Thomas, M.2    Lopez, J.R.3    Allen, P.D.4    Yuan, Q.5    Kranias, E.G.6
  • 14
    • 0025139194 scopus 로고
    • Molecular interactions of the junctional foot protein and dihydropyridine receptor in skeletal muscle triads
    • N.R. Brandt, A.H. Caswell, S.R. Wen, and J.A. Talvenheimo Molecular interactions of the junctional foot protein and dihydropyridine receptor in skeletal muscle triads Journal of Membrane Biology 113 1990 237 251 (Pubitemid 20070321)
    • (1990) Journal of Membrane Biology , vol.113 , Issue.3 , pp. 237-251
    • Brandt, N.R.1    Caswell, A.H.2    Wen, S.-R.3    Talvenheimo, J.A.4
  • 18
    • 26044442555 scopus 로고    scopus 로고
    • Functional equivalence of dihydropyridine receptor alpha1S and beta1a subunits in triggering excitation-contraction coupling in skeletal muscle
    • R. Coronado, C.A. Ahern, D.C. Sheridan, W. Cheng, L. Carbonneau, and D. Bhattacharya Functional equivalence of dihydropyridine receptor alpha1S and beta1a subunits in triggering excitation-contraction coupling in skeletal muscle Biological Research 37 2004 565 575
    • (2004) Biological Research , vol.37 , pp. 565-575
    • Coronado, R.1    Ahern, C.A.2    Sheridan, D.C.3    Cheng, W.4    Carbonneau, L.5    Bhattacharya, D.6
  • 19
    • 58149284005 scopus 로고    scopus 로고
    • A dihydropyridine receptor alpha1s loop region critical for skeletal muscle contraction is intrinsically unstructured and binds to a SPRY domain of the type 1 ryanodine receptor
    • Y. Cui, H.S. Tae, N.C. Norris, Y. Karunasekara, P. Pouliquin, and P.G. Board et al. A dihydropyridine receptor alpha1s loop region critical for skeletal muscle contraction is intrinsically unstructured and binds to a SPRY domain of the type 1 ryanodine receptor International Journal of Biochemistry & Cell Biology 41 2009 677 686
    • (2009) International Journal of Biochemistry & Cell Biology , vol.41 , pp. 677-686
    • Cui, Y.1    Tae, H.S.2    Norris, N.C.3    Karunasekara, Y.4    Pouliquin, P.5    Board, P.G.6
  • 22
    • 77953912188 scopus 로고    scopus 로고
    • Skeletal muscle excitation-contraction coupling is independent of a conserved heptad repeat motif in the C-terminus of the DHPRbeta(1a) subunit
    • A. Dayal, J. Schredelseker, C. Franzini-Armstrong, and M. Grabner Skeletal muscle excitation-contraction coupling is independent of a conserved heptad repeat motif in the C-terminus of the DHPRbeta(1a) subunit Cell Calcium 47 2010 500 506
    • (2010) Cell Calcium , vol.47 , pp. 500-506
    • Dayal, A.1    Schredelseker, J.2    Franzini-Armstrong, C.3    Grabner, M.4
  • 23
    • 82955196578 scopus 로고    scopus 로고
    • Expression and regulation of excitation-contraction coupling proteins in aging skeletal muscle
    • O. Delbono Expression and regulation of excitation-contraction coupling proteins in aging skeletal muscle Current Aging Science 4 2011 248 259
    • (2011) Current Aging Science , vol.4 , pp. 248-259
    • Delbono, O.1
  • 25
    • 0036512386 scopus 로고    scopus 로고
    • Bi-directional coupling between dihydropyridine receptors and ryanodine receptors
    • R.T. Dirksen Bi-directional coupling between dihydropyridine receptors and ryanodine receptors Frontiers in Bioscience 7 2002 d659 d670
    • (2002) Frontiers in Bioscience , vol.7
    • Dirksen, R.T.1
  • 26
    • 0036021090 scopus 로고    scopus 로고
    • 2+ release channels?
    • DOI 10.1016/S1050-1738(02)00163-9, PII S1050173802001639
    • R.T. Dirksen, and G. Avila Altered ryanodine receptor function in central core disease: leaky or uncoupled Ca(2+) release channels? Trends in Cardiovascular Medicine 12 2002 189 197 (Pubitemid 34823628)
    • (2002) Trends in Cardiovascular Medicine , vol.12 , Issue.5 , pp. 189-197
    • Dirksen, R.T.1    Avila, G.2
  • 28
    • 33747045217 scopus 로고    scopus 로고
    • Excitation-contraction coupling from the 1950s into the new millennium
    • DOI 10.1111/j.1440-1681.2006.04441.x
    • A.F. Dulhunty Excitation-contraction coupling from the 1950s into the new millennium Clinical and Experimental Pharmacology and Physiology 33 2006 763 772 (Pubitemid 44215127)
    • (2006) Clinical and Experimental Pharmacology and Physiology , vol.33 , Issue.9 , pp. 763-772
    • Dulhunty, A.F.1
  • 29
    • 84866149411 scopus 로고    scopus 로고
    • Regulation and dysregulation of cardiac ryanodine receptor (RyR2) open probability during diastole in health and disease
    • A.F. Dulhunty, N.A. Beard, and A.D. Hanna Regulation and dysregulation of cardiac ryanodine receptor (RyR2) open probability during diastole in health and disease Journal of General Physiology 140 2012 87 92
    • (2012) Journal of General Physiology , vol.140 , pp. 87-92
    • Dulhunty, A.F.1    Beard, N.A.2    Hanna, A.D.3
  • 32
    • 79952042738 scopus 로고    scopus 로고
    • Reduced gain of excitation-contraction coupling in triadin-null myotubes is mediated by the disruption of FKBP12/RyR1 interaction
    • J.M. Eltit, J. Szpyt, H. Li, P.D. Allen, and C.F. Perez Reduced gain of excitation-contraction coupling in triadin-null myotubes is mediated by the disruption of FKBP12/RyR1 interaction Cell Calcium 49 2011 128 135
    • (2011) Cell Calcium , vol.49 , pp. 128-135
    • Eltit, J.M.1    Szpyt, J.2    Li, H.3    Allen, P.D.4    Perez, C.F.5
  • 34
    • 38149069020 scopus 로고    scopus 로고
    • Regulatory roles of junctin in sarcoplasmic reticulum calcium cycling and myocardial function
    • G.C. Fan, Q. Yuan, and E.G. Kranias Regulatory roles of junctin in sarcoplasmic reticulum calcium cycling and myocardial function Trends in Cardiovascular Medicine 18 2008 1 5
    • (2008) Trends in Cardiovascular Medicine , vol.18 , pp. 1-5
    • Fan, G.C.1    Yuan, Q.2    Kranias, E.G.3
  • 35
    • 0034676004 scopus 로고    scopus 로고
    • The triad targeting signal of the skeletal muscle calcium channel is localized in the COOH terminus of the alpha(1S) subunit
    • B.E. Flucher, N. Kasielke, and M. Grabner The triad targeting signal of the skeletal muscle calcium channel is localized in the COOH terminus of the alpha(1S) subunit Journal of Cell Biology 151 2000 467 478
    • (2000) Journal of Cell Biology , vol.151 , pp. 467-478
    • Flucher, B.E.1    Kasielke, N.2    Grabner, M.3
  • 37
    • 0032839459 scopus 로고    scopus 로고
    • Shape, size, and distribution of Ca(2+) release units and couplons in skeletal and cardiac muscles
    • C. Franzini-Armstrong, F. Protasi, and V. Ramesh Shape, size, and distribution of Ca(2+) release units and couplons in skeletal and cardiac muscles Biophysical Journal 77 1999 1528 1539
    • (1999) Biophysical Journal , vol.77 , pp. 1528-1539
    • Franzini-Armstrong, C.1    Protasi, F.2    Ramesh, V.3
  • 41
    • 0033618408 scopus 로고    scopus 로고
    • The II-III loop of the skeletal muscle dihydropyridine receptor is responsible for the bi-directional coupling with the ryanodine receptor
    • M. Grabner, R.T. Dirksen, N. Suda, and K.G. Beam The II-III loop of the skeletal muscle dihydropyridine receptor is responsible for the bi-directional coupling with the ryanodine receptor Journal of Biological Chemistry 274 1999 21913 21919
    • (1999) Journal of Biological Chemistry , vol.274 , pp. 21913-21919
    • Grabner, M.1    Dirksen, R.T.2    Suda, N.3    Beam, K.G.4
  • 45
    • 84868194081 scopus 로고    scopus 로고
    • Mapping domains and mutations on the skeletal muscle ryanodine receptor channel
    • J.H. Hwang, F. Zorzato, N.F. Clarke, and S. Treves Mapping domains and mutations on the skeletal muscle ryanodine receptor channel Trends in Molecular Medicine 18 2012 644 657
    • (2012) Trends in Molecular Medicine , vol.18 , pp. 644-657
    • Hwang, J.H.1    Zorzato, F.2    Clarke, N.F.3    Treves, S.4
  • 46
    • 84858025677 scopus 로고    scopus 로고
    • Nanoscale organization of junctophilin-2 and ryanodine receptors within peripheral couplings of rat ventricular cardiomyocytes
    • I.D. Jayasinghe, D. Baddeley, C.H. Kong, X.H. Wehrens, M.B. Cannell, and C. Soeller Nanoscale organization of junctophilin-2 and ryanodine receptors within peripheral couplings of rat ventricular cardiomyocytes Biophysical Journal 102 2012 L19 L21
    • (2012) Biophysical Journal , vol.102
    • Jayasinghe, I.D.1    Baddeley, D.2    Kong, C.H.3    Wehrens, X.H.4    Cannell, M.B.5    Soeller, C.6
  • 51
    • 33846323688 scopus 로고    scopus 로고
    • A variably spliced region in the type 1 ryanodine receptor may participate in an inter-domain interaction
    • DOI 10.1042/BJ20060686
    • T. Kimura, S.M. Pace, L. Wei, N.A. Beard, R.T. Dirksen, and A.F. Dulhunty A variably spliced region in the type 1 ryanodine receptor may participate in an inter-domain interaction Biochemical Journal 401 2007 317 324 (Pubitemid 46114624)
    • (2007) Biochemical Journal , vol.401 , Issue.1 , pp. 317-324
    • Kimura, T.1    Pace, S.M.2    Wei, L.3    Beard, N.A.4    Dirksen, R.T.5    Dulhunty, A.F.6
  • 52
  • 53
    • 1042289749 scopus 로고    scopus 로고
    • 1S II-III Loop for Skeletal-type Excitation-Contraction Coupling
    • DOI 10.1074/jbc.M307538200
    • G. Kugler, R.G. Weiss, B.E. Flucher, and M. Grabner Structural requirements of the dihydropyridine receptor alpha1S II-III loop for skeletal-type excitation-contraction coupling Journal of Biological Chemistry 279 2004 4721 4728 (Pubitemid 38199066)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.6 , pp. 4721-4728
    • Kugler, G.1    Weiss, R.G.2    Flucher, B.E.3    Grabner, M.4
  • 56
    • 0035955601 scopus 로고    scopus 로고
    • Interaction of HRC (histidine-rich Ca(2+)-binding protein) and triadin in the lumen of sarcoplasmic reticulum
    • H.G. Lee, H. Kang, D.H. Kim, and W.J. Park Interaction of HRC (histidine-rich Ca(2+)-binding protein) and triadin in the lumen of sarcoplasmic reticulum Journal of Biological Chemistry 276 2001 39533 39538
    • (2001) Journal of Biological Chemistry , vol.276 , pp. 39533-39538
    • Lee, H.G.1    Kang, H.2    Kim, D.H.3    Park, W.J.4
  • 57
    • 84862908835 scopus 로고    scopus 로고
    • Role of Junctin protein interactions in cellular dynamics of calsequestrin polymer upon calcium perturbation
    • K.W. Lee, J.S. Maeng, J.Y. Choi, Y.R. Lee, C.Y. Hwang, and S.S. Park et al. Role of Junctin protein interactions in cellular dynamics of calsequestrin polymer upon calcium perturbation Journal of Biological Chemistry 287 2012 1679 1687
    • (2012) Journal of Biological Chemistry , vol.287 , pp. 1679-1687
    • Lee, K.W.1    Maeng, J.S.2    Choi, J.Y.3    Lee, Y.R.4    Hwang, C.Y.5    Park, S.S.6
  • 58
    • 0032478812 scopus 로고    scopus 로고
    • A 37-amino acid sequence in the skeletal muscle ryanodine receptor interacts with the cytoplasmic loop between domains II and III in the skeletal muscle dihydropyridine receptor
    • DOI 10.1074/jbc.273.14.7791
    • P. Leong, and D.H. MacLennan A 37-amino acid sequence in the skeletal muscle ryanodine receptor interacts with the cytoplasmic loop between domains II and III in the skeletal muscle dihydropyridine receptor Journal of Biological Chemistry 273 1998 7791 7794 (Pubitemid 28168820)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.14 , pp. 7791-7794
    • Leong, P.1    MacLennan, D.H.2
  • 59
    • 33645647478 scopus 로고    scopus 로고
    • 1a subunits in triad junctions in skeletal muscle
    • DOI 10.1074/jbc.M509566200
    • V. Leuranguer, S. Papadopoulos, and K.G. Beam Organization of calcium channel beta1a subunits in triad junctions in skeletal muscle Journal of Biological Chemistry 281 2006 3521 3527 (Pubitemid 43845968)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.6 , pp. 3521-3527
    • Leuranguer, V.1    Papadopoulos, S.2    Beam, K.G.3
  • 60
    • 34748860581 scopus 로고    scopus 로고
    • Accessibility of targeted DHPR sites to streptavidin and functional effects of binding on EC coupling
    • DOI 10.1085/jgp.200609730
    • N.M. Lorenzon, and K.G. Beam Accessibility of targeted DHPR sites to streptavidin and functional effects of binding on EC coupling Journal of General Physiology 130 2007 379 388 (Pubitemid 47481601)
    • (2007) Journal of General Physiology , vol.130 , Issue.4 , pp. 379-388
    • Lorenzon, N.M.1    Beam, K.G.2
  • 61
    • 6344226668 scopus 로고    scopus 로고
    • Metabolic biotinylation as a probe of supramolecular structure of the triad junction in skeletal muscle
    • DOI 10.1074/jbc.M405318200
    • N.M. Lorenzon, C.S. Haarmann, E.E. Norris, S. Papadopoulos, and K.G. Beam Metabolic biotinylation as a probe of supramolecular structure of the triad junction in skeletal muscle Journal of Biological Chemistry 279 2004 44057 44064 (Pubitemid 39390715)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.42 , pp. 44057-44064
    • Lorenzon, N.M.1    Haarmann, C.S.2    Norris, E.E.3    Papadopoulos, S.4    Beam, K.G.5
  • 62
    • 0033042659 scopus 로고    scopus 로고
    • Regulatory role of SH3 domain-mediated protein-protein interactions in synaptic vesicle endocytosis
    • DOI 10.1016/S0898-6568(98)00059-X, PII S089865689800059X
    • P.S. McPherson Regulatory role of SH3 domain-mediated protein-protein interactions in synaptic vesicle endocytosis Cell Signalling 11 1999 229 238 (Pubitemid 29185124)
    • (1999) Cellular Signalling , vol.11 , Issue.4 , pp. 229-238
    • McPherson, P.S.1
  • 64
    • 0030968771 scopus 로고    scopus 로고
    • 1- dihydropyridine receptor in rabbit skeletal muscle triads
    • B.E. Murray, and K. Ohlendieck Cross-linking analysis of the ryanodine receptor and alpha1-dihydropyridine receptor in rabbit skeletal muscle triads Biochemical Journal 324 Pt 2 1997 689 696 (Pubitemid 27268019)
    • (1997) Biochemical Journal , vol.324 , Issue.2 , pp. 689-696
    • Murray, B.E.1    Ohlendieck, K.2
  • 65
    • 0034626683 scopus 로고    scopus 로고
    • Increased susceptibility to fatigue of slow- and fast-twitch muscles from mice lacking the MG29 gene
    • R.Y. Nagaraj, C.M. Nosek, M.A. Brotto, M. Nishi, H. Takeshima, and T.M. Nosek et al. Increased susceptibility to fatigue of slow- and fast-twitch muscles from mice lacking the MG29 gene Physiological Genomics 4 2000 43 49 (Pubitemid 33676679)
    • (2001) Physiological Genomics , vol.2001 , Issue.4 , pp. 43-49
    • Nagaraj, R.Y.1    Nosek, C.M.2    Brotto, M.A.P.3    Nishi, M.4    Takeshima, H.5    Nosek, T.M.6    Ma, J.7
  • 66
    • 0029983398 scopus 로고    scopus 로고
    • Enhanced dihydropyridine receptor channel activity in the presence of ryanodine receptor
    • DOI 10.1038/380072a0
    • J. Nakai, R.T. Dirksen, H.T. Nguyen, I.N. Pessah, K.G. Beam, and P.D. Allen Enhanced dihydropyridine receptor channel activity in the presence of ryanodine receptor Nature 380 1996 72 75 (Pubitemid 26076239)
    • (1996) Nature , vol.380 , Issue.6569 , pp. 72-75
    • Nakai, J.1    Dirksen, R.T.2    Nguyen, H.T.3    Pessah, I.N.4    Beam, K.G.5    Allen, P.D.6
  • 76
    • 81555226040 scopus 로고    scopus 로고
    • Differential effect of calsequestrin ablation on structure and function of fast and slow skeletal muscle fibers
    • C. Paolini, M. Quarta, L. D'Onofrio, C. Reggiani, and F. Protasi Differential effect of calsequestrin ablation on structure and function of fast and slow skeletal muscle fibers Journal of Biomedicine & Biotechnology 2011 2011 634075
    • (2011) Journal of Biomedicine & Biotechnology , vol.2011 , pp. 634075
    • Paolini, C.1    Quarta, M.2    D'Onofrio, L.3    Reggiani, C.4    Protasi, F.5
  • 77
    • 84875491683 scopus 로고    scopus 로고
    • Targeted ablation of the histidine-rich Ca(2+)-binding protein (HRC) gene is associated with abnormal SR Ca(2+)-cycling and severe pathology under pressure-overload stress
    • C.S. Park, S. Chen, H. Lee, H. Cha, J.G. Oh, and S. Hong et al. Targeted ablation of the histidine-rich Ca(2+)-binding protein (HRC) gene is associated with abnormal SR Ca(2+)-cycling and severe pathology under pressure-overload stress Basic Research in Cardiology 108 2013 344
    • (2013) Basic Research in Cardiology , vol.108 , pp. 344
    • Park, C.S.1    Chen, S.2    Lee, H.3    Cha, H.4    Oh, J.G.5    Hong, S.6
  • 79
    • 34247847732 scopus 로고    scopus 로고
    • Conformation-dependent stability of junctophilin 1 (JP1) and Ryanodine Receptor Type 1 (RyR1) channel complex is mediated by their hyper-reactive thiols
    • DOI 10.1074/jbc.M609936200
    • A.J. Phimister, J. Lango, E.H. Lee, M.A. Ernst-Russell, H. Takeshima, and J. Ma et al. Conformation-dependent stability of junctophilin 1 (JP1) and ryanodine receptor type 1 (RyR1) channel complex is mediated by their hyper-reactive thiols Journal of Biological Chemistry 282 2007 8667 8677 (Pubitemid 47093508)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.12 , pp. 8667-8677
    • Phimister, A.J.1    Lango, J.2    Eun, H.L.3    Ernst-Russell, M.A.4    Takeshima, H.5    Jianjie, M.6    Allen, P.D.7    Pessah, I.N.8
  • 80
    • 84870387573 scopus 로고    scopus 로고
    • Fluorescence resonance energy transfer (FRET) indicates that association with the type i ryanodine receptor (RyR1) causes reorientation of multiple cytoplasmic domains of the dihydropyridine receptor (DHPR) alpha(1S) subunit
    • A. Polster, J.D. Ohrtman, K.G. Beam, and S. Papadopoulos Fluorescence resonance energy transfer (FRET) indicates that association with the type I ryanodine receptor (RyR1) causes reorientation of multiple cytoplasmic domains of the dihydropyridine receptor (DHPR) alpha(1S) subunit Journal of Biological Chemistry 287 2012 41560 41568
    • (2012) Journal of Biological Chemistry , vol.287 , pp. 41560-41568
    • Polster, A.1    Ohrtman, J.D.2    Beam, K.G.3    Papadopoulos, S.4
  • 82
    • 4243279444 scopus 로고    scopus 로고
    • Structural interaction between RYRs and DHPRs in calcium release units of cardiac and skeletal muscle cells
    • F. Protasi Structural interaction between RYRs and DHPRs in calcium release units of cardiac and skeletal muscle cells Frontiers in Bioscience 7 2002 d650 d658
    • (2002) Frontiers in Bioscience , vol.7
    • Protasi, F.1
  • 84
    • 0036930754 scopus 로고    scopus 로고
    • 1S-dihydropyridine receptors in skeletal muscle
    • F. Protasi, C. Paolini, J. Nakai, K.G. Beam, C. Franzini-Armstrong, and P.D. Allen Multiple regions of RyR1 mediate functional and structural interactions with alpha(1S)-dihydropyridine receptors in skeletal muscle Biophysical Journal 83 2002 3230 3244 (Pubitemid 36041942)
    • (2002) Biophysical Journal , vol.83 , Issue.6 , pp. 3230-3244
    • Protasi, F.1    Paolini, C.2    Nakai, J.3    Beam, K.G.4    Franzini-Armstrong, C.5    Allen, P.D.6
  • 85
    • 79951820580 scopus 로고    scopus 로고
    • The beta(1a) subunit of the skeletal DHPR binds to skeletal RyR1 and activates the channel via its 35-residue C-terminal tail
    • R.T. Rebbeck, Y. Karunasekara, E.M. Gallant, P.G. Board, N.A. Beard, and M.G. Casarotto et al. The beta(1a) subunit of the skeletal DHPR binds to skeletal RyR1 and activates the channel via its 35-residue C-terminal tail Biophysical Journal 100 2011 922 930
    • (2011) Biophysical Journal , vol.100 , pp. 922-930
    • Rebbeck, R.T.1    Karunasekara, Y.2    Gallant, E.M.3    Board, P.G.4    Beard, N.A.5    Casarotto, M.G.6
  • 86
    • 84876573203 scopus 로고    scopus 로고
    • Stac3 is a novel regulator of skeletal muscle development in mice
    • B.M. Reinholt, X. Ge, X. Cong, D.E. Gerrard, and H. Jiang Stac3 is a novel regulator of skeletal muscle development in mice PLoS ONE 8 2013 e62760
    • (2013) PLoS ONE , vol.8 , pp. 62760
    • Reinholt, B.M.1    Ge, X.2    Cong, X.3    Gerrard, D.E.4    Jiang, H.5
  • 87
    • 0030922504 scopus 로고    scopus 로고
    • Dihydropyridine receptor-ryanodine receptor uncoupling in aged skeletal muscle
    • DOI 10.1007/s002329900233
    • M. Renganathan, M.L. Messi, and O. Delbono Dihydropyridine receptor-ryanodine receptor uncoupling in aged skeletal muscle Journal of Membrane Biology 157 1997 247 253 (Pubitemid 27276167)
    • (1997) Journal of Membrane Biology , vol.157 , Issue.3 , pp. 247-253
    • Renganathan, M.1    Messi, M.L.2    Delbono, O.3
  • 90
    • 22444444618 scopus 로고    scopus 로고
    • Internal structure and visualization of transmembrane domains of the RyR1 calcium release channel by cryo-EM
    • DOI 10.1038/nsmb938, PII NSMB938
    • M. Samso, T. Wagenknecht, and P.D. Allen Internal structure and visualization of transmembrane domains of the RyR1 calcium release channel by cryo-EM Nature Structural & Molecular Biology 12 2005 539 544 (Pubitemid 43085885)
    • (2005) Nature Structural and Molecular Biology , vol.12 , Issue.6 , pp. 539-544
    • Samso, M.1    Wagenknecht, T.2    Allen, P.D.3
  • 91
    • 84862824078 scopus 로고    scopus 로고
    • Mitsugumin 29 is transcriptionally induced in senile plaque-associated astrocytes
    • K. Satoh, H. Akatsu, T. Yamamoto, K. Kosaka, H. Yokota, and T. Yamada Mitsugumin 29 is transcriptionally induced in senile plaque-associated astrocytes Brain Research 1441 2012 9 16
    • (2012) Brain Research , vol.1441 , pp. 9-16
    • Satoh, K.1    Akatsu, H.2    Yamamoto, T.3    Kosaka, K.4    Yokota, H.5    Yamada, T.6
  • 92
    • 59449093461 scopus 로고    scopus 로고
    • Proper restoration of excitation-contraction coupling in the dihydropyridine receptor beta1-null zebrafish relaxed is an exclusive function of the beta1a subunit
    • J. Schredelseker, A. Dayal, T. Schwerte, C. Franzini-Armstrong, and M. Grabner Proper restoration of excitation-contraction coupling in the dihydropyridine receptor beta1-null zebrafish relaxed is an exclusive function of the beta1a subunit Journal of Biological Chemistry 284 2009 1242 1251
    • (2009) Journal of Biological Chemistry , vol.284 , pp. 1242-1251
    • Schredelseker, J.1    Dayal, A.2    Schwerte, T.3    Franzini-Armstrong, C.4    Grabner, M.5
  • 95
    • 4143124295 scopus 로고    scopus 로고
    • Involvement of a heptad repeat in the carboxyl terminus of the dihydropyridine receptor β1a subunit in the mechanism of excitation-contraction coupling in skeletal muscle
    • DOI 10.1529/biophysj.104.043810
    • D.C. Sheridan, W. Cheng, L. Carbonneau, C.A. Ahern, and R. Coronado Involvement of a heptad repeat in the carboxyl terminus of the dihydropyridine receptor beta1a subunit in the mechanism of excitation-contraction coupling in skeletal muscle Biophysical Journal 87 2004 929 942 (Pubitemid 39095074)
    • (2004) Biophysical Journal , vol.87 , Issue.2 , pp. 929-942
    • Sheridan, D.C.1    Cheng, W.2    Carbonneau, L.3    Ahern, C.A.4    Coronado, R.5
  • 96
    • 84860329338 scopus 로고    scopus 로고
    • Bimolecular fluorescence complementation and targeted biotinylation provide insight into the topology of the skeletal muscle Ca(2+) channel beta1a subunit
    • D.C. Sheridan, O. Moua, N.M. Lorenzon, and K.G. Beam Bimolecular fluorescence complementation and targeted biotinylation provide insight into the topology of the skeletal muscle Ca(2+) channel beta1a subunit Channels 6 2012 26 40
    • (2012) Channels , vol.6 , pp. 26-40
    • Sheridan, D.C.1    Moua, O.2    Lorenzon, N.M.3    Beam, K.G.4
  • 98
    • 0032541149 scopus 로고    scopus 로고
    • Structure and expression of mitsugumin29 gene
    • DOI 10.1016/S0014-5793(98)00770-4, PII S0014579398007704
    • M. Shimuta, S. Komazaki, M. Nishi, M. Iino, K. Nakagawara, and H. Takeshima Structure and expression of mitsugumin29 gene FEBS Letters 431 1998 263 267 (Pubitemid 28334230)
    • (1998) FEBS Letters , vol.431 , Issue.2 , pp. 263-267
    • Shimuta, M.1    Komazaki, S.2    Nishi, M.3    Iino, M.4    Nakagawara, K.-I.5    Takeshima, H.6
  • 101
    • 0030885385 scopus 로고    scopus 로고
    • Local control model of excitation-contraction coupling in skeletal muscle
    • DOI 10.1085/jgp.110.4.415
    • M.D. Stern, G. Pizarro, and E. Rios Local control model of excitation-contraction coupling in skeletal muscle Journal of General Physiology 110 1997 415 440 (Pubitemid 27431179)
    • (1997) Journal of General Physiology , vol.110 , Issue.4 , pp. 415-440
    • Stern, M.D.1    Pizarro, G.2    Rios, E.3
  • 104
  • 107
    • 0028065352 scopus 로고
    • Restoration of junctional tetrads in dysgenic myotubes by dihydropyridine receptor cDNA
    • H. Takekura, L. Bennett, T. Tanabe, K.G. Beam, and C. Franzini-Armstrong Restoration of junctional tetrads in dysgenic myotubes by dihydropyridine receptor cDNA Biophysical Journal 67 1994 793 803 (Pubitemid 24235408)
    • (1994) Biophysical Journal , vol.67 , Issue.2 , pp. 793-803
    • Takekura, H.1    Bennett, L.2    Tanabe, T.3    Beam, K.G.4    Franzini-Armstrong, C.5
  • 108
    • 9444246475 scopus 로고    scopus 로고
    • Differential contribution of skeletal and cardiac II-III loop sequences to the assembly of dihydropyridine-receptor arrays in skeletal muscle
    • DOI 10.1091/mbc.E04-05-0414
    • H. Takekura, C. Paolini, C. Franzini-Armstrong, G. Kugler, M. Grabner, and B.E. Flucher Differential contribution of skeletal and cardiac II-III loop sequences to the assembly of dihydropyridine-receptor arrays in skeletal muscle Molecular Biology of the Cell 15 2004 5408 5419 (Pubitemid 39564734)
    • (2004) Molecular Biology of the Cell , vol.15 , Issue.12 , pp. 5408-5419
    • Takekura, H.1    Paolini, C.2    Franzini-Armstrong, C.3    Kugler, G.4    Grabner, M.5    Flucher, B.E.6
  • 109
    • 0344826004 scopus 로고    scopus 로고
    • Plasticity of the transverse tubules following denervation and subsequent reinnervation in rat slow and fast muscle fibres
    • DOI 10.1023/A:1027356912404
    • H. Takekura, H. Tamaki, T. Nishizawa, and N. Kasuga Plasticity of the transverse tubules following denervation and subsequent reinnervation in rat slow and fast muscle fibres Journal of Muscle Research and Cell Motility 24 2003 439 451 (Pubitemid 37475988)
    • (2003) Journal of Muscle Research and Cell Motility , vol.24 , Issue.7 , pp. 439-451
    • Takekura, H.1    Tamaki, H.2    Nishizawa, T.3    Kasuga, N.4
  • 110
    • 0347075453 scopus 로고    scopus 로고
    • Calmodulin modulation of proteins involved in excitation-contraction coupling
    • W. Tang, S. Sencer, and S.L. Hamilton Calmodulin modulation of proteins involved in excitation-contraction coupling Frontiers in Bioscience 7 2002 d1583 d1589
    • (2002) Frontiers in Bioscience , vol.7
    • Tang, W.1    Sencer, S.2    Hamilton, S.L.3
  • 111
    • 0034671917 scopus 로고    scopus 로고
    • Molecular cloning, expression, functional characterization, chromosomal localization, and gene structure of junctate, a novel integral calcium binding protein of sarco(endo)plasmic reticulum membrane
    • DOI 10.1074/jbc.M005473200
    • S. Treves, G. Feriotto, L. Moccagatta, R. Gambari, and F. Zorzato Molecular cloning, expression, functional characterization, chromosomal localization, and gene structure of junctate, a novel integral calcium binding protein of sarco(endo)plasmic reticulum membrane Journal of Biological Chemistry 275 2000 39555 39568 (Pubitemid 32058982)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.50 , pp. 39555-39568
    • Treves, S.1    Feriotto, G.2    Moccagatta, L.3    Gambari, R.4    Zorzato, F.5
  • 113
    • 67650385767 scopus 로고    scopus 로고
    • Minor sarcoplasmic reticulum membrane components that modulate excitation-contraction coupling in striated muscles
    • S. Treves, M. Vukcevic, M. Maj, R. Thurnheer, B. Mosca, and F. Zorzato Minor sarcoplasmic reticulum membrane components that modulate excitation-contraction coupling in striated muscles Journal of Physiology 587 2009 3071 3079
    • (2009) Journal of Physiology , vol.587 , pp. 3071-3079
    • Treves, S.1    Vukcevic, M.2    Maj, M.3    Thurnheer, R.4    Mosca, B.5    Zorzato, F.6
  • 114
    • 79952739100 scopus 로고    scopus 로고
    • Disrupted junctional membrane complexes and hyperactive ryanodine receptors after acute junctophilin knockdown in mice
    • R.J. van Oort, A. Garbino, W. Wang, S.S. Dixit, A.P. Landstrom, and N. Gaur et al. Disrupted junctional membrane complexes and hyperactive ryanodine receptors after acute junctophilin knockdown in mice Circulation 123 2011 979 988
    • (2011) Circulation , vol.123 , pp. 979-988
    • Van Oort, R.J.1    Garbino, A.2    Wang, W.3    Dixit, S.S.4    Landstrom, A.P.5    Gaur, N.6
  • 115
    • 84866395344 scopus 로고    scopus 로고
    • Ryanodine receptors: Structure and function
    • F. Van Petegem Ryanodine receptors: structure and function Journal of Biological Chemistry 287 2012 31624 31632
    • (2012) Journal of Biological Chemistry , vol.287 , pp. 31624-31632
    • Van Petegem, F.1
  • 116
    • 2942615325 scopus 로고    scopus 로고
    • Structure of a complex between a voltage-gated calcium channel β-subunit and an α-subunit domain
    • DOI 10.1038/nature02588
    • F. Van Petegem, K.A. Clark, F.C. Chatelain, and D.L. Minor Jr. Structure of a complex between a voltage-gated calcium channel beta-subunit and an alpha-subunit domain Nature 429 2004 671 675 (Pubitemid 38812320)
    • (2004) Nature , vol.429 , Issue.6992 , pp. 671-675
    • Van Petegam, F.1    Clark, K.A.2    Chatelain, F.C.3    Minor Jr., D.L.4
  • 117
    • 38949120535 scopus 로고    scopus 로고
    • Vβ Interaction Site that Is Critical for Channel Modulation
    • DOI 10.1016/j.str.2007.11.010, PII S0969212608000063
    • F. Van Petegem, K.E. Duderstadt, K.A. Clark, M. Wang, and D.L. Minor Jr. Alanine-scanning mutagenesis defines a conserved energetic hotspot in the CaValpha1 AID-CaVbeta interaction site that is critical for channel modulation Structure 16 2008 280 294 (Pubitemid 351222651)
    • (2008) Structure , vol.16 , Issue.2 , pp. 280-294
    • Van Petegem, F.1    Duderstadt, K.E.2    Clark, K.A.3    Wang, M.4    Minor Jr., D.L.5
  • 118
    • 58149110941 scopus 로고    scopus 로고
    • Altered stored calcium release in skeletal myotubes deficient of triadin and junctin
    • Y. Wang, X. Li, H. Duan, T.R. Fulton, J.P. Eu, and G. Meissner Altered stored calcium release in skeletal myotubes deficient of triadin and junctin Cell Calcium 45 2009 29 37
    • (2009) Cell Calcium , vol.45 , pp. 29-37
    • Wang, Y.1    Li, X.2    Duan, H.3    Fulton, T.R.4    Eu, J.P.5    Meissner, G.6
  • 119
    • 67650464941 scopus 로고    scopus 로고
    • Junctin and triadin each activate skeletal ryanodine receptors but junctin alone mediates functional interactions with calsequestrin
    • L. Wei, E.M. Gallant, A.F. Dulhunty, and N.A. Beard Junctin and triadin each activate skeletal ryanodine receptors but junctin alone mediates functional interactions with calsequestrin International Journal of Biochemistry & Cell Biology 41 2009 2214 2224
    • (2009) International Journal of Biochemistry & Cell Biology , vol.41 , pp. 2214-2224
    • Wei, L.1    Gallant, E.M.2    Dulhunty, A.F.3    Beard, N.A.4
  • 120
    • 67349175061 scopus 로고    scopus 로고
    • Unique isoform-specific properties of calsequestrin in the heart and skeletal muscle
    • L. Wei, A.D. Hanna, N.A. Beard, and A.F. Dulhunty Unique isoform-specific properties of calsequestrin in the heart and skeletal muscle Cell Calcium 45 2009 474 484
    • (2009) Cell Calcium , vol.45 , pp. 474-484
    • Wei, L.1    Hanna, A.D.2    Beard, N.A.3    Dulhunty, A.F.4
  • 121
    • 4544330774 scopus 로고    scopus 로고
    • Functional analysis of the R1086H malignant hyperthermia mutation in the DHPR reveals an unexpected influence of the III-IV loop on skeletal muscle EC coupling
    • R.G. Weiss, K.M. O'Connell, B.E. Flucher, P.D. Allen, M. Grabner, and R.T. Dirksen Functional analysis of the R1086H malignant hyperthermia mutation in the DHPR reveals an unexpected influence of the III-IV loop on skeletal muscle EC coupling American Journal of Physiology - Cell Physiology 287 2004 C1094 C1102
    • (2004) American Journal of Physiology - Cell Physiology , vol.287
    • Weiss, R.G.1    O'Connell, K.M.2    Flucher, B.E.3    Allen, P.D.4    Grabner, M.5    Dirksen, R.T.6
  • 123
    • 84871609091 scopus 로고    scopus 로고
    • JP-45/JSRP1 variants affect skeletal muscle excitation-contraction coupling by decreasing the sensitivity of the dihydropyridine receptor
    • T. Yasuda, O. Delbono, Z.M. Wang, M.L. Messi, T. Girard, and A. Urwyler et al. JP-45/JSRP1 variants affect skeletal muscle excitation-contraction coupling by decreasing the sensitivity of the dihydropyridine receptor Human Mutation 34 2013 184 190
    • (2013) Human Mutation , vol.34 , pp. 184-190
    • Yasuda, T.1    Delbono, O.2    Wang, Z.M.3    Messi, M.L.4    Girard, T.5    Urwyler, A.6
  • 124
    • 12844272946 scopus 로고    scopus 로고
    • 2+ release channel on lipid membranes
    • DOI 10.1016/j.jsb.2004.10.008, PII S1047847704002096
    • 2+ release channel on lipid membranes Journal of Structural Biology 149 2005 219 224 (Pubitemid 40170104)
    • (2005) Journal of Structural Biology , vol.149 , Issue.2 , pp. 219-224
    • Yin, C.-C.1    Han, H.2    Wei, R.3    Lai, F.A.4
  • 126
    • 0034667521 scopus 로고    scopus 로고
    • Identification of a novel 45 kDa protein (JP-45) from rabbit sarcoplasmic-reticulum junctional-face membrane
    • F. Zorzato, A.A. Anderson, K. Ohlendieck, G. Froemming, R. Guerrini, and S. Treves Identification of a novel 45 kDa protein (JP-45) from rabbit sarcoplasmic-reticulum junctional-face membrane Biochemical Journal 351 Pt 2 2000 537 543
    • (2000) Biochemical Journal , vol.351 , Issue.PART 2 , pp. 537-543
    • Zorzato, F.1    Anderson, A.A.2    Ohlendieck, K.3    Froemming, G.4    Guerrini, R.5    Treves, S.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.