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Volumn 4, Issue , 2015, Pages

Regulation of ryanodine receptor RyR2 by protein-protein interactions: Prediction of a PKA binding site on the N-terminal domain of RyR2 and its relation to disease causing mutations

Author keywords

[No Author keywords available]

Indexed keywords

CYCLIC AMP DEPENDENT PROTEIN KINASE; RYANODINE RECEPTOR 2;

EID: 84931291661     PISSN: 20461402     EISSN: 1759796X     Source Type: Journal    
DOI: 10.12688/f1000research.5858.1     Document Type: Article
Times cited : (1)

References (35)
  • 1
    • 79960625443 scopus 로고    scopus 로고
    • The structural biology of ryanodine receptors
    • 21786194
    • Kimlicka L Van Petegem F: The structural biology of ryanodine receptors. Sci China Life Sci. 2011;54(8):712-724. 21786194 10.1007/s11427-011-4198-2
    • (2011) Sci China Life Sci , vol.54 , Issue.8 , pp. 712-724
    • Kimlicka, L.1    Van Petegem, F.2
  • 2
    • 63249089821 scopus 로고    scopus 로고
    • Ryanodine receptor structure: progress and challenges
    • 18927076, 3837402
    • Hamilton SL Serysheva II: Ryanodine receptor structure: progress and challenges. J Biol Chem. 2009;284(7):4047-4051. 18927076 10.1074/jbc.R800054200 3837402
    • (2009) J Biol Chem , vol.284 , Issue.7 , pp. 4047-4051
    • Hamilton, S.L.1    Serysheva, I.I.2
  • 3
    • 70350709897 scopus 로고    scopus 로고
    • Crystal structures of the N-terminal domains of cardiac and skeletal muscle ryanodine receptors: insights into disease mutations
    • 3a, 19913485
    • 3a Lobo PA Van Petegem F: Crystal structures of the N-terminal domains of cardiac and skeletal muscle ryanodine receptors: insights into disease mutations. Structure. 2009;17(11):1505-1514. 19913485 10.1016/j.str.2009.08.016
    • (2009) Structure , vol.17 , Issue.11 , pp. 1505-1514
    • Lobo, P.A.1    Van Petegem, F.2
  • 4
    • 79958173577 scopus 로고    scopus 로고
    • The deletion of exon 3 in the cardiac ryanodine receptor is rescued by β strand switching
    • 3b, 21645850
    • 3b Lobo PA Kimlicka L Tung CC: The deletion of exon 3 in the cardiac ryanodine receptor is rescued by β strand switching. Structure. 2011;19(6):790-798. 21645850 10.1016/j.str.2011.03.016
    • (2011) Structure , vol.19 , Issue.6 , pp. 790-798
    • Lobo, P.A.1    Kimlicka, L.2    Tung, C.C.3
  • 5
    • 78649469923 scopus 로고    scopus 로고
    • The amino-terminal disease hotspot of ryanodine receptors forms a cytoplasmic vestibule
    • 3c, 21048710
    • 3c Tung CC Lobo PA Kimlicka L: The amino-terminal disease hotspot of ryanodine receptors forms a cytoplasmic vestibule. Nature. 2010;468(7323):585-588. 21048710 10.1038/nature09471
    • (2010) Nature , vol.468 , Issue.7323 , pp. 585-588
    • Tung, C.C.1    Lobo, P.A.2    Kimlicka, L.3
  • 6
    • 0345490780 scopus 로고    scopus 로고
    • Altered function and regulation of cardiac ryanodine receptors in cardiac disease
    • 14659699
    • Wehrens XH Marks AR: Altered function and regulation of cardiac ryanodine receptors in cardiac disease. Trends Biochem Sci. 2003;28(12):671-678. 14659699 10.1016/j.tibs.2003.10.003
    • (2003) Trends Biochem Sci , vol.28 , Issue.12 , pp. 671-678
    • Wehrens, X.H.1    Marks, A.R.2
  • 7
    • 0033825967 scopus 로고    scopus 로고
    • Differential Ca(2+) sensitivity of skeletal and cardiac muscle ryanodine receptors in the presence of calmodulin
    • 10942723
    • Fruen BR Bardy JM Byrem TM: Differential Ca(2+) sensitivity of skeletal and cardiac muscle ryanodine receptors in the presence of calmodulin. Am J Physiol Cell Physiol. 2000;279(3):C724-C733. 10942723
    • (2000) Am J Physiol Cell Physiol , vol.279 , Issue.3 , pp. C724-C733
    • Fruen, B.R.1    Bardy, J.M.2    Byrem, T.M.3
  • 8
    • 0035827726 scopus 로고    scopus 로고
    • Coupled gating between cardiac calcium release channels (ryanodine receptors)
    • 6a, 11397781
    • 6a Marx SO Gaburjakova J Gaburjakova M: Coupled gating between cardiac calcium release channels (ryanodine receptors). Circ Res. 2001;88(11):1151-1158. 11397781 10.1161/hh1101.091268
    • (2001) Circ Res , vol.88 , Issue.11 , pp. 1151-1158
    • Marx, S.O.1    Gaburjakova, J.2    Gaburjakova, M.3
  • 9
    • 0028358901 scopus 로고
    • Stabilization of calcium-release channel (ryanodine receptor) function by Fk506-binding protein
    • 6b, 7514503
    • 6b Brillantes AB Ondrias K Scott A: Stabilization of calcium-release channel (ryanodine receptor) function by Fk506-binding protein. Cell. 1994;77(4):513-523. 7514503 10.1016/0092-8674(94)90214-3
    • (1994) Cell , vol.77 , Issue.4 , pp. 513-523
    • Brillantes, A.B.1    Ondrias, K.2    Scott, A.3
  • 10
    • 0034640113 scopus 로고    scopus 로고
    • PKA phosphorylation dissociates FKBP12.6 from the calcium release channel (ryanodine receptor): defective regulation in failing hearts
    • 10830164
    • Marx SO Reiken S Hisamatsu Y: PKA phosphorylation dissociates FKBP12.6 from the calcium release channel (ryanodine receptor): defective regulation in failing hearts. Cell. 2000;101(4):365-376. 10830164 10.1016/S0092-8674(00)80847-8
    • (2000) Cell , vol.101 , Issue.4 , pp. 365-376
    • Marx, S.O.1    Reiken, S.2    Hisamatsu, Y.3
  • 11
    • 0028840294 scopus 로고
    • Association of sorcin with the cardiac ryanodine receptor
    • 7592856
    • Meyers MB Pickel VM Sheu SS: Association of sorcin with the cardiac ryanodine receptor. J Biol Chem. 1995;270(44):26411-26418. 7592856 10.1074/jbc.270.44.26411
    • (1995) J Biol Chem , vol.270 , Issue.44 , pp. 26411-26418
    • Meyers, M.B.1    Pickel, V.M.2    Sheu, S.S.3
  • 12
    • 0030770826 scopus 로고    scopus 로고
    • Complex formation between junction, triadin, calsequestrin, and the ryanodine receptor. Proteins of the cardiac junctional sarcoplasmic reticulum membrane
    • 9287354
    • Zhang L Kelley J Schmeisser G: Complex formation between junction, triadin, calsequestrin, and the ryanodine receptor. Proteins of the cardiac junctional sarcoplasmic reticulum membrane. J Biol Chem. 1997;272(37):23389-23397. 9287354 10.1074/jbc.272.37.23389
    • (1997) J Biol Chem , vol.272 , Issue.37 , pp. 23389-23397
    • Zhang, L.1    Kelley, J.2    Schmeisser, G.3
  • 13
    • 34548253106 scopus 로고    scopus 로고
    • Comparison of novel echocardiographic parameters of right ventricular function with ejection fraction by cardiac magnetic resonance
    • 17555927
    • Wang J Prakasa K Bomma C: Comparison of novel echocardiographic parameters of right ventricular function with ejection fraction by cardiac magnetic resonance. J Am Soc Echocardiogr. 2007;20(9):1058-1064. 17555927 10.1016/j.echo.2007.01.038
    • (2007) J Am Soc Echocardiogr , vol.20 , Issue.9 , pp. 1058-1064
    • Wang, J.1    Prakasa, K.2    Bomma, C.3
  • 14
    • 79960625443 scopus 로고    scopus 로고
    • The structural biology of ryanodine receptors
    • 11a, 21786194
    • 11a Kimlicka L Van Petegem F: The structural biology of ryanodine receptors. Sci China Life Sci. 2011;54(8):712-724. 21786194 10.1007/s11427-011-4198-2
    • (2011) Sci China Life Sci , vol.54 , Issue.8 , pp. 712-724
    • Kimlicka, L.1    Van Petegem, F.2
  • 15
    • 77955562391 scopus 로고    scopus 로고
    • Ryanodine receptor channelopathies
    • 11b, 20179962, 2885589
    • 11b Betzenhauser MJ Marks AR: Ryanodine receptor channelopathies. Pflugers Arch. 2010;460(2):467-480. 20179962 10.1007/s00424-010-0794-4 2885589
    • (2010) Pflugers Arch , vol.460 , Issue.2 , pp. 467-480
    • Betzenhauser, M.J.1    Marks, A.R.2
  • 16
    • 79954594124 scopus 로고    scopus 로고
    • Inherited dysfunction of sarcoplasmic reticulum Ca2+ handling and arrhythmogenesis
    • 11c, 21454795, 3085083
    • 11c Priori SG Chen SR: Inherited dysfunction of sarcoplasmic reticulum Ca2+ handling and arrhythmogenesis. Circ Res. 2011;108(7):871-883. 21454795 10.1161/CIRCRESAHA.110.226845 3085083
    • (2011) Circ Res , vol.108 , Issue.7 , pp. 871-883
    • Priori, S.G.1    Chen, S.R.2
  • 17
    • 77952673006 scopus 로고    scopus 로고
    • Ryanodine receptor mutations in arrhythmia: The continuing mystery of channel dysfunction
    • 11d, 20132818
    • 11d Thomas NL Maxwell C Mukherjee S: Ryanodine receptor mutations in arrhythmia: The continuing mystery of channel dysfunction. FEBS Lett. 2010;584(10):2153-2160. 20132818 10.1016/j.febslet.2010.01.057
    • (2010) FEBS Lett , vol.584 , Issue.10 , pp. 2153-2160
    • Thomas, N.L.1    Maxwell, C.2    Mukherjee, S.3
  • 18
    • 0030903895 scopus 로고    scopus 로고
    • Identification of a novel protein kinase A anchoring protein that binds both type I and type II regulatory subunits
    • 9065479
    • Huang LJ Durick K Weiner JA: Identification of a novel protein kinase A anchoring protein that binds both type I and type II regulatory subunits. J Biol Chem. 1997;272(12):8057-8064. 9065479 10.1074/jbc.272.12.8057
    • (1997) J Biol Chem , vol.272 , Issue.12 , pp. 8057-8064
    • Huang, L.J.1    Durick, K.2    Weiner, J.A.3
  • 19
    • 80052650221 scopus 로고    scopus 로고
    • Relationships between ligand binding sites, protein architecture and correlated paths of energy and conformational fluctuations
    • 13a, 21832802
    • 13a Erman B: Relationships between ligand binding sites, protein architecture and correlated paths of energy and conformational fluctuations. Phys Biol. 2011;8(5):056003. 21832802 10.1088/1478-3975/8/5/056003
    • (2011) Phys Biol , vol.8 , Issue.5 , pp. 056003
    • Erman, B.1
  • 20
    • 61849151934 scopus 로고    scopus 로고
    • Analysis of correlations between energy and residue fluctuations in native proteins and determination of specific sites for binding
    • 13b, 19257794
    • 13b Haliloglu T Erman B: Analysis of correlations between energy and residue fluctuations in native proteins and determination of specific sites for binding. Phys Rev Lett. 2009;102(8):088103. 19257794 10.1103/PhysRevLett.102.088103
    • (2009) Phys Rev Lett , vol.102 , Issue.8 , pp. 088103
    • Haliloglu, T.1    Erman, B.2
  • 21
    • 44949215646 scopus 로고    scopus 로고
    • Prediction of binding sites in receptor-ligand complexes with the Gaussian Network Model
    • 13c, 18643462
    • 13c Haliloglu T Seyrek E Erman B: Prediction of binding sites in receptor-ligand complexes with the Gaussian Network Model. Phys Rev Lett. 2008;100(22):228102. 18643462 10.1103/PhysRevLett.100.228102
    • (2008) Phys Rev Lett , vol.100 , Issue.22 , pp. 228102
    • Haliloglu, T.1    Seyrek, E.2    Erman, B.3
  • 22
    • 0033536602 scopus 로고    scopus 로고
    • Evolutionarily conserved pathways of energetic connectivity in protein families
    • 14a, 10514373
    • 14a Lockless SW Ranganathan R: Evolutionarily conserved pathways of energetic connectivity in protein families. Science. 1999;286(5438):295-299. 10514373 10.1126/science.286.5438.295
    • (1999) Science , vol.286 , Issue.5438 , pp. 295-299
    • Lockless, S.W.1    Ranganathan, R.2
  • 23
    • 64849111005 scopus 로고    scopus 로고
    • Sending signals dynamically
    • 14b, 19359576, 2921701
    • 14b Smock RG Gierasch LM: Sending signals dynamically. Science. 2009;324(5924):198-203. 19359576 10.1126/science.1169377 2921701
    • (2009) Science , vol.324 , Issue.5924 , pp. 198-203
    • Smock, R.G.1    Gierasch, L.M.2
  • 24
    • 84931290281 scopus 로고    scopus 로고
    • http://www.ccdc.cam.ac.uk/products/life_sciences/gold/
  • 25
    • 61849151934 scopus 로고    scopus 로고
    • Analysis of correlations between energy and residue fluctuations in native proteins and determination of specific sites for binding
    • 16a, 19257794
    • 16a Haliloglu T Erman B: Analysis of correlations between energy and residue fluctuations in native proteins and determination of specific sites for binding. Phys Rev Lett. 2009;102(8):088103-088106. 19257794 10.1103/PhysRevLett.102.088103
    • (2009) Phys Rev Lett , vol.102 , Issue.8 , pp. 088103-088106
    • Haliloglu, T.1    Erman, B.2
  • 26
    • 62249140304 scopus 로고    scopus 로고
    • Statistical thermodynamics of residue fluctuations in native proteins
    • 095103-13, 16b, 19275429
    • 16b Yogurtcu ON Gur M Erman B: Statistical thermodynamics of residue fluctuations in native proteins. J Chem Phys. 2009;130(9):095103-13. 19275429 10.1063/1.3078517
    • (2009) J Chem Phys , vol.130 , Issue.9
    • Yogurtcu, O.N.1    Gur, M.2    Erman, B.3
  • 27
    • 78049307626 scopus 로고    scopus 로고
    • Predicting important residues and interaction pathways in proteins using Gaussian Network Model: binding and stability of HLA proteins
    • 16c, 20628622, 2900293
    • 16c Haliloglu T Gul A Erman B: Predicting important residues and interaction pathways in proteins using Gaussian Network Model: binding and stability of HLA proteins. PLoS Comput Biol. 2010;6(7):e1000845. 20628622 10.1371/journal.pcbi.1000845 2900293
    • (2010) PLoS Comput Biol , vol.6 , Issue.7 , pp. e1000845
    • Haliloglu, T.1    Gul, A.2    Erman, B.3
  • 28
    • 79551555719 scopus 로고    scopus 로고
    • Identification of ligand binding sites of proteins using the Gaussian Network Model
    • 21283550, 3026835
    • Tuzmen C Erman B: Identification of ligand binding sites of proteins using the Gaussian Network Model. PLoS One. 2011;6(1):e16474. 21283550 10.1371/journal.pone.0016474 3026835
    • (2011) PLoS One , vol.6 , Issue.1 , pp. e16474
    • Tuzmen, C.1    Erman, B.2
  • 29
    • 80455164574 scopus 로고    scopus 로고
    • Apo and InsP3-bound crystal structures of the ligand-binding domain of an InsP3 receptor
    • 18a, 21892169, 3242432
    • 18a Lin CC Baek K Lu Z: Apo and InsP 3-bound crystal structures of the ligand-binding domain of an InsP 3 receptor. Nat Struct Mol Biol. 2011;18(10):1172-1174. 21892169 10.1038/nsmb.2112 3242432
    • (2011) Nat Struct Mol Biol , vol.18 , Issue.10 , pp. 1172-1174
    • Lin, C.C.1    Baek, K.2    Lu, Z.3
  • 30
    • 79952546947 scopus 로고    scopus 로고
    • Common allosteric mechanisms between ryanodine and inositol-1,4,5-trisphosphate receptors
    • 18b, 21150295
    • 18b Yuchi Z Van Petegem F: Common allosteric mechanisms between ryanodine and inositol-1,4,5-trisphosphate receptors. Channels (Austin). 2011;5(2):120-123. 21150295 10.4161/chan.5.2.14313
    • (2011) Channels (Austin) , vol.5 , Issue.2 , pp. 120-123
    • Yuchi, Z.1    Van Petegem, F.2
  • 31
    • 84939740624 scopus 로고    scopus 로고
    • Private correspondence
    • van Petegem F: Private correspondence.
    • van Petegem, F.1
  • 32
    • 78751665063 scopus 로고    scopus 로고
    • Correlating allostery with rigidity
    • 21060909
    • Rader AJ Brown SM: Correlating allostery with rigidity. Mol Biosyst. 2011;7(2):464-471. 21060909 10.1039/c0mb00054j
    • (2011) Mol Biosyst , vol.7 , Issue.2 , pp. 464-471
    • Rader, A.J.1    Brown, S.M.2
  • 33
    • 67650469595 scopus 로고    scopus 로고
    • Crystal structure of type 1 ryanodine receptor amino-terminal beta-trefoil domain reveals a disease-associated mutation "hot spot? loop
    • 19541610, 2708722
    • Amador FJ Liu S Ishiyama N: Crystal structure of type 1 ryanodine receptor amino-terminal beta-trefoil domain reveals a disease-associated mutation "hot spot? loop. Proc Natl Acad Sci U S A. 2009;106(27):11040-11044. 19541610 10.1073/pnas.0905186106 2708722
    • (2009) Proc Natl Acad Sci U S A , vol.106 , Issue.27 , pp. 11040-11044
    • Amador, F.J.1    Liu, S.2    Ishiyama, N.3
  • 34
    • 84931290282 scopus 로고    scopus 로고
    • Reference Source
    • PDBSUM. Reference Source
  • 35
    • 84931290283 scopus 로고    scopus 로고
    • Data of predicted PKA binding sites on RyR2
    • Data Source
    • Erman B Walpoth BN Erman B: Data of predicted PKA binding sites on RyR2. figshare. 2015. Data Source
    • (2015) figshare
    • Erman, B.1    Walpoth, B.N.2    Erman, B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.