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Volumn 96, Issue 5, 2009, Pages 1770-1785

CaMKII-induced shift in modal gating explains L-type Ca2+ current facilitation: A modeling study

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM CALMODULIN DEPENDENT PROTEIN KINASE II; CALCIUM CHANNEL L TYPE; CALMODULIN; PHOSPHATASE; CALCIUM;

EID: 65549160090     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2008.11.055     Document Type: Article
Times cited : (45)

References (80)
  • 1
    • 0036702526 scopus 로고    scopus 로고
    • Calcium, calmodulin, and calcium-calmodulin kinase II: Heartbeat to heartbeat and beyond
    • Maier, L. S., and D. M. Bers. 2002. Calcium, calmodulin, and calcium-calmodulin kinase II: heartbeat to heartbeat and beyond. J. Mol. Cell. Cardiol. 34:919-939.
    • (2002) J. Mol. Cell. Cardiol , vol.34 , pp. 919-939
    • Maier, L.S.1    Bers, D.M.2
  • 2
    • 33846858884 scopus 로고    scopus 로고
    • 2+/calmodulin- dependent protein kinase (CaMK) in excitation-contraction coupling in the heart
    • 2+/calmodulin- dependent protein kinase (CaMK) in excitation-contraction coupling in the heart. Cardiovasc. Res. 73:631-640.
    • (2007) Cardiovasc. Res , vol.73 , pp. 631-640
    • Maier, L.S.1    Bers, D.M.2
  • 3
    • 0032239112 scopus 로고    scopus 로고
    • ++/calmodulin-dependent protein kinase, decreases early afterdepolarizations in rabbit heart
    • ++/calmodulin-dependent protein kinase, decreases early afterdepolarizations in rabbit heart. J. Pharmacol. Exp. Ther. 287:996-1006.
    • (1998) J. Pharmacol. Exp. Ther , vol.287 , pp. 996-1006
    • Anderson, M.E.1    Braun, A.P.2    Wu, Y.3    Lu, T.4    Wu, Y.5
  • 6
    • 3242744450 scopus 로고    scopus 로고
    • 2+/calmodulin- dependent protein kinase II in cardiac hypertrophy and heart failure
    • 2+/calmodulin- dependent protein kinase II in cardiac hypertrophy and heart failure. Cardiovasc. Res. 63:476-486.
    • (2004) Cardiovasc. Res , vol.63 , pp. 476-486
    • Zhang, T.1    Brown, J.H.2
  • 7
    • 33644865926 scopus 로고    scopus 로고
    • Increased sarcoplasmic reticulum calcium leak but unaltered contractility by acute camkii overexpression in isolated rabbit cardiac myocytes
    • Kohlhaas, M., T. Zhang, T. Seidler, D. Zibrova, N. Dybkova, et al. 2006. Increased sarcoplasmic reticulum calcium leak but unaltered contractility by acute camkii overexpression in isolated rabbit cardiac myocytes. Circ. Res. 98:235-244.
    • (2006) Circ. Res , vol.98 , pp. 235-244
    • Kohlhaas, M.1    Zhang, T.2    Seidler, T.3    Zibrova, D.4    Dybkova, N.5
  • 8
    • 0038643583 scopus 로고    scopus 로고
    • Transgenic CaMKIIδC overexpression uniquely alters cardiac myocyte Ca2+ handling: Reduced SR Ca2+ load and activated SR Ca2+ release
    • Maier, L. S., T. Zhang, L. Chen, J. DeSantiago, J. H. Brown, et al. 2003. Transgenic CaMKIIδC overexpression uniquely alters cardiac myocyte Ca2+ handling: reduced SR Ca2+ load and activated SR Ca2+ release. Circ. Res. 92:904-911.
    • (2003) Circ. Res , vol.92 , pp. 904-911
    • Maier, L.S.1    Zhang, T.2    Chen, L.3    DeSantiago, J.4    Brown, J.H.5
  • 15
    • 0027966195 scopus 로고
    • Ca-dependent facilitation of cardiac Ca current is due to Ca-calmodulin-dependent protein kinase
    • Yuan, W., and D. M. Bers. 1994. Ca-dependent facilitation of cardiac Ca current is due to Ca-calmodulin-dependent protein kinase. Am. J. Physiol. Heart Circ. Physiol. 267:H982-H993.
    • (1994) Am. J. Physiol. Heart Circ. Physiol , vol.267
    • Yuan, W.1    Bers, D.M.2
  • 16
    • 0033781028 scopus 로고    scopus 로고
    • Calmodulin kinase determines calcium-dependent facilitation of L-type calcium channels
    • Dzhura, I., Y. Wu, R. J. Colbran, J. R. Balser, and M. E. Anderson. 2000. Calmodulin kinase determines calcium-dependent facilitation of L-type calcium channels. Nat. Cell Biol. 2:173-177.
    • (2000) Nat. Cell Biol , vol.2 , pp. 173-177
    • Dzhura, I.1    Wu, Y.2    Colbran, R.J.3    Balser, J.R.4    Anderson, M.E.5
  • 18
    • 33748741562 scopus 로고    scopus 로고
    • Calmodulin kinase II is involved in voltage-dependent facilitation of the L-type Cav1.2 calcium channel: Identification of the phosphorylation sites
    • Lee, T. -S., R. Karl, S. Moosmang, P. Lenhardt, N. Klugbauer, et al. 2006. Calmodulin kinase II is involved in voltage-dependent facilitation of the L-type Cav1.2 calcium channel: identification of the phosphorylation sites. J. Biol. Chem. 281:25560-25567.
    • (2006) J. Biol. Chem , vol.281 , pp. 25560-25567
    • Lee, T.-S.1    Karl, R.2    Moosmang, S.3    Lenhardt, P.4    Klugbauer, N.5
  • 19
    • 33745751387 scopus 로고    scopus 로고
    • 2+]i in rat ventricular myocytes
    • 2+]i in rat ventricular myocytes. J. Physiol. 574:509-518.
    • (2006) J. Physiol , vol.574 , pp. 509-518
    • Guo, J.1    Duff, H.J.2
  • 20
    • 0030906866 scopus 로고    scopus 로고
    • 2+-calmodulin-dependent protein kinase II on cardiac excitation-contraction coupling in ferret ventricular myocytes
    • 2+-calmodulin-dependent protein kinase II on cardiac excitation-contraction coupling in ferret ventricular myocytes. J. Physiol. 501:17-31.
    • (1997) J. Physiol , vol.501 , pp. 17-31
    • Li, L.1    Satoh, H.2    Ginsburg, K.S.3    Bers, D.M.4
  • 21
    • 0025124412 scopus 로고
    • β-adrenergic stimulation of calcium channels occurs by potentiation of high-activity gating modes
    • Yue, D. T., S. Herzig, and E. Marban. 1990. β-adrenergic stimulation of calcium channels occurs by potentiation of high-activity gating modes. Proc. Natl. Acad. Sci. USA. 87:753-757.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 753-757
    • Yue, D.T.1    Herzig, S.2    Marban, E.3
  • 24
    • 0026718175 scopus 로고
    • Calmodulin trapping by calcium-calmodulin-dependent protein kinase
    • Meyer, T., P. I. Hanson, L. Stryer, and H. Schulman. 1992. Calmodulin trapping by calcium-calmodulin-dependent protein kinase. Science. 256:1199-1202.
    • (1992) Science , vol.256 , pp. 1199-1202
    • Meyer, T.1    Hanson, P.I.2    Stryer, L.3    Schulman, H.4
  • 25
    • 0022519298 scopus 로고
    • 2+-triggered molecular switch
    • 2+-triggered molecular switch. Cell. 44:861-870.
    • (1986) Cell , vol.44 , pp. 861-870
    • Miller, S.G.1    Kennedy, M.B.2
  • 27
    • 0028306195 scopus 로고
    • Dual role of calmodulin in autophosphorylation of multifunctional CaM kinase may underlie decoding of calcium signals
    • Hanson, P. I., T. Meyer, L. Stryer, and H. Schulman. 1994. Dual role of calmodulin in autophosphorylation of multifunctional CaM kinase may underlie decoding of calcium signals. Neuron. 12:943-956.
    • (1994) Neuron , vol.12 , pp. 943-956
    • Hanson, P.I.1    Meyer, T.2    Stryer, L.3    Schulman, H.4
  • 28
    • 0035544717 scopus 로고    scopus 로고
    • Transient versus asymptotic dynamics of CaM kinase II: Possible roles of phosphatase
    • Kubota, Y., and J. M. Bower. 2001. Transient versus asymptotic dynamics of CaM kinase II: possible roles of phosphatase. J. Comput. Neurosci. 11:263-279.
    • (2001) J. Comput. Neurosci , vol.11 , pp. 263-279
    • Kubota, Y.1    Bower, J.M.2
  • 29
    • 0034116677 scopus 로고    scopus 로고
    • Models of calmodulin trapping and CaM kinase II activation in a dendritic spine
    • Holmes, W. R. 2000. Models of calmodulin trapping and CaM kinase II activation in a dendritic spine. J. Comput. Neurosci. 8:65-86.
    • (2000) J. Comput. Neurosci , vol.8 , pp. 65-86
    • Holmes, W.R.1
  • 30
    • 8744246332 scopus 로고    scopus 로고
    • Rate dependence and regulation of action potential and calcium transient in a canine cardiac ventricular cell model
    • Hund, T. J., and Y. Rudy. 2004. Rate dependence and regulation of action potential and calcium transient in a canine cardiac ventricular cell model. Circulation. 110:3168-3174.
    • (2004) Circulation , vol.110 , pp. 3168-3174
    • Hund, T.J.1    Rudy, Y.2
  • 31
    • 34447525230 scopus 로고    scopus 로고
    • 2+ and electrical alternans in cardiac myocytes: Role of CaMKII and repolarizing currents
    • 2+ and electrical alternans in cardiac myocytes: role of CaMKII and repolarizing currents. Am. J. Physiol. Heart Circ. Physiol. 292:H2854-H2866.
    • (2007) Am. J. Physiol. Heart Circ. Physiol , vol.292
    • Livshitz, L.M.1    Rudy, Y.2
  • 32
    • 36849057068 scopus 로고    scopus 로고
    • Simulation of Ca-calmodulin-dependent protein kinase II on rabbit ventricular myocyte ion currents and action potentials
    • Grandi, E., J. L. Puglisi, S. Wagner, L. S. Maier, S. Severi, et al. 2007. Simulation of Ca-calmodulin-dependent protein kinase II on rabbit ventricular myocyte ion currents and action potentials. Biophys. J. 93:3835-3847.
    • (2007) Biophys. J , vol.93 , pp. 3835-3847
    • Grandi, E.1    Puglisi, J.L.2    Wagner, S.3    Maier, L.S.4    Severi, S.5
  • 33
    • 28344445756 scopus 로고    scopus 로고
    • Structure of the autoinhibited kinase domain of CAMKII and SAXS analysis of the holoenzyme
    • Rosenberg, O. S., S. Deindl, R. -J. Sung, A. C. Nairn, and J. Kuriyan. 2005. Structure of the autoinhibited kinase domain of CAMKII and SAXS analysis of the holoenzyme. Cell. 123:849-860.
    • (2005) Cell , vol.123 , pp. 849-860
    • Rosenberg, O.S.1    Deindl, S.2    Sung, R.-J.3    Nairn, A.C.4    Kuriyan, J.5
  • 34
    • 0034640259 scopus 로고    scopus 로고
    • Three-dimensional reconstructions of calcium/calmodulin-dependent (CaM) kinase IIα and truncated CaM kinase IIα reveal a unique organization for its structural core and functional domains
    • Kolodziej, S. J., A. Hudmon, M. N. Waxham, and J. K. Stoops. 2000. Three-dimensional reconstructions of calcium/calmodulin-dependent (CaM) kinase IIα and truncated CaM kinase IIα reveal a unique organization for its structural core and functional domains. J. Biol. Chem. 275:14354-14359.
    • (2000) J. Biol. Chem , vol.275 , pp. 14354-14359
    • Kolodziej, S.J.1    Hudmon, A.2    Waxham, M.N.3    Stoops, J.K.4
  • 35
    • 0035917320 scopus 로고    scopus 로고
    • Oligomeric structure of α-calmodulin-dependent protein kinase II
    • Morris, E. P., and K. Török. 2001. Oligomeric structure of α-calmodulin-dependent protein kinase II. J. Mol. Biol. 308:1-8.
    • (2001) J. Mol. Biol , vol.308 , pp. 1-8
    • Morris, E.P.1    Török, K.2
  • 38
    • 0026733599 scopus 로고
    • Theory of excitation-contraction coupling in cardiac muscle
    • Stern, M. D. 1992. Theory of excitation-contraction coupling in cardiac muscle. Biophys. J. 63:497-517.
    • (1992) Biophys. J , vol.63 , pp. 497-517
    • Stern, M.D.1
  • 39
    • 0037097022 scopus 로고    scopus 로고
    • 2+/calmodulin-dependent protein kinase II
    • 2+/calmodulin-dependent protein kinase II. Biochem. J. 364:593-611.
    • (2002) Biochem. J , vol.364 , pp. 593-611
    • Hudmon, A.1    Schulman, H.2
  • 40
    • 33847363658 scopus 로고    scopus 로고
    • Temporal dissociation of frequency-dependent acceleration of relaxation and protein phosphorylation by CaMKII
    • Huke, S., and D. M. Bers. 2007. Temporal dissociation of frequency-dependent acceleration of relaxation and protein phosphorylation by CaMKII. J. Mol. Cell. Cardiol. 42:590-599.
    • (2007) J. Mol. Cell. Cardiol , vol.42 , pp. 590-599
    • Huke, S.1    Bers, D.M.2
  • 41
    • 0022929859 scopus 로고
    • 2+(calmodulin)- dependent protein kinase II by an autophosphorylation mechanism
    • 2+(calmodulin)- dependent protein kinase II by an autophosphorylation mechanism. J. Biol. Chem. 261:8581-8584.
    • (1986) J. Biol. Chem , vol.261 , pp. 8581-8584
    • Schworer, C.M.1    Colbran, R.J.2    Soderling, T.R.3
  • 42
    • 0027340006 scopus 로고
    • 2+/calmodulin-dependent protein kinase II by basal autophosphorylation
    • 2+/calmodulin-dependent protein kinase II by basal autophosphorylation. J. Biol. Chem. 268:7163-7170.
    • (1993) J. Biol. Chem , vol.268 , pp. 7163-7170
    • Colbran, R.J.1
  • 43
    • 0026806967 scopus 로고
    • 2+/calmodulin- dependent protein kinase analyzed by site-directed mutagenesis
    • 2+/calmodulin- dependent protein kinase analyzed by site-directed mutagenesis. J. Biol. Chem. 267:17216-17224.
    • (1992) J. Biol. Chem , vol.267 , pp. 17216-17224
    • Hanson, P.I.1    Schulman, H.2
  • 44
    • 0035858868 scopus 로고    scopus 로고
    • Phosphorylation-dependent regulation of ryanodine receptors: A novel role for leucine/isoleucine zippers
    • Marx, S. O., S. Reiken, Y. Hisamatsu, M. Gaburjakova, J. Gaburjakova, et al. 2001. Phosphorylation-dependent regulation of ryanodine receptors: a novel role for leucine/isoleucine zippers. J. Cell Biol. 153:699-708.
    • (2001) J. Cell Biol , vol.153 , pp. 699-708
    • Marx, S.O.1    Reiken, S.2    Hisamatsu, Y.3    Gaburjakova, M.4    Gaburjakova, J.5
  • 45
    • 3042763171 scopus 로고    scopus 로고
    • 2+/calmodulin-dependent protein kinase II phosphorylation regulates the cardiac ryanodine receptor
    • 2+/calmodulin-dependent protein kinase II phosphorylation regulates the cardiac ryanodine receptor. Circ. Res. 94:e61-e70.
    • (2004) Circ. Res , vol.94
    • Wehrens, X.H.T.1    Lehnart, S.E.2    Reiken, S.R.3    Marks, A.R.4
  • 47
    • 0034671738 scopus 로고    scopus 로고
    • Protein phosphatase 2A is associated with class C L-type calcium channels (Cav1.2) and antagonizes channel phosphorylation by cAMP-dependent protein kinase
    • Davare, M. A., M. C. Horne, and J. W. Hell. 2000. Protein phosphatase 2A is associated with class C L-type calcium channels (Cav1.2) and antagonizes channel phosphorylation by cAMP-dependent protein kinase. J. Biol. Chem. 275:39710-39717.
    • (2000) J. Biol. Chem , vol.275 , pp. 39710-39717
    • Davare, M.A.1    Horne, M.C.2    Hell, J.W.3
  • 49
    • 0031594597 scopus 로고    scopus 로고
    • 2+ dynamics: The roles of ryanodine receptor adaptation and sarcoplasmic reticulum load
    • 2+ dynamics: the roles of ryanodine receptor adaptation and sarcoplasmic reticulum load. Biophys. J. 74:1149-1168.
    • (1998) Biophys. J , vol.74 , pp. 1149-1168
    • Jafri, M.S.1    Rice, J.J.2    Winslow, R.L.3
  • 50
    • 0032401951 scopus 로고    scopus 로고
    • Control of L-type calcium current during the action potential of guinea-pig ventricular myocytes
    • Linz, K. W., and R. Meyer. 1998. Control of L-type calcium current during the action potential of guinea-pig ventricular myocytes. J. Physiol. 513:425-442.
    • (1998) J. Physiol , vol.513 , pp. 425-442
    • Linz, K.W.1    Meyer, R.2
  • 51
  • 52
    • 34247887625 scopus 로고    scopus 로고
    • Protein geometry and placement in the cardiac dyad influence macroscopic properties of calcium-induced calcium release
    • Tanskanen, A. J., J. L. Greenstein, A. Chen, S. X. Sun, and R. L. Winslow. 2007. Protein geometry and placement in the cardiac dyad influence macroscopic properties of calcium-induced calcium release. Biophys. J. 92:3379-3396.
    • (2007) Biophys. J , vol.92 , pp. 3379-3396
    • Tanskanen, A.J.1    Greenstein, J.L.2    Chen, A.3    Sun, S.X.4    Winslow, R.L.5
  • 54
    • 0026885495 scopus 로고
    • Rate dependence of action potential duration and calcium current in isolated guinea-pig cardiocytes
    • Peineau, N., D. Garnier, and J. A. Argibay. 1992. Rate dependence of action potential duration and calcium current in isolated guinea-pig cardiocytes. Exp. Physiol. 77:615-625.
    • (1992) Exp. Physiol , vol.77 , pp. 615-625
    • Peineau, N.1    Garnier, D.2    Argibay, J.A.3
  • 55
    • 0028300397 scopus 로고
    • Relaxation in rabbit and rat cardiac cells: Species-dependent differences in cellular mechanisms
    • Bassani, J. W., R. A. Bassani, and D. M. Bers. 1994. Relaxation in rabbit and rat cardiac cells: species-dependent differences in cellular mechanisms. J. Physiol. 476:279-293.
    • (1994) J. Physiol , vol.476 , pp. 279-293
    • Bassani, J.W.1    Bassani, R.A.2    Bers, D.M.3
  • 56
    • 0034683082 scopus 로고    scopus 로고
    • Calcium fluxes involved in control of cardiac myocyte contraction
    • Bers, D. M. 2000. Calcium fluxes involved in control of cardiac myocyte contraction. Circ. Res. 87:275-281.
    • (2000) Circ. Res , vol.87 , pp. 275-281
    • Bers, D.M.1
  • 57
    • 0025082249 scopus 로고
    • Ca current facilitation during postrest recovery depends on Ca entry
    • Hryshko, L. V., and D. M. Bers. 1990. Ca current facilitation during postrest recovery depends on Ca entry. Am. J. Physiol. Heart Circ. Physiol. 259:H951-H961.
    • (1990) Am. J. Physiol. Heart Circ. Physiol , vol.259
    • Hryshko, L.V.1    Bers, D.M.2
  • 58
    • 0023680261 scopus 로고
    • Calcium current restitution in mammalian ventricular myocytes is modulated by intracellular calcium
    • Tseng, G. N. 1988. Calcium current restitution in mammalian ventricular myocytes is modulated by intracellular calcium. Circ. Res. 63:468-482.
    • (1988) Circ. Res , vol.63 , pp. 468-482
    • Tseng, G.N.1
  • 59
    • 0033583266 scopus 로고    scopus 로고
    • Winslow, R. L., J. Rice, S. Jafri, E. Marban, and B. O'Rourke. 1999. Mechanisms of altered excitation-contraction coupling in canine tachycardia-induced heart failure, II: model studies. Circ. Res. 84:571-586.
    • Winslow, R. L., J. Rice, S. Jafri, E. Marban, and B. O'Rourke. 1999. Mechanisms of altered excitation-contraction coupling in canine tachycardia-induced heart failure, II: model studies. Circ. Res. 84:571-586.
  • 60
    • 0026542534 scopus 로고
    • Intracellular calcium handling in isolated ventricular myocytes from patients with terminal heart failure
    • Beuckelmann, D. J., M. Nabauer, and E. Erdmann. 1992. Intracellular calcium handling in isolated ventricular myocytes from patients with terminal heart failure. Circulation. 85:1046-1055.
    • (1992) Circulation , vol.85 , pp. 1046-1055
    • Beuckelmann, D.J.1    Nabauer, M.2    Erdmann, E.3
  • 61
    • 0023189660 scopus 로고
    • Abnormal intracellular calcium handling in myocardium from patients with end-stage heart failure
    • Gwathmey, J. K., L. Copelas, R. MacKinnon, F. J. Schoen, M. D. Feldman, et al. 1987. Abnormal intracellular calcium handling in myocardium from patients with end-stage heart failure. Circ. Res. 61:70-76.
    • (1987) Circ. Res , vol.61 , pp. 70-76
    • Gwathmey, J.K.1    Copelas, L.2    MacKinnon, R.3    Schoen, F.J.4    Feldman, M.D.5
  • 62
    • 20244377242 scopus 로고    scopus 로고
    • Enhancement of cardiac function and suppression of heart failure progression by inhibition of protein phosphatase 1
    • Pathak, A., F. del Monte, W. Zhao, J. -E. Schultz, J. N. Lorenz, et al. 2005. Enhancement of cardiac function and suppression of heart failure progression by inhibition of protein phosphatase 1. Circ. Res. 96:756-766.
    • (2005) Circ. Res , vol.96 , pp. 756-766
    • Pathak, A.1    del Monte, F.2    Zhao, W.3    Schultz, J.-E.4    Lorenz, J.N.5
  • 63
    • 33845611066 scopus 로고    scopus 로고
    • Inhibition of protein phosphatase 1 by inhibitor-2 gene delivery ameliorates heart failure progression in genetic cardiomyopathy
    • Yamada, M., Y. Ikeda, M. Yano, K. Yoshimura, S. Nishino, et al. 2006. Inhibition of protein phosphatase 1 by inhibitor-2 gene delivery ameliorates heart failure progression in genetic cardiomyopathy. FASEB J. 20:1197-1199.
    • (2006) FASEB J , vol.20 , pp. 1197-1199
    • Yamada, M.1    Ikeda, Y.2    Yano, M.3    Yoshimura, K.4    Nishino, S.5
  • 64
    • 4644323242 scopus 로고    scopus 로고
    • Overexpression of the catalytic subunit of protein phosphatase 2A impairs cardiac function
    • Gergs, U., P. Boknik, I. Buchwalow, L. Fabritz, M. Matus, et al. 2004. Overexpression of the catalytic subunit of protein phosphatase 2A impairs cardiac function. J. Biol. Chem. 279:40827-40834.
    • (2004) J. Biol. Chem , vol.279 , pp. 40827-40834
    • Gergs, U.1    Boknik, P.2    Buchwalow, I.3    Fabritz, L.4    Matus, M.5
  • 65
    • 0024455621 scopus 로고
    • Tissue-specific expression of four types of rat calmodulin-dependent protein kinase II mRNAs
    • Tobimatsu, T., and H. Fujisawa. 1989. Tissue-specific expression of four types of rat calmodulin-dependent protein kinase II mRNAs. J. Biol. Chem. 264:17907-17912.
    • (1989) J. Biol. Chem , vol.264 , pp. 17907-17912
    • Tobimatsu, T.1    Fujisawa, H.2
  • 66
    • 1842425022 scopus 로고    scopus 로고
    • Comparative analyses of the three-dimensional structures and enzymatic properties of α-, β-, γ-, and δ-isoforms of Ca2+-calmodulin-dependent protein kinase II
    • Gaertner, T. R., S. J. Kolodziej, D. Wang, R. Kobayashi, J. M. Koomen, et al. 2004. Comparative analyses of the three-dimensional structures and enzymatic properties of α-, β-, γ-, and δ-isoforms of Ca2+-calmodulin-dependent protein kinase II. J. Biol. Chem. 279: 12484-12494.
    • (2004) J. Biol. Chem , vol.279 , pp. 12484-12494
    • Gaertner, T.R.1    Kolodziej, S.J.2    Wang, D.3    Kobayashi, R.4    Koomen, J.M.5
  • 67
    • 0034640113 scopus 로고    scopus 로고
    • PKA phosphorylation dissociates FKBP12.6 from the calcium release channel (ryanodine receptor): Defective regulation in failing hearts
    • Marx, S. O., S. Reiken, Y. Hisamatsu, T. Jayaraman, D. Burkhoff, et al. 2000. PKA phosphorylation dissociates FKBP12.6 from the calcium release channel (ryanodine receptor): defective regulation in failing hearts. Cell. 101:365-376.
    • (2000) Cell , vol.101 , pp. 365-376
    • Marx, S.O.1    Reiken, S.2    Hisamatsu, Y.3    Jayaraman, T.4    Burkhoff, D.5
  • 69
    • 0033958106 scopus 로고    scopus 로고
    • Decreased protein phosphatase 2A activity in hippocampal long-term potentiation
    • Fukunaga, K., D. Muller, M. Ohmitsu, E. Bakó , A. A. DePaoli-Roach, et al. 2000. Decreased protein phosphatase 2A activity in hippocampal long-term potentiation. J. Neurochem. 74:807-817.
    • (2000) J. Neurochem , vol.74 , pp. 807-817
    • Fukunaga, K.1    Muller, D.2    Ohmitsu, M.3    Bakó, E.4    DePaoli-Roach, A.A.5
  • 70
    • 0017130995 scopus 로고
    • Separation and characterization of two phosphorylase phosphatase inhibitors from rabbit skeletal muscle
    • Freesia, L., and W. H. G. Huang. 1976. Separation and characterization of two phosphorylase phosphatase inhibitors from rabbit skeletal muscle. Eur. J. Biochem. 70:419-426.
    • (1976) Eur. J. Biochem , vol.70 , pp. 419-426
    • Freesia, L.1    Huang, W.H.G.2
  • 71
    • 0029870187 scopus 로고    scopus 로고
    • Multiple structural elements define the specificity of recombinant human inhibitor-1 as a protein phosphatase-1 inhibitor
    • Endo, S., X. Zhou, J. Connor, B. Wang, and S. Shenolikar. 1996. Multiple structural elements define the specificity of recombinant human inhibitor-1 as a protein phosphatase-1 inhibitor. Biochemistry. 35:5220-5228.
    • (1996) Biochemistry , vol.35 , pp. 5220-5228
    • Endo, S.1    Zhou, X.2    Connor, J.3    Wang, B.4    Shenolikar, S.5
  • 72
    • 0032546994 scopus 로고    scopus 로고
    • Gating of CaMKII by cAMP-regulated protein phosphatase activity during LTP
    • Blitzer, R. D., J. H. Connor, G. P. Brown, T. Wong, S. Shenolikar, et al. 1998. Gating of CaMKII by cAMP-regulated protein phosphatase activity during LTP. Science. 280:1940-1943.
    • (1998) Science , vol.280 , pp. 1940-1943
    • Blitzer, R.D.1    Connor, J.H.2    Brown, G.P.3    Wong, T.4    Shenolikar, S.5
  • 73
    • 0029583122 scopus 로고
    • Crystal structure of the catalytic subunit of human protein phosphatase 1 and its complex with tungstate
    • Egloff, M. -P., P. T. W. Cohen, P. Reinemer, and D. Barford. 1995. Crystal structure of the catalytic subunit of human protein phosphatase 1 and its complex with tungstate. J. Mol. Biol. 254:942-959.
    • (1995) J. Mol. Biol , vol.254 , pp. 942-959
    • Egloff, M.-P.1    Cohen, P.T.W.2    Reinemer, P.3    Barford, D.4
  • 74
    • 0034647344 scopus 로고    scopus 로고
    • 2+ channels both depend on specific amino acid residues in a consensus calmodulin-binding motif in the α 1C subunit
    • 2+ channels both depend on specific amino acid residues in a consensus calmodulin-binding motif in the α 1C subunit. J. Biol. Chem. 275:21121-21129.
    • (2000) J. Biol. Chem , vol.275 , pp. 21121-21129
    • Zuhlke, R.D.1    Pitt, G.S.2    Tsien, R.W.3    Reuter, H.4
  • 75
    • 0019860734 scopus 로고
    • Studies on phosphorylation of canine cardiac sarcoplasmic reticulum by calmodulin-dependent protein kinase
    • Bilezikjian, L. M., E. G. Kranias, J. D. Potter, and A. Schwartz. 1981. Studies on phosphorylation of canine cardiac sarcoplasmic reticulum by calmodulin-dependent protein kinase. Circ. Res. 49:1356-1362.
    • (1981) Circ. Res , vol.49 , pp. 1356-1362
    • Bilezikjian, L.M.1    Kranias, E.G.2    Potter, J.D.3    Schwartz, A.4
  • 76
    • 0020323508 scopus 로고
    • 2+)- activated ATPase activity in isolated cardiac sarcoplasmic reticulum
    • 2+)- activated ATPase activity in isolated cardiac sarcoplasmic reticulum. J. Biol. Chem. 257:5685-5691.
    • (1982) J. Biol. Chem , vol.257 , pp. 5685-5691
    • Kirchberger, M.A.1    Antonetz, T.2
  • 77
    • 0018674267 scopus 로고
    • Concerted regulation of cardiac sarcoplasmic reticulum calcium transport by cyclic adenosine monophosphate dependent and calcium-calmodulin-dependent phosphorylations
    • Le Peuch, C. J., J. Haiech, and J. G. Demaille. 1979. Concerted regulation of cardiac sarcoplasmic reticulum calcium transport by cyclic adenosine monophosphate dependent and calcium-calmodulin-dependent phosphorylations. Biochemistry. 18:5150-5157.
    • (1979) Biochemistry , vol.18 , pp. 5150-5157
    • Le Peuch, C.J.1    Haiech, J.2    Demaille, J.G.3
  • 78
    • 0029080486 scopus 로고
    • Modulation of cardiac ryanodine receptors of swine and rabbit by a phosphorylation-dephosphorylation mechanism
    • Lokuta, A. J., T. B. Rogers, W. J. Lederer, and H. H. Valdivia. 1995. Modulation of cardiac ryanodine receptors of swine and rabbit by a phosphorylation-dephosphorylation mechanism. J. Physiol. 487:609-622.
    • (1995) J. Physiol , vol.487 , pp. 609-622
    • Lokuta, A.J.1    Rogers, T.B.2    Lederer, W.J.3    Valdivia, H.H.4
  • 79
    • 0025772161 scopus 로고
    • Unique phosphorylation site on the cardiac ryanodine receptor regulates calcium channel activity
    • Witcher, D. R., R. J. Kovacs, H. Schulman, D. C. Cefali, and L. R. Jones. 1991. Unique phosphorylation site on the cardiac ryanodine receptor regulates calcium channel activity. J. Biol. Chem. 266:11144-11152.
    • (1991) J. Biol. Chem , vol.266 , pp. 11144-11152
    • Witcher, D.R.1    Kovacs, R.J.2    Schulman, H.3    Cefali, D.C.4    Jones, L.R.5


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