The CaMKII inhibitor KN93-calmodulin interaction and implications for calmodulin tuning of NaV1.5 and RyR2 function
Tài liệu tham khảo
Sorensen, 2013, Calmodulin in a heartbeat, FEBS J., 280, 5511, 10.1111/febs.12337
Kursula, 2014, The many structural faces of calmodulin: a multitasking molecular jackknife, Amino Acids, 10.1007/s00726-014-1795-y
D.M. Bers (Ed.), Excitation-Contraction Coupling and Cardiac Contractile Force, 2002.
Pitt, 2007, Calmodulin and CaMKII as molecular switches for cardiac ion channels, Cardiovasc. Res., 73, 641, 10.1016/j.cardiores.2006.10.019
Barbato, 1992, Backbone dynamics of calmodulin studied by 15N relaxation using inverse detected two-dimensional NMR spectroscopy: the central Helix Is flexible, Biochemistry, 31, 5269, 10.1021/bi00138a005
Babu, 1988, Structure of calmodulin refined at 2.2 Å resolution, J. Mol. Biol., 204, 191, 10.1016/0022-2836(88)90608-0
Sorensen, 1998, Interactions between Domains of Apo Calmodulin Alter Calcium Binding and stability, Biochemistry, 2960, 4244, 10.1021/bi9718200
Tsalkova, 1985, Thermodynamic study of domain organization in troponin C and calmodulin, J. Mol. Biol., 181, 533, 10.1016/0022-2836(85)90425-5
Teleman, 1986, Kinetics of Ca2+binding to calmodulin and its tryptic fragments studied by43Ca-NMR, Biochim. Biophys. Acta (BBA)/Protein Struct. Mol., 873, 204
Bayley, 1984, The kinetics of calcium binding to calmodulin: quin 2 and ANS stopped-flow fluorescence studies, Biochem. Biophys. Res. Commun., 120, 185, 10.1016/0006-291X(84)91431-1
Kovalevskaya, 2013, Structural analysis of calmodulin binding to ion channels demonstrates the role of its plasticity in regulation, Pflugers Arch., 465, 1507, 10.1007/s00424-013-1278-0
Chao, 2011, A mechanism for tunable autoinhibition in the structure of a human Ca2+/calmodulin- dependent kinase II holoenzyme, Cell, 146, 732, 10.1016/j.cell.2011.07.038
Pellicena, 2014, CaMKII inhibitors: from research tools to therapeutic agents, Front. Pharmacol., 5, 1
Sumi, 1991, The newly synthesized selective Ca2+calmodulin dependent protein kinase II inhibitor KN-93 reduces dopamine contents in PC12h cells, Biochem. Biophys. Res. Commun., 181, 968, 10.1016/0006-291X(91)92031-E
Ishida, 1995, A novel highly specific and potent inhibitor of calmodulin-dependent protein kinase II, Biochem. Biophys. Res. Commun., 212, 806, 10.1006/bbrc.1995.2040
Johnson, 2018, A mechanism of calmodulin modulation of the human cardiac sodium channel, Structure, 26, 10.1016/j.str.2018.03.005
Herren, 2015, CaMKII phosphorylation of Na V 1.5: novel in vitro sites identified by mass spectrometry and reduced S516 phosphorylation in human heart failure HHS public access, J. Proteome Res., 14, 2298, 10.1021/acs.jproteome.5b00107
Glynn, 2015, Voltage-gated sodium channel phosphorylation at Ser571 regulates late current, arrhythmia, and cardiac function in vivo, Circulation, 132, 567, 10.1161/CIRCULATIONAHA.114.015218
Oort, 2010, Ryanodine receptor phosphorylation by CaMKII promotes life- threatening ventricular arrhythmias in mice with heart failure, Circulation, 122, 2669, 10.1161/CIRCULATIONAHA.110.982298
Walweel, 2017, The emerging role of calmodulin regulation of RyR2 in controlling heart rhythm, the progression of heart failure and the antiarrhythmic action of dantrolene, Clin. Exp. Pharmacol. Physiol., 44, 135, 10.1111/1440-1681.12669
Walweel, 2019, Calmodulin inhibition of human RyR2 channels requires phosphorylation of RyR2-S2808 or RyR2-S2814, J. Mol. Cell. Cardiol., 10.1016/j.yjmcc.2019.03.018
Liu, 2018, Gene transfer of engineered calmodulin alleviates ventricular arrhythmias in a calsequestrin-associated mouse model of catecholaminergic polymorphic ventricular tachycardia, J. Am. Heart Assoc., 7, 10.1161/JAHA.117.008155
Fielding, 2007, NMR methods for the determination of protein–ligand dissociation constants, Prog. Nucl. Magn. Reson. Spectrosc., 51, 219, 10.1016/j.pnmrs.2007.04.001
Gaertner, 2004, RC3/neurogranin and Ca2+/calmodulin-dependent protein kinase II produce opposing effects on the affinity of calmodulin for calcium, J. Biol. Chem., 279, 39374, 10.1074/jbc.M405352200
Davis, 1999, Characterizing the response of calcium signal transducers to generated calcium transients, Biochemistry, 38, 4235, 10.1021/bi982495z
Metzger, 2004, Variations in cross-bridge attachment rate and tension with phosphorylation of myosin in mammalian skinned skeletal muscle fibers. Implications for twitch potentiation in intact muscle, J. Gen. Physiol., 93, 855, 10.1085/jgp.93.5.855
Van Lierop, 2002, Activation of smooth muscle myosin light chain kinase by calmodulin. Role of LYS30 and GLY40, J. Biol. Chem., 277, 6550, 10.1074/jbc.M111404200
Sigalas, 2009, Ca(2+)-calmodulin can activate and inactivate cardiac ryanodine receptors, Br. J. Pharmacol., 156, 794, 10.1111/j.1476-5381.2008.00092.x
Maximciuc, 2006, Complex of Calmodulin with a ryanodine receptor target reveals a novel, flexible binding mode, Structure, 14, 1547, 10.1016/j.str.2006.08.011
Her, 2018, Structural dynamics of calmodulin-ryanodine receptor interactions: electron paramagnetic resonance using stereospecific spin labels, Sci. Rep., 8, 1, 10.1038/s41598-018-29064-8
Cornea, 2009, FRET-based mapping of calmodulin bound to the RyR1 Ca 2+ release channel, Proc. Natl. Acad. Sci. U. S. A., 106, 2, 10.1073/pnas.0813010106
Rebbeck, 2016, S100A1 protein does not compete with calmodulin for ryanodine receptor binding but structurally alters the ryanodine receptoro·calmodulin complex, J. Biol. Chem., 291, 15896, 10.1074/jbc.M115.713107
Cornea, 2010, Mapping the ryanodine receptor FK506-binding protein subunit using fluorescence resonance energy transfer, J. Biol. Chem., 285, 19219, 10.1074/jbc.M109.066944
Guo, 2011, FRET detection of calmodulin binding to the cardiac RyR2 calcium release channel, Biophys. J., 101, 2170, 10.1016/j.bpj.2011.09.030
Wong, 2019, The KN-93 molecule inhibits Calcium/Calmodulin-Dependent protein kinase II (CaMKII) activity by binding to Ca 2+ /CaM, J. Mol. Biol., 431, 1440, 10.1016/j.jmb.2019.02.001
Johnson, 2017, Sorting out Ca2+ regulation by calmodulin dependent kinase II (CaMKII) and calmodulin, J. Mol. Cell. Cardiol., 109, 33
Backs, 2009, The delta isoform of CaM kinase II is required for pathological cardiac hypertrophy and remodeling after pressure overload, Proc. Natl. Acad. Sci. U. S. A., 106, 2342, 10.1073/pnas.0813013106
Joiner, 2012, CaMKII determines mitochondrial stress responses in heart, Nature, 491, 269, 10.1038/nature11444
Nickel, 2019, CaMKII does not control mitochondrial Ca 2+ uptake in cardiac myocytes, J. Physiol., 0, 1
Bayley, 1996, Target recognition by calmodulin: dissecting the kinetics and affinity of interaction using short peptide sequences, Protein Sci., 5, 1215, 10.1002/pro.5560050701
Barbato, 1992, Backbone dynamics of calmodulin studied by15N relaxation using inverse detected two-dimensional NMR spectroscopy: the central Helix Is flexible, Biochemistry, 31, 5269, 10.1021/bi00138a005
James, 1995, Calmodulin-binding domains: just two faced or multi-faceted?, Trends Biochem. Sci., 20, 38, 10.1016/S0968-0004(00)88949-5
Siddiqui, 2016, Myofilament Calcium Sensitivity: Consequences of the effective concentration of troponin I, Front. Physiol., 7, 1, 10.3389/fphys.2016.00632
Van Valen, 2009, Biochemistry on a leash: the roles of tether length and geometry in signal integration proteins, Biophys. J., 96, 1275, 10.1016/j.bpj.2008.10.052
Hulme, 2010, Ligand binding assays at equilibrium: validation and interpretation, Br. J. Pharmacol., 161, 1219, 10.1111/j.1476-5381.2009.00604.x
Johnson, 2019, Calcium modulation of cardiac sodium channels, J. Physiol., 0, 1
Nof, 2019, Mutations in Na V 1. 5 reveal calcium-calmodulin regulation of sodium channel, Front. Physiol., 10, 1, 10.3389/fphys.2019.00700
Crotti, 2013, Calmodulin mutations associated with recurrent cardiac arrest in infants, Circulation, 127, 1009, 10.1161/CIRCULATIONAHA.112.001216
Van Duyne, 1993, Atomic structures of the human immunophilin FKBP-12 complexes with FK506 and rapamycin, J. Mol. Biol., 229, 105, 10.1006/jmbi.1993.1012
Kabsch, 2010, Xds, Acta Crystallogr. Sect. D Biol. Crystallogr., 66, 125, 10.1107/S0907444909047337
Afonine, 2012, Towards automated crystallographic structure refinement with phenix. refine, Acta Crystallogr. Sect. D Biol. Crystallogr., 68, 352, 10.1107/S0907444912001308
Emsley, 2010, Features and development of coot, Acta Crystallogr. Sect. D Biol. Crystallogr., 66, 486, 10.1107/S0907444910007493
Chen, 2010, MolProbity: all-atom structure validation for macromolecular crystallography, Acta Crystallogr. Sect. D Biol. Crystallogr., 66, 12, 10.1107/S0907444909042073
Knollmann, 2006, Casq2 deletion causes sarcoplasmic reticulum volume increase, premature Ca2+ release, and catecholaminergic polymorphic ventricular tachycardia, J. Clin. Invest., 116, 2510
Batiste, 2019, Unnatural verticilide enantiomer inhibits type 2 ryanodine receptor-mediated calcium leak and is antiarrhythmic, Proc. Natl. Acad. Sci., 116, 4810, 10.1073/pnas.1816685116
Fruen, 2000, Differential Ca 2+ sensitivity of skeletal and cardiac muscle ryanodine receptors in the presence of calmodulin, Am. J. Physiol. Physiol., 279, C724, 10.1152/ajpcell.2000.279.3.C724
Fruen, 2003, Regulation of the RYR1 and RYR2 Ca 2+ release channel isoforms by Ca 2+ -insensitive mutants of calmodulin, Biochemistry, 42, 2740, 10.1021/bi0267689
Stroik, 2018, Targeting protein-protein interactions for therapeutic discovery via FRET-based high-throughput screening in living cells, Sci. Rep., 8, 1, 10.1038/s41598-018-29685-z
Schaaf, 2017, High-Throughput spectral and lifetime-based FRET screening in living cells to identify small-molecule effectors of SERCA, SLAS Discov., 22, 262, 10.1177/1087057116680151
