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Volumn 290, Issue 2, 2006, Pages

Role of calmodulin methionine residues in mediating productive association with cardiac ryanodine receptors

Author keywords

Excitation contraction; Methionine sulfoxide; Oxidative stress; Ryanodine receptor Ca2+ release channel; Sarcoplasmic reticulum

Indexed keywords

CALMODULIN; GLUTAMINE; LEUCINE; METHIONINE; MUTANT PROTEIN; RYANODINE RECEPTOR;

EID: 33644860796     PISSN: 03636135     EISSN: 15221539     Source Type: Journal    
DOI: 10.1152/ajpheart.00706.2005     Document Type: Article
Times cited : (20)

References (35)
  • 2
    • 0038182558 scopus 로고    scopus 로고
    • Calmodulin oxidation and methionine to glutamine substitutions reveal methionine residues critical for functional interaction with ryanodine receptor-1
    • Balog EM, Norton LE, Bloomquist RA, Cornea RL, Black DJ, Louis CF, Thomas DD, and Fruen BR. Calmodulin oxidation and methionine to glutamine substitutions reveal methionine residues critical for functional interaction with ryanodine receptor-1. J Biol Chem 278: 15615-15621, 2003.
    • (2003) J Biol Chem , vol.278 , pp. 15615-15621
    • Balog, E.M.1    Norton, L.E.2    Bloomquist, R.A.3    Cornea, R.L.4    Black, D.J.5    Louis, C.F.6    Thomas, D.D.7    Fruen, B.R.8
  • 3
    • 0036147144 scopus 로고    scopus 로고
    • Modulation of intracellular calcium-release channels by calmodulin
    • Balshaw DM, Yamaguchi N, and Meissner G. Modulation of intracellular calcium-release channels by calmodulin. J Membr Biol 185: 1-8, 2002.
    • (2002) J Membr Biol , vol.185 , pp. 1-8
    • Balshaw, D.M.1    Yamaguchi, N.2    Meissner, G.3
  • 4
    • 0035827585 scopus 로고    scopus 로고
    • Calmodulin binding and inhibition of cardiac muscle calcium release channel (ryanodine receptor)
    • Balshaw DM, Xu L, Yanaguchi N, Pasek DA, and Meissner G. Calmodulin binding and inhibition of cardiac muscle calcium release channel (ryanodine receptor). J Biol Chem 276: 20144-20153, 2001.
    • (2001) J Biol Chem , vol.276 , pp. 20144-20153
    • Balshaw, D.M.1    Xu, L.2    Yanaguchi, N.3    Pasek, D.A.4    Meissner, G.5
  • 5
    • 12844257477 scopus 로고    scopus 로고
    • Redox modulation of cellular signaling and metabolism through reversible oxidation of methionine sensors in calcium regulatory proteins
    • Bigelow DJ and Squier TC. Redox modulation of cellular signaling and metabolism through reversible oxidation of methionine sensors in calcium regulatory proteins. Biochim Biophys Acta 1703: 121-134, 2005.
    • (2005) Biochim Biophys Acta , vol.1703 , pp. 121-134
    • Bigelow, D.J.1    Squier, T.C.2
  • 6
    • 33646432170 scopus 로고
    • Bound and determined: A computer program for making buffers of defined ion concentrations
    • Brooks SJP and Storey KB. Bound and determined: a computer program for making buffers of defined ion concentrations. Anal Biochem 223: 271-281, 1983.
    • (1983) Anal Biochem , vol.223 , pp. 271-281
    • Brooks, S.J.P.1    Storey, K.B.2
  • 7
    • 0020582583 scopus 로고
    • Biochemistry and physiological role of methionine sulfoxide residues in proteins
    • Brot N and Weissbach H. Biochemistry and physiological role of methionine sulfoxide residues in proteins. Arch Biochem Biophys 233: 271-281, 1983.
    • (1983) Arch Biochem Biophys , vol.233 , pp. 271-281
    • Brot, N.1    Weissbach, H.2
  • 8
    • 0029803672 scopus 로고    scopus 로고
    • Methionine to glutamine substitutions in the C-terminal domain of calmodulin impair the activation of three protein kinases
    • Chin D and Means AR. Methionine to glutamine substitutions in the C-terminal domain of calmodulin impair the activation of three protein kinases. J Biol Chem 271: 30465-30471, 1996.
    • (1996) J Biol Chem , vol.271 , pp. 30465-30471
    • Chin, D.1    Means, A.R.2
  • 9
    • 0034256090 scopus 로고    scopus 로고
    • Calmodulin: A prototypical calcium sensor
    • Chin D and Means AR. Calmodulin: a prototypical calcium sensor. Trends Cell Biol 10: 322-328, 2000.
    • (2000) Trends Cell Biol , vol.10 , pp. 322-328
    • Chin, D.1    Means, A.R.2
  • 10
    • 0031454412 scopus 로고    scopus 로고
    • Characterization of substrate phosphorylation and use of calmodulin mutants to address implications form the enzyme crystal structure of calmodulin-dependent protein kinase I
    • Chin D, Winkler KE, and Means AR. Characterization of substrate phosphorylation and use of calmodulin mutants to address implications form the enzyme crystal structure of calmodulin-dependent protein kinase I. J Biol Chem 272: 31235-31240, 1997.
    • (1997) J Biol Chem , vol.272 , pp. 31235-31240
    • Chin, D.1    Winkler, K.E.2    Means, A.R.3
  • 11
    • 0025301950 scopus 로고
    • Ryanodine as a probe for the functional state of the skeletal muscle sarcoplasmic reticulum calcium release channel
    • Chu A, Diaz-Munoz M, Hawkes MJ, Brush K, and Hamilton SL. Ryanodine as a probe for the functional state of the skeletal muscle sarcoplasmic reticulum calcium release channel. Mol Pharmacol 37: 735-741, 1990.
    • (1990) Mol Pharmacol , vol.37 , pp. 735-741
    • Chu, A.1    Diaz-Munoz, M.2    Hawkes, M.J.3    Brush, K.4    Hamilton, S.L.5
  • 12
    • 0023006881 scopus 로고
    • Isolation of the yeast calmodulin gene: Calmodulin is an essential protein
    • Davis TN, Urdea MS, Masiarz FR, and Thorner J. Isolation of the yeast calmodulin gene: calmodulin is an essential protein. Cell 47: 423-431, 1986.
    • (1986) Cell , vol.47 , pp. 423-431
    • Davis, T.N.1    Urdea, M.S.2    Masiarz, F.R.3    Thorner, J.4
  • 14
    • 0036788917 scopus 로고    scopus 로고
    • Ryanodine receptor calcium release channels
    • Fill M and Copello JA. Ryanodine receptor calcium release channels. Physiol Rev 82: 893-922, 2002.
    • (2002) Physiol Rev , vol.82 , pp. 893-922
    • Fill, M.1    Copello, J.A.2
  • 17
    • 0025823572 scopus 로고
    • On the role of methionine residues in the sequence-independent recognition of nonpolar protein surfaces
    • Gellman SH. On the role of methionine residues in the sequence-independent recognition of nonpolar protein surfaces. Biochemistry 30: 6633-6636, 1991.
    • (1991) Biochemistry , vol.30 , pp. 6633-6636
    • Gellman, S.H.1
  • 18
    • 0020493109 scopus 로고
    • 2+-induced hydrophobic site on calmodulin: Application for purification of calmodulin by phenyl-Sepharose affinity chromatography
    • 2+-induced hydrophobic site on calmodulin: application for purification of calmodulin by phenyl-Sepharose affinity chromatography. Biochem Biophys Res Commun 29: 830-836, 1982.
    • (1982) Biochem Biophys Res Commun , vol.29 , pp. 830-836
    • Gopalakrishna, R.1    Anderson, W.B.2
  • 24
    • 0025159272 scopus 로고
    • How calmodulin binds its targets: Sequence independent recognition of amphiphilic α-helices
    • O'Neil KT and DeGrado WF. How calmodulin binds its targets: sequence independent recognition of amphiphilic α-helices. Trends Biochem Sci 15: 59-64, 1990.
    • (1990) Trends Biochem Sci , vol.15 , pp. 59-64
    • O'Neil, K.T.1    Degrado, W.F.2
  • 25
    • 0035900010 scopus 로고    scopus 로고
    • The carboxy-terminal calcium binding sites of calmodulin control calmodulin's switch from an activator to an inhibitor of RyR1
    • Rodney GG, Krol J, Williams B, Beckingham K, and Hamilton SL. The carboxy-terminal calcium binding sites of calmodulin control calmodulin's switch from an activator to an inhibitor of RyR1. Biochemistry 40: 12430-12435, 2001.
    • (2001) Biochemistry , vol.40 , pp. 12430-12435
    • Rodney, G.G.1    Krol, J.2    Williams, B.3    Beckingham, K.4    Hamilton, S.L.5
  • 26
    • 0036199229 scopus 로고    scopus 로고
    • Calmodulin as an ion channel subunit
    • Saimi Y and Kung C. Calmodulin as an ion channel subunit. Annu Rev Physiol 64: 289-311, 2002.
    • (2002) Annu Rev Physiol , vol.64 , pp. 289-311
    • Saimi, Y.1    Kung, C.2
  • 27
    • 0026076664 scopus 로고
    • Extracting hydrophobic free energies from experimental data: Relationship to protein folding and theoretical models
    • Sharp KA, Nicholls A, Friedman R, and Honig B. Extracting hydrophobic free energies from experimental data: relationship to protein folding and theoretical models. Biochemistry 30: 9686-9697, 1991.
    • (1991) Biochemistry , vol.30 , pp. 9686-9697
    • Sharp, K.A.1    Nicholls, A.2    Friedman, R.3    Honig, B.4
  • 28
    • 0034185616 scopus 로고    scopus 로고
    • Protein oxidation and age-dependent alterations in calcium homeostasis
    • Squier TC and Bigelow DJ. Protein oxidation and age-dependent alterations in calcium homeostasis. Front Biosci 504-526, 2000.
    • (2000) Front Biosci , pp. 504-526
    • Squier, T.C.1    Bigelow, D.J.2
  • 29
    • 0023880226 scopus 로고
    • Site-specific derivatives of wheat germ calmodulin. Interactions with troponin and sarcoplasmic reticulum
    • Strasburg GM, Hogan M, Birmachu W, Thomas DD, and Louis CF. Site-specific derivatives of wheat germ calmodulin. Interactions with troponin and sarcoplasmic reticulum. J Biol Chem 263: 542-548, 1988.
    • (1988) J Biol Chem , vol.263 , pp. 542-548
    • Strasburg, G.M.1    Hogan, M.2    Birmachu, W.3    Thomas, D.D.4    Louis, C.F.5
  • 30
    • 0037318056 scopus 로고    scopus 로고
    • Novel aspects of calmodulin target recognition and activation
    • Vetter SW and Leclerc E. Novel aspects of calmodulin target recognition and activation. Eur J Biochem 270: 404-414, 2003.
    • (2003) Eur J Biochem , vol.270 , pp. 404-414
    • Vetter, S.W.1    Leclerc, E.2
  • 31
    • 0028879352 scopus 로고
    • Protein engineering and NMR studies of calmodulin
    • Vogel HJ and Zhang M. Protein engineering and NMR studies of calmodulin. Mol Cell Biochem 149/150: 3-15, 1995.
    • (1995) Mol Cell Biochem , vol.149-150 , pp. 3-15
    • Vogel, H.J.1    Zhang, M.2
  • 32
    • 3142661063 scopus 로고    scopus 로고
    • Essential role of methionine residues in calmodulin binding to Bordetella pertussis adenylate cyclase, as probed by selective oxidation and repair by peptide methionine sulfoxide reductases
    • Vougier S, Mary J, Dautin N, Vinh J, Friguer B, and Ladant D. Essential role of methionine residues in calmodulin binding to Bordetella pertussis adenylate cyclase, as probed by selective oxidation and repair by peptide methionine sulfoxide reductases. J Biol Chem 279: 30210-30218, 2004.
    • (2004) J Biol Chem , vol.279 , pp. 30210-30218
    • Vougier, S.1    Mary, J.2    Dautin, N.3    Vinh, J.4    Friguer, B.5    Ladant, D.6
  • 33
    • 0018129651 scopus 로고
    • 2+-dependent protein modulator: The role of methionine residues in the activation of cyclic nucleotide phosphodiesterase
    • 2+-dependent protein modulator: the role of methionine residues in the activation of cyclic nucleotide phosphodiesterase. Biochemistry 17: 3924-3930, 1978.
    • (1978) Biochemistry , vol.17 , pp. 3924-3930
    • Walsh, M.1    Stevens, F.C.2
  • 34
    • 0033550067 scopus 로고    scopus 로고
    • Nonessential role for methionines in the productive association between calmodulin and the plasma membrane Ca-ATPase
    • Yin D, Sun H, Weaver RF, and Squier TC. Nonessential role for methionines in the productive association between calmodulin and the plasma membrane Ca-ATPase. Biochemistry 38: 13654-13660, 1999.
    • (1999) Biochemistry , vol.38 , pp. 13654-13660
    • Yin, D.1    Sun, H.2    Weaver, R.F.3    Squier, T.C.4
  • 35
    • 0033605726 scopus 로고    scopus 로고
    • Surface exposure of methionine side chains of calmodulin in solution
    • Yuan T, Ouyang H, and Vogel HJ. Surface exposure of methionine side chains of calmodulin in solution. J Biol Chem 274: 8411-8420, 1999.
    • (1999) J Biol Chem , vol.274 , pp. 8411-8420
    • Yuan, T.1    Ouyang, H.2    Vogel, H.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.