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Volumn 288, Issue 10, 2013, Pages 6881-6889

Sarcolipin protein interaction with Sarco(endo)plasmic reticulum CA 2+ ATPase (SERCA) Is distinct from phospholamban protein,and only sarcolipin can promote uncoupling of the serca pump

Author keywords

[No Author keywords available]

Indexed keywords

HEAT PRODUCTION; KINETIC CYCLES; MUSCLE-BASED; PHOSPHOLAMBAN; PROTEIN INTERACTION;

EID: 84874846595     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.436915     Document Type: Article
Times cited : (92)

References (55)
  • 1
    • 38849115741 scopus 로고    scopus 로고
    • 2+ ATPase pump expression and its relevance to cardiac muscle physiology and pathology
    • DOI 10.1093/cvr/cvm056
    • 2+ ATPase pump expression and its relevance to cardiac muscle physiology and pathology. Cardiovasc. Res. 77, 265-273 (Pubitemid 351197644)
    • (2008) Cardiovascular Research , vol.77 , Issue.2 , pp. 265-273
    • Periasamy, M.1    Bhupathy, P.2    Babu, G.J.3
  • 3
    • 34447501977 scopus 로고    scopus 로고
    • Differential expression of sarcolipin protein during muscle development and cardiac pathophysiology
    • DOI 10.1016/j.yjmcc.2007.05.009, PII S0022282807010486
    • Babu, G. J., Bhupathy, P., Carnes, C. A., Billman, G. E., and Periasamy, M. (2007) Differential expression of sarcolipin protein during muscle development and cardiac pathophysiology. J. Mol. Cell. Cardiol. 43, 215-222 (Pubitemid 47069382)
    • (2007) Journal of Molecular and Cellular Cardiology , vol.43 , Issue.2 , pp. 215-222
    • Babu, G.J.1    Bhupathy, P.2    Carnes, C.A.3    Billman, G.E.4    Periasamy, M.5
  • 4
    • 22144491856 scopus 로고    scopus 로고
    • Sarcolipin and phospholamban mRNA and protein expression in cardiac and skeletal muscle of different species
    • DOI 10.1042/BJ20050068
    • Vangheluwe, P., Schuermans, M., Zádor, E., Waelkens, E., Raeymaekers, L., and Wuytack, F. (2005) Sarcolipin and phospholamban mRNA and protein expression in cardiac and skeletal muscle of different species. Biochem. J. 389, 151-159 (Pubitemid 40978018)
    • (2005) Biochemical Journal , vol.389 , Issue.1 , pp. 151-159
    • Vangheluwe, P.1    Schuermans, M.2    Zador, E.3    Waelkens, E.4    Raeymaekers, L.5    Wuytack, F.6
  • 5
    • 33847687200 scopus 로고    scopus 로고
    • Phospholamban and sarcolipin are maintained in the endoplasmic reticulum by retrieval from the ER-Golgi intermediate compartment
    • DOI 10.1016/j.cardiores.2007.01.006, PII S0008636307000132
    • Butler, J., Lee, A. G., Wilson, D. I., Spalluto, C., Hanley, N. A., and East, J. M. (2007) Phospholamban and sarcolipin are maintained in the endoplasmic reticulum by retrieval from the ER-Golgi intermediate compartment. Cardiovasc. Res. 74, 114-123 (Pubitemid 46366951)
    • (2007) Cardiovascular Research , vol.74 , Issue.1 , pp. 114-123
    • Butler, J.1    Lee, A.G.2    Wilson, D.I.3    Spalluto, C.4    Hanley, N.A.5    East, J.M.6
  • 8
    • 0038464639 scopus 로고    scopus 로고
    • Phospholamban: A crucial regulator of cardiac contractility
    • DOI 10.1038/nrm1151
    • MacLennan, D. H., and Kranias, E. G. (2003) Phospholamban: A crucial regulator of cardiac contractility. Nat. Rev. Mol. Cell Biol. 4, 566-577 (Pubitemid 36773408)
    • (2003) Nature Reviews Molecular Cell Biology , vol.4 , Issue.7 , pp. 566-577
    • MacLennan, D.H.1    Kranias, E.G.2
  • 10
    • 0034623718 scopus 로고    scopus 로고
    • 16) phosphorylation in phospholamban is sufficient in mediating its maximal cardiac responses to β-agonists
    • DOI 10.1074/jbc.M004079200
    • Chu, G., Lester, J. W., Young, K. B., Luo, W., Zhai, J., and Kranias, E. G. (2000) A single site (Ser16) phosphorylation in phospholamban is sufficient in mediating its maximal cardiac responses to β-agonists. J. Biol. Chem. 275, 38938-38943 (Pubitemid 32009233)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.49 , pp. 38938-38943
    • Chu, G.1    Lester, J.W.2    Young, K.B.3    Luo, W.4    Zhai, J.5    Kranias, E.G.6
  • 11
    • 0027932798 scopus 로고
    • Targeted ablation of the phospholamban gene is associated with markedly enhanced myocardial contractility and loss of β-agonist stimulation
    • Luo, W., Grupp, I. L., Harrer, J., Ponniah, S., Grupp, G., Duffy, J. J., Doetschman, T., and Kranias, E. G. (1994) Targeted ablation of the phospholamban gene is associated with markedly enhanced myocardial contractility and loss of β-agonist stimulation. Circ. Res. 75, 401-409
    • (1994) Circ. Res. , vol.75 , pp. 401-409
    • Luo, W.1    Grupp, I.L.2    Harrer, J.3    Ponniah, S.4    Grupp, G.5    Duffy, J.J.6    Doetschman, T.7    Kranias, E.G.8
  • 15
    • 33744921916 scopus 로고    scopus 로고
    • 2+ pump of cardiac sarcoplasmic reticulum to probe spatial and functional interactions within the transmembrane domain
    • DOI 10.1074/jbc.M601338200
    • 2+ pump of cardiac sarcoplasmic reticulum to probe spatial and functional interactions within the transmembrane domain. J. Biol. Chem. 281, 14163-14172 (Pubitemid 43848344)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.20 , pp. 14163-14172
    • Chen, Z.1    Akin, B.L.2    Stokes, D.L.3    Jones, L.R.4
  • 18
  • 20
    • 33646110094 scopus 로고    scopus 로고
    • Defining the intramembrane binding mechanism of sarcolipin to calcium ATPase using solution NMR spectroscopy
    • Buffy, J. J., Buck-Koehntop, B. A., Porcelli, F., Traaseth, N. J., Thomas, D. D., and Veglia, G. (2006) Defining the intramembrane binding mechanism of sarcolipin to calcium ATPase using solution NMR spectroscopy. J. Mol. Biol. 358, 420-429
    • (2006) J. Mol. Biol. , vol.358 , pp. 420-429
    • Buffy, J.J.1    Buck-Koehntop, B.A.2    Porcelli, F.3    Traaseth, N.J.4    Thomas, D.D.5    Veglia, G.6
  • 21
    • 77449089784 scopus 로고    scopus 로고
    • 2+ pump is sufficient to dissociate phospholamban
    • 2+ pump is sufficient to dissociate phospholamban. J. Biol. Chem. 285, 3253-3260
    • (2010) J. Biol. Chem. , vol.285 , pp. 3253-3260
    • Chen, Z.1    Akin, B.L.2    Jones, L.R.3
  • 26
    • 0037625894 scopus 로고    scopus 로고
    • 2+ adenosine triphosphatase by phospholamban and sarcolipin: Implication for cardiac hypertrophy and failure
    • DOI 10.1016/S1050-1738(03)00037-9, PII S1050173803000379
    • 2+ adenosine triphosphatase by phospholamban and sarcolipin: Implication for cardiac hypertrophy and failure. Trends Cardiovasc. Med. 13, 152-157 (Pubitemid 36547684)
    • (2003) Trends in Cardiovascular Medicine , vol.13 , Issue.4 , pp. 152-157
    • Asahi, M.1    Nakayama, H.2    Tada, M.3    Otsu, K.4
  • 33
    • 0345643419 scopus 로고    scopus 로고
    • 2+ ATPase enzymatic properties using mouse cardiac tissue homogenates
    • DOI 10.1006/abio.1999.4059
    • 2+ ATPase enzymatic properties using mouse cardiac tissue homogenates. Anal. Biochem. 269, 236-244 (Pubitemid 29201021)
    • (1999) Analytical Biochemistry , vol.269 , Issue.2 , pp. 236-244
    • Ji, Y.1    Loukianov, E.2    Periasamy, M.3
  • 34
    • 0028924959 scopus 로고
    • Functional consequences of alterations to amino acids at the M5S5 boundary of the Ca-ATPase of sarcoplasmic reticulum
    • Andersen, J. P. (1995) Functional consequences of alterations to amino acids at the M5S5 boundary of the Ca-ATPase of sarcoplasmic reticulum. J. Biol. Chem. 270, 908-914
    • (1995) J. Biol. Chem. , vol.270 , pp. 908-914
    • Andersen, J.P.1
  • 38
    • 0015446430 scopus 로고
    • The effect of calcium ionophores on fragmented sarcoplasmic reticulum
    • Scarpa, A., Baldassare, J., and Inesi, G. (1972) The effect of calcium ionophores on fragmented sarcoplasmic reticulum. J. Gen. Physiol. 60, 735-749
    • (1972) J. Gen. Physiol. , vol.60 , pp. 735-749
    • Scarpa, A.1    Baldassare, J.2    Inesi, G.3
  • 42
    • 0019320911 scopus 로고
    • Cooperative calcium binding and ATPase activation in sarcoplasmic reticulum vesicles
    • Inesi, G., Kurzmack, M., Coan, C., and Lewis, D. (1980) Cooperative calcium binding and ATPase activation in sarcoplasmic reticulum vesicles. J. Biol. Chem. 255, 3025-3031
    • (1980) J. Biol. Chem. , vol.255 , pp. 3025-3031
    • Inesi, G.1    Kurzmack, M.2    Coan, C.3    Lewis, D.4
  • 46
    • 3943055518 scopus 로고    scopus 로고
    • 2+-ATPase of the sarcoplasmic reticulum
    • DOI 10.1146/annurev.biochem.73.011303.073700
    • 2+-ATPase of the sarcoplasmic reticulum. Ann. Rev. Biochem. 73, 269-292 (Pubitemid 39050370)
    • (2004) Annual Review of Biochemistry , vol.73 , pp. 269-292
    • Toyoshima, C.1    Inesi, G.2
  • 47
    • 77956502772 scopus 로고    scopus 로고
    • 2+ for binding to SERCA2a by stabilizing a unique nucleotide-dependent conformational state
    • 2+ for binding to SERCA2a by stabilizing a unique nucleotide-dependent conformational state. J. Biol. Chem. 285, 28540-28552
    • (2010) J. Biol. Chem. , vol.285 , pp. 28540-28552
    • Akin, B.L.1    Chen, Z.2    Jones, L.R.3
  • 49
    • 0033583036 scopus 로고    scopus 로고
    • Coreconstitution of phospholamban mutants with the Ca-ATPase reveals dependence of inhibitory function on phospholamban structure
    • Reddy, L. G., Autry, J. M., Jones, L. R., and Thomas, D. D. (1999) Coreconstitution of phospholamban mutants with the Ca-ATPase reveals dependence of inhibitory function on phospholamban structure. J. Biol. Chem. 274, 7649-7655
    • (1999) J. Biol. Chem. , vol.274 , pp. 7649-7655
    • Reddy, L.G.1    Autry, J.M.2    Jones, L.R.3    Thomas, D.D.4
  • 51
    • 34548820966 scopus 로고    scopus 로고
    • Solid-state NMR and functional measurements indicate that the conserved tyrosine residues of sarcolipin are involved directly in the inhibition of SERCA1
    • DOI 10.1074/jbc.M611668200
    • Hughes, E., Clayton, J. C., Kitmitto, A., Esmann, M., and Middleton, D. A. (2007) Solid-state NMR and functional measurements indicate that the conserved tyrosine residues of sarcolipin are involved directly in the inhibition of SERCA1. J. Biol. Chem. 282, 26603-26613 (Pubitemid 47443793)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.36 , pp. 26603-26613
    • Hughes, E.1    Clayton, J.C.2    Kitmitto, A.3    Esmann, M.4    Middleton, D.A.5
  • 52
    • 3242888769 scopus 로고    scopus 로고
    • Crystal structure of the calcium pump with a bound ATP analogue
    • DOI 10.1038/nature02680
    • Toyoshima, C., and Mizutani, T. (2004) Crystal structure of the calcium pump with a bound ATP analogue. Nature 430, 529-535 (Pubitemid 38998620)
    • (2004) Nature , vol.430 , Issue.6999 , pp. 529-535
    • Toyoshima, C.1    Mizutani, T.2
  • 53
    • 0034621834 scopus 로고    scopus 로고
    • Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 A resolution
    • DOI 10.1038/35015017
    • Toyoshima, C., Nakasako, M., Nomura, H., and Ogawa, H. (2000) Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 Ä resolution. Nature 405, 647-655 (Pubitemid 30428644)
    • (2000) Nature , vol.405 , Issue.6787 , pp. 647-655
    • Toyoshima, C.1    Nakasako, M.2    Nomura, H.3    Ogawa, H.4
  • 54
    • 0037043709 scopus 로고    scopus 로고
    • Structural changes in the calcium pump accompanying the dissociation of calcium
    • Toyoshima, C., and Nomura, H. (2002) Structural changes in the calcium pump accompanying the dissociation of calcium. Nature 418, 605-611
    • (2002) Nature , vol.418 , pp. 605-611
    • Toyoshima, C.1    Nomura, H.2
  • 55
    • 0036667745 scopus 로고    scopus 로고
    • A calcium pump made visible
    • Lee, A. G. (2002) A calcium pump made visible. Curr. Opin. Struct. Biol. 12, 547-554
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 547-554
    • Lee, A.G.1


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