메뉴 건너뛰기




Volumn 288, Issue 12, 2013, Pages 8456-8467

Sarco(endo)plasmic reticulum calcium ATPase (SERCA) inhibition by sarcolipin is encoded in its luminal tail

Author keywords

[No Author keywords available]

Indexed keywords

FUNCTIONAL PROPERTIES; INTEGRAL MEMBRANE PROTEINS; MODE OF BINDING; REGULATORY MECHANISM; SEQUENCE HOMOLOGY; SKELETAL MUSCLE; TISSUE-DEPENDENT MANNER; TRANSMEMBRANE REGIONS;

EID: 84875448440     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.446161     Document Type: Article
Times cited : (56)

References (61)
  • 1
    • 0026450976 scopus 로고
    • Sarcolipin, the "proteolipid" of skeletal muscle sarcoplasmic reticulum, is a unique, amphipathic, 31-residue peptide
    • Wawrzynow, A., Theibert, J. L., Murphy, C., Jona, I., Martonosi, A., and Collins, J. H. (1992) Sarcolipin, the "proteolipid" of skeletal muscle sarcoplasmic reticulum, is a unique, amphipathic, 31-residue peptide. Arch. Biochem. Biophys. 298, 620-623
    • (1992) Arch. Biochem. Biophys. , vol.298 , pp. 620-623
    • Wawrzynow, A.1    Theibert, J.L.2    Murphy, C.3    Jona, I.4    Martonosi, A.5    Collins, J.H.6
  • 3
    • 0038237303 scopus 로고    scopus 로고
    • Atrial chamber-specific expression of sarcolipin is regulated during development and hypertrophic remodeling
    • DOI 10.1074/jbc.M213132200
    • Minamisawa, S., Wang, Y., Chen, J., Ishikawa, Y., Chien, K. R., and Matsuoka, R. (2003) Atrial chamber-specific expression of sarcolipin is regulated during development and hypertrophic remodeling. J. Biol. Chem. 278, 9570-9575 (Pubitemid 36800451)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.11 , pp. 9570-9575
    • Minamisawa, S.1    Wang, Y.2    Chen, J.3    Ishikawa, Y.4    Chien, K.R.5    Matsuoka, R.6
  • 4
    • 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
  • 6
    • 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
  • 7
    • 0038031808 scopus 로고    scopus 로고
    • Sarcolipin regulates sarco(endo)plasmic reticulum Ca2-ATPase (SERCA) by binding to transmembrane helices alone or in association with phospholamban
    • Asahi, M., Sugita, Y., Kurzydlowski, K., De Leon, S., Tada, M., Toyoshima, C., and MacLennan, D. H. (2003) Sarcolipin regulates sarco(endo)plasmic reticulum Ca2-ATPase (SERCA) by binding to transmembrane helices alone or in association with phospholamban. Proc. Natl. Acad. Sci. U.S.A. 100, 5040-5045
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 5040-5045
    • Asahi, M.1    Sugita, Y.2    Kurzydlowski, K.3    De Leon, S.4    Tada, M.5    Toyoshima, C.6    MacLennan, D.H.7
  • 8
    • 0022921924 scopus 로고
    • Sequence analysis of phospholamban. Identification of phosphorylation sites and two major structural domains
    • Simmerman, H. K., Collins, J. H., Theibert, J. L., Wegener, A. D., and Jones, L. R. (1986) Sequence analysis of phospholamban. Identification of phosphorylation sites and two major structural domains. J. Biol. Chem. 261, 13333-13341 (Pubitemid 17006915)
    • (1986) Journal of Biological Chemistry , vol.261 , Issue.28 , pp. 13333-13341
    • Simmerman, H.K.B.1    Collins, J.H.2    Theibert, J.L.3
  • 10
    • 33847028027 scopus 로고    scopus 로고
    • Phospholamban inhibits Ca-ATPase conformational changes involving the E2 intermediate
    • Waggoner, J. R., Huffman, J., Froehlich, J. P., and Mahaney, J. E. (2007) Phospholamban inhibits Ca-ATPase conformational changes involving the E2 intermediate. Biochemistry 46, 1999-2009
    • (2007) Biochemistry , vol.46 , pp. 1999-2009
    • Waggoner, J.R.1    Huffman, J.2    Froehlich, J.P.3    Mahaney, J.E.4
  • 11
    • 77449089784 scopus 로고    scopus 로고
    • Ca2- binding to site i of the cardiac Ca2- pump is sufficient to dissociate phospholamban
    • Chen, Z., Akin, B. L., and Jones, L. R. (2010) Ca2- binding to site I of the cardiac Ca2- 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
  • 12
    • 0034306417 scopus 로고    scopus 로고
    • Phospholamban remains associated with the Ca2- and Mg2-dependent ATPase following phosphorylation by cAMP-dependent protein kinase
    • Negash, S., Yao, Q., Sun, H., Li, J., Bigelow, D. J., and Squier, T. C. (2000) Phospholamban remains associated with the Ca2- and Mg2-dependent ATPase following phosphorylation by cAMP-dependent protein kinase. Biochem. J. 351, 195-205
    • (2000) Biochem. J. , vol.351 , pp. 195-205
    • Negash, S.1    Yao, Q.2    Sun, H.3    Li, J.4    Bigelow, D.J.5    Squier, T.C.6
  • 13
    • 33646097119 scopus 로고    scopus 로고
    • 2+-ATPase complex
    • DOI 10.1016/j.jmb.2006.02.047, PII S0022283606002464
    • Traaseth, N. J., Thomas, D. D., and Veglia, G. (2006) Effects of Ser16 phosphorylation on the allosteric transitions of phospholamban/Ca2- ATPase complex. J. Mol. Biol. 358, 1041-1050 (Pubitemid 44382448)
    • (2006) Journal of Molecular Biology , vol.358 , Issue.4 , pp. 1041-1050
    • Traaseth, N.J.1    Thomas, D.D.2    Veglia, G.3
  • 14
    • 33646112404 scopus 로고    scopus 로고
    • Phosphorylation-dependent conformational switch in spinlabeled phospholamban bound to SERCA
    • Karim, C. B., Zhang, Z., Howard, E. C., Torgersen, K. D., and Thomas, D. D. (2006) Phosphorylation-dependent conformational switch in spinlabeled phospholamban bound to SERCA. J. Mol. Biol. 358, 1032-1040
    • (2006) J. Mol. Biol. , vol.358 , pp. 1032-1040
    • Karim, C.B.1    Zhang, Z.2    Howard, E.C.3    Torgersen, K.D.4    Thomas, D.D.5
  • 15
    • 0026567125 scopus 로고
    • Molecular mechanism of regulation of Ca2- pump ATPase by phospholamban in cardiac sarcoplasmic reticulum. Effects of synthetic phospholamban peptides on Ca2- pump ATPase
    • Sasaki, T., Inui, M., Kimura, Y., Kuzuya, T., and Tada, M. (1992) Molecular mechanism of regulation of Ca2- pump ATPase by phospholamban in cardiac sarcoplasmic reticulum. Effects of synthetic phospholamban peptides on Ca2- pump ATPase. J. Biol. Chem. 267, 1674-1679
    • (1992) J. Biol. Chem. , vol.267 , pp. 1674-1679
    • Sasaki, T.1    Inui, M.2    Kimura, Y.3    Kuzuya, T.4    Tada, M.5
  • 16
    • 0028910529 scopus 로고
    • Functional reconstitution of recombinant phospholamban with rabbit skeletal Ca2-ATPase
    • Reddy, L. G., Jones, L. R., Cala, S. E., O'Brian, J. J., Tatulian, S. A., and Stokes, D. L. (1995) Functional reconstitution of recombinant phospholamban with rabbit skeletal Ca2-ATPase. J. Biol. Chem. 270, 9390-9397
    • (1995) J. Biol. Chem. , vol.270 , pp. 9390-9397
    • Reddy, L.G.1    Jones, L.R.2    Cala, S.E.3    O'Brian, J.J.4    Tatulian, S.A.5    Stokes, D.L.6
  • 17
    • 70349756663 scopus 로고    scopus 로고
    • Threonine-5 at the N-terminus can modulate sarcolipin function in cardiac myocytes
    • Bhupathy, P., Babu, G. J., Ito, M., and Periasamy, M. (2009) Threonine-5 at the N-terminus can modulate sarcolipin function in cardiac myocytes. J. Mol. Cell. Cardiol. 47, 723-729
    • (2009) J. Mol. Cell. Cardiol. , vol.47 , pp. 723-729
    • Bhupathy, P.1    Babu, G.J.2    Ito, M.3    Periasamy, M.4
  • 19
    • 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
  • 20
    • 0037160127 scopus 로고    scopus 로고
    • Sarcolipin overexpression in rat slow twitch muscle inhibits sarcoplasmic reticulum Ca2- uptake and impairs contractile function
    • Tupling, A. R., Asahi, M., and MacLennan, D. H. (2002) Sarcolipin overexpression in rat slow twitch muscle inhibits sarcoplasmic reticulum Ca2- uptake and impairs contractile function. J. Biol. Chem. 277, 44740-44746
    • (2002) J. Biol. Chem. , vol.277 , pp. 44740-44746
    • Tupling, A.R.1    Asahi, M.2    MacLennan, D.H.3
  • 24
    • 0035903095 scopus 로고    scopus 로고
    • Sarcolipin, the shorter homologue of phospholamban, forms oligomeric structures in detergent micelles and in liposomes
    • Hellstern, S., Pegoraro, S., Karim, C. B., Lustig, A., Thomas, D. D., Moroder, L., and Engel, J. (2001) Sarcolipin, the shorter homologue of phospholamban, forms oligomeric structures in detergent micelles and in liposomes. J. Biol. Chem. 276, 30845-30852
    • (2001) J. Biol. Chem. , vol.276 , pp. 30845-30852
    • Hellstern, S.1    Pegoraro, S.2    Karim, C.B.3    Lustig, A.4    Thomas, D.D.5    Moroder, L.6    Engel, J.7
  • 25
    • 51549118890 scopus 로고    scopus 로고
    • Peptide inhibitors use two related mechanisms to alter the apparent calcium affinity of the sarcoplasmic reticulum calcium pump
    • Afara, M. R., Trieber, C. A., Ceholski, D. K., and Young, H. S. (2008) Peptide inhibitors use two related mechanisms to alter the apparent calcium affinity of the sarcoplasmic reticulum calcium pump. Biochemistry 47, 9522-9530
    • (2008) Biochemistry , vol.47 , pp. 9522-9530
    • Afara, M.R.1    Trieber, C.A.2    Ceholski, D.K.3    Young, H.S.4
  • 27
    • 14644414175 scopus 로고    scopus 로고
    • The effects of mutation on the regulatory properties of phospholamban in Co-reconstituted membranes
    • DOI 10.1021/bi047878d
    • Trieber, C. A., Douglas, J. L., Afara, M., and Young, H. S. (2005) The effects of mutation on the regulatory properties of phospholamban in co-reconstituted membranes. Biochemistry 44, 3289-3297 (Pubitemid 40321999)
    • (2005) Biochemistry , vol.44 , Issue.9 , pp. 3289-3297
    • Trieber, C.A.1    Douglas, J.L.2    Afara, M.3    Young, H.S.4
  • 28
    • 0027236766 scopus 로고
    • 2+
    • Cantilina, T., Sagara, Y., Inesi, G., and Jones, L. R. (1993) Comparative studies of cardiac and skeletal sarcoplasmic reticulum ATPases: effect of phospholamban antibody on enzyme activation. J. Biol. Chem. 268, 17018-17025 (Pubitemid 23236927)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.23 , pp. 17018-17025
    • Cantilina, T.1    Sagara, Y.2    Inesi, G.3    Jones, L.R.4
  • 29
    • 70349632866 scopus 로고    scopus 로고
    • Effects of phospholamban transmembrane mutants on the calcium affinity, maximal activity, and cooperativity of the sarcoplasmic reticulum calcium pump
    • Trieber, C. A., Afara, M., and Young, H. S. (2009) Effects of phospholamban transmembrane mutants on the calcium affinity, maximal activity, and cooperativity of the sarcoplasmic reticulum calcium pump. Biochemistry 48, 9287-9296
    • (2009) Biochemistry , vol.48 , pp. 9287-9296
    • Trieber, C.A.1    Afara, M.2    Young, H.S.3
  • 30
    • 13844267771 scopus 로고    scopus 로고
    • Rapid, high-yield expression and purification of Ca2-ATPase regulatory proteins for high-resolution structural studies
    • Douglas, J. L., Trieber, C. A., Afara, M., and Young, H. S. (2005) Rapid, high-yield expression and purification of Ca2-ATPase regulatory proteins for high-resolution structural studies. Protein Expr. Purif. 40, 118-125
    • (2005) Protein Expr. Purif. , vol.40 , pp. 118-125
    • Douglas, J.L.1    Trieber, C.A.2    Afara, M.3    Young, H.S.4
  • 31
    • 33746033781 scopus 로고    scopus 로고
    • Rational design of peptide inhibitors of the sarcoplasmic reticulum calcium pump
    • DOI 10.1021/bi0523761
    • Afara, M. R., Trieber, C. A., Glaves, J. P., and Young, H. S. (2006) Rational design of peptide inhibitors of the sarcoplasmic reticulum calcium pump. Biochemistry 45, 8617-8627 (Pubitemid 44078882)
    • (2006) Biochemistry , vol.45 , Issue.28 , pp. 8617-8627
    • Afara, M.R.1    Trieber, C.A.2    Glaves, J.P.3    Young, H.S.4
  • 32
    • 84864535546 scopus 로고    scopus 로고
    • Lethal, hereditary mutants of phospholamban elude phosphorylation by protein kinase A
    • Ceholski, D. K., Trieber, C. A., Holmes, C. F., and Young, H. S. (2012) Lethal, hereditary mutants of phospholamban elude phosphorylation by protein kinase A. J. Biol. Chem. 287, 26596-26605
    • (2012) J. Biol. Chem. , vol.287 , pp. 26596-26605
    • Ceholski, D.K.1    Trieber, C.A.2    Holmes, C.F.3    Young, H.S.4
  • 33
    • 84860863765 scopus 로고    scopus 로고
    • Hydrophobic imbalance in the cytoplasmic domain of phospholamban is a determinant for lethal dilated cardiomyopathy
    • Ceholski, D. K., Trieber, C. A., and Young, H. S. (2012) Hydrophobic imbalance in the cytoplasmic domain of phospholamban is a determinant for lethal dilated cardiomyopathy. J. Biol. Chem. 287, 16521-16529
    • (2012) J. Biol. Chem. , vol.287 , pp. 16521-16529
    • Ceholski, D.K.1    Trieber, C.A.2    Young, H.S.3
  • 34
    • 0034901813 scopus 로고    scopus 로고
    • Locating phospholamban in co-crystals with Ca2-ATPase by cryoelectron microscopy
    • Young, H. S., Jones, L. R., and Stokes, D. L. (2001) Locating phospholamban in co-crystals with Ca2-ATPase by cryoelectron microscopy. Biophys. J. 81, 884-894
    • (2001) Biophys. J. , vol.81 , pp. 884-894
    • Young, H.S.1    Jones, L.R.2    Stokes, D.L.3
  • 35
    • 33744942325 scopus 로고    scopus 로고
    • Interactions between Ca2-ATPase and the pentameric form of phospholamban in two-dimensional co-crystals
    • Stokes, D. L., Pomfret, A. J., Rice, W. J., Glaves, J. P., and Young, H. S. (2006) Interactions between Ca2-ATPase and the pentameric form of phospholamban in two-dimensional co-crystals. Biophys. J. 90, 4213-4223
    • (2006) Biophys. J. , vol.90 , pp. 4213-4223
    • Stokes, D.L.1    Pomfret, A.J.2    Rice, W.J.3    Glaves, J.P.4    Young, H.S.5
  • 36
    • 78650889008 scopus 로고    scopus 로고
    • Phosphorylation and mutation of phospholamban alter physical interactions with the sarcoplasmic reticulum calcium pump
    • Glaves, J. P., Trieber, C. A., Ceholski, D. K., Stokes, D. L., and Young, H. S. (2011) Phosphorylation and mutation of phospholamban alter physical interactions with the sarcoplasmic reticulum calcium pump. J. Mol. Biol. 405, 707-723
    • (2011) J. Mol. Biol. , vol.405 , pp. 707-723
    • Glaves, J.P.1    Trieber, C.A.2    Ceholski, D.K.3    Stokes, D.L.4    Young, H.S.5
  • 37
    • 0037027332 scopus 로고    scopus 로고
    • Comparable levels of Ca-ATPase inhibition by phospholamban in slow-twitch skeletal and cardiac sarcoplasmic reticulum
    • DOI 10.1021/bi026407t
    • Ferrington, D. A., Yao, Q., Squier, T. C., and Bigelow, D. J. (2002) Comparable levels of Ca-ATPase inhibition by phospholamban in slow-twitch skeletal and cardiac sarcoplasmic reticulum. Biochemistry 41, 13289-13296 (Pubitemid 35244719)
    • (2002) Biochemistry , vol.41 , Issue.44 , pp. 13289-13296
    • Ferrington, D.A.1    Yao, Q.2    Squier, T.C.3    Bigelow, D.J.4
  • 38
    • 0029757515 scopus 로고    scopus 로고
    • Phosphorylation of phospholamban by cAMP-dependent protein kinase enhances interactions between Ca-ATPase polypeptide chains in cardiac sarcoplasmic reticulum membranes
    • DOI 10.1021/bi960864q
    • Negash, S., Chen, L. T., Bigelow, D. J., and Squier, T. C. (1996) Phosphorylation of phospholamban by cAMP-dependent protein Kinase enhances interactions between Ca-ATPase polypeptide chains in cardiac sarcoplasmic reticulum membranes. Biochemistry 35, 11247-11259 (Pubitemid 26299297)
    • (1996) Biochemistry , vol.35 , Issue.35 , pp. 11247-11259
    • Negash, S.1    Chen, L.T.2    Bigelow, D.J.3    Squier, T.C.4
  • 39
    • 72049106635 scopus 로고    scopus 로고
    • The role of sarcolipin and ATP in the transport of phosphate ion into the sarcoplasmic reticulum
    • Becucci, L., Guidelli, R., Karim, C. B., Thomas, D. D., and Veglia, G. (2009) The role of sarcolipin and ATP in the transport of phosphate ion into the sarcoplasmic reticulum. Biophys. J. 97, 2693-2699
    • (2009) Biophys. J. , vol.97 , pp. 2693-2699
    • Becucci, L.1    Guidelli, R.2    Karim, C.B.3    Thomas, D.D.4    Veglia, G.5
  • 40
    • 0042069902 scopus 로고    scopus 로고
    • Overexpression, purification, and characterization of recombinant Ca-ATPase regulators for high-resolution solution and solid-state NMR studies
    • DOI 10.1016/S1046-5928(03)00127-X
    • Buck, B., Zamoon, J., Kirby, T. L., DeSilva, T. M., Karim, C., Thomas, D., and Veglia, G. (2003) Overexpression, purification, and characterization of recombinant Ca-ATPase regulators for high-resolution solution and solid-state NMR studies. Protein Expr. Purif. 30, 253-261 (Pubitemid 36990339)
    • (2003) Protein Expression and Purification , vol.30 , Issue.2 , pp. 253-261
    • Buck, B.1    Zamoon, J.2    Kirby, T.L.3    DeSilva, T.M.4    Karim, C.5    Thomas, D.6    Veglia, G.7
  • 41
    • 0024246121 scopus 로고
    • Kinetic and equilibrium characterization of an energy-transducing enzyme and its partial reactions
    • DOI 10.1016/0076-6879(88)57074-X
    • Inesi, G., Kurzmack, M., and Lewis, D. (1988) Kinetic and equilibrium characterization of an energy-transducing enzyme and its partial reactions. Methods Enzymol. 157, 154-190 (Pubitemid 19020272)
    • (1988) Methods in Enzymology , vol.157 , pp. 154-190
    • Inesi, G.1    Kurzmack, M.2    Lewis, D.3
  • 42
    • 0024357485 scopus 로고
    • The effects of calcium, temperature and phospholamban phosphorylation on the dynamics of the calcium-stimulated ATPase of canine cardiac sarcoplasmic reticulum
    • DOI 10.1016/0005-2736(89)90323-4
    • Fowler, C., Huggins, J. P., Hall, C., Restall, C. J., and Chapman, D. (1989) The effects of calcium, temperature, and phospholamban phosphorylation on the dynamics of the calcium-stimulated ATPase of canine cardiac sarcoplasmic reticulum. Biochim. Biophys. Acta 980, 348-356 (Pubitemid 19224666)
    • (1989) Biochimica et Biophysica Acta - Biomembranes , vol.980 , Issue.3 , pp. 348-356
    • Fowler, C.1    Huggins, J.P.2    Hall, C.3    Restall, C.J.4    Chapman, D.5
  • 43
    • 80053415325 scopus 로고    scopus 로고
    • Phospholamban binds with differential affinity to calcium pump conformers
    • Bidwell, P., Blackwell, D. J., Hou, Z., Zima, A. V., and Robia, S. L. (2011) Phospholamban binds with differential affinity to calcium pump conformers. J. Biol. Chem. 286, 35044-35050
    • (2011) J Biol Chem , vol.286 , pp. 35044-35050
    • Bidwell, P.1    Blackwell, D.J.2    Hou, Z.3    Zima, A.V.4    Robia, S.L.5
  • 44
    • 0030989981 scopus 로고    scopus 로고
    • Phospholamban inhibitory function is activated by depolymerization
    • DOI 10.1074/jbc.272.24.15061
    • Kimura, Y., Kurzydlowski, K., Tada, M., and MacLennan, D. H. (1997) Phospholamban inhibitory function is enhanced by depolymerization. J. Biol. Chem. 272, 15061-15064 (Pubitemid 27255517)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.24 , pp. 15061-15064
    • Kimura, Y.1    Kurzydlowski, K.2    Tada, M.3    MacLennan, D.H.4
  • 45
    • 0038607720 scopus 로고    scopus 로고
    • Structure and function of integral membrane protein domains resolved by peptide-amphiphiles: Application to phospholamban
    • DOI 10.1002/bip.10365
    • Lockwood, N. A., Tu, R. S., Zhang, Z., Tirrell, M. V., Thomas, D. D., and Karim, C. B. (2003) Structure and function of integral membrane protein domains resolved by peptide-amphiphiles: application to phospholamban. Biopolymers 69, 283-292 (Pubitemid 36841392)
    • (2003) Biopolymers , vol.69 , Issue.3 , pp. 283-292
    • Lockwood, N.A.1    Tu, R.S.2    Zhang, Z.3    Tirrell, M.V.4    Thomas, D.D.5    Karim, C.B.6
  • 46
    • 42049119152 scopus 로고    scopus 로고
    • Structural characterization of Ca2-ATPasebound phospholamban in lipid bilayers by solid-state nuclear magnetic resonance (NMR) spectroscopy
    • Seidel, K., Andronesi, O. C., Krebs, J., Griesinger, C., Young, H. S., Becker, S., and Baldus, M. (2008) Structural characterization of Ca2-ATPasebound phospholamban in lipid bilayers by solid-state nuclear magnetic resonance (NMR) spectroscopy. Biochemistry 47, 4369-4376
    • (2008) Biochemistry , vol.47 , pp. 4369-4376
    • Seidel, K.1    Andronesi, O.C.2    Krebs, J.3    Griesinger, C.4    Young, H.S.5    Becker, S.6    Baldus, M.7
  • 47
    • 0029934318 scopus 로고    scopus 로고
    • Purified, reconstituted cardiac Ca2-ATPase is regulated by phospholamban but not by direct phosphorylation with Ca2-/calmodulin-dependent protein kinase
    • Reddy, L. G., Jones, L. R., Pace, R. C., and Stokes, D. L. (1996) Purified, reconstituted cardiac Ca2-ATPase is regulated by phospholamban but not by direct phosphorylation with Ca2-/calmodulin-dependent protein kinase. J. Biol. Chem. 271, 14964-14970
    • (1996) J. Biol. Chem. , vol.271 , pp. 14964-14970
    • Reddy, L.G.1    Jones, L.R.2    Pace, R.C.3    Stokes, D.L.4
  • 49
    • 0033616627 scopus 로고    scopus 로고
    • Depolymerization of phospholamban in the presence of calcium pump: A fluorescence energy transfer study
    • Reddy, L. G., Jones, L. R., and Thomas, D. D. (1999) Depolymerization of phospholamban in the presence of calcium pump: a fluorescence energy transfer study. Biochemistry 38, 3954-3962
    • (1999) Biochemistry , vol.38 , pp. 3954-3962
    • Reddy, L.G.1    Jones, L.R.2    Thomas, D.D.3
  • 50
    • 0035914315 scopus 로고    scopus 로고
    • Role of cysteine residues in structural stability and function of a transmembrane helix bundle
    • Karim, C. B., Paterlini, M. G., Reddy, L. G., Hunter, G. W., Barany, G., and Thomas, D. D. (2001) Role of cysteine residues in structural stability and function of a transmembrane helix bundle. J. Biol. Chem. 276, 38814-38819
    • (2001) J. Biol. Chem. , vol.276 , pp. 38814-38819
    • Karim, C.B.1    Paterlini, M.G.2    Reddy, L.G.3    Hunter, G.W.4    Barany, G.5    Thomas, D.D.6
  • 51
    • 0037461273 scopus 로고    scopus 로고
    • Defining the molecular components of calcium transport regulation in a reconstituted membrane system
    • DOI 10.1021/bi026995a
    • Reddy, L. G., Cornea, R. L., Winters, D. L., McKenna, E., and Thomas, D. D. (2003) Defining the molecular components of calcium transport regulation in a reconstituted membrane system. Biochemistry 42, 4585-4592 (Pubitemid 36457628)
    • (2003) Biochemistry , vol.42 , Issue.15 , pp. 4585-4592
    • Reddy, L.G.1    Cornea, R.L.2    Winters, D.L.3    McKenna, E.4    Thomas, D.D.5
  • 52
    • 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
  • 53
    • 0034609576 scopus 로고    scopus 로고
    • Synthetic null-cysteine phospholamban analogue and the corresponding transmembrane domain inhibit the Ca-ATPase
    • Karim, C. B., Marquardt, C. G., Stamm, J. D., Barany, G., and Thomas, D. D. (2000) Synthetic null-cysteine phospholamban analogue and the corresponding transmembrane domain inhibit the Ca-ATPase. Biochemistry 39, 10892-10897
    • (2000) Biochemistry , vol.39 , pp. 10892-10897
    • Karim, C.B.1    Marquardt, C.G.2    Stamm, J.D.3    Barany, G.4    Thomas, D.D.5
  • 54
    • 0029664966 scopus 로고    scopus 로고
    • Phospholamban regulates the Ca2-ATPase through intramembrane interactions
    • Kimura, Y., Kurzydlowski, K., Tada, M., and MacLennan, D. H. (1996) Phospholamban regulates the Ca2-ATPase through intramembrane interactions. J. Biol. Chem. 271, 21726-21731
    • (1996) J. Biol. Chem. , vol.271 , pp. 21726-21731
    • Kimura, Y.1    Kurzydlowski, K.2    Tada, M.3    MacLennan, D.H.4
  • 56
    • 33744921916 scopus 로고    scopus 로고
    • Cross-linking of C-terminal residues of phospholamban to the Ca2- pump of cardiac sarcoplasmic reticulum to probe spatial and functional interactions within the transmembrane domain
    • Chen, Z., Akin, B. L., Stokes, D. L., and Jones, L. R. (2006) Cross-linking of C-terminal residues of phospholamban to the Ca2- pump of cardiac sarcoplasmic reticulum to probe spatial and functional interactions within the transmembrane domain. J. Biol. Chem. 281, 14163-14172
    • (2006) J. Biol. Chem. , vol.281 , pp. 14163-14172
    • Chen, Z.1    Akin, B.L.2    Stokes, D.L.3    Jones, L.R.4
  • 57
    • 77955391360 scopus 로고    scopus 로고
    • Endoplasmic reticulum protein targeting of phospholamban: A common role for an N-terminal di-arginine motif in ER retention?
    • Sharma, P., Ignatchenko, V., Grace, K., Ursprung, C., Kislinger, T., and Gramolini, A. O. (2010) Endoplasmic reticulum protein targeting of phospholamban: a common role for an N-terminal di-arginine motif in ER retention? PLoS One 5, e11496
    • (2010) PLoS One , vol.5
    • Sharma, P.1    Ignatchenko, V.2    Grace, K.3    Ursprung, C.4    Kislinger, T.5    Gramolini, A.O.6
  • 58
    • 0032486465 scopus 로고    scopus 로고
    • Phospholamban domain Ib mutations influence functional interactions with the Ca2-ATPase isoform of cardiac sarcoplasmic reticulum
    • Kimura, Y., Asahi, M., Kurzydlowski, K., Tada, M., and MacLennan, D. H. (1998) Phospholamban domain Ib mutations influence functional interactions with the Ca2-ATPase isoform of cardiac sarcoplasmic reticulum. J. Biol. Chem. 273, 14238-14241
    • (1998) J. Biol. Chem. , vol.273 , pp. 14238-14241
    • Kimura, Y.1    Asahi, M.2    Kurzydlowski, K.3    Tada, M.4    MacLennan, D.H.5
  • 59
    • 0030978470 scopus 로고    scopus 로고
    • Mutation and phosphorylation change the oligomeric structure of phospholamban in lipid bilayers
    • DOI 10.1021/bi961955q
    • Cornea, R. L., Jones, L. R., Autry, J. M., and Thomas, D. D. (1997) Mutation and phosphorylation change the oligomeric structure of phospholamban in lipid bilayers. Biochemistry 36, 2960-2967 (Pubitemid 27138580)
    • (1997) Biochemistry , vol.36 , Issue.10 , pp. 2960-2967
    • Cornea, R.L.1    Jones, L.R.2    Autry, J.M.3    Thomas, D.D.4
  • 60
    • 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.