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Volumn 46, Issue 7, 2007, Pages 1999-2009

Phospholamban inhibits Ca-ATPase conformational changes involving the E2 intermediate

Author keywords

[No Author keywords available]

Indexed keywords

CONFORMATIONAL TRANSITION; FLUORESCENCE SPECTROSCOPY; MICROSOMES; PHOSPHORYLATION;

EID: 33847028027     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi061365k     Document Type: Article
Times cited : (15)

References (54)
  • 2
    • 3943055518 scopus 로고    scopus 로고
    • Structural basis of ion pumping by Ca-ATPase of the sarcoplasmic reticulum
    • Toyoshima, C., and Inesi, G. (2004) Structural basis of ion pumping by Ca-ATPase of the sarcoplasmic reticulum, Ann. Rev. Biochem. 73, 269-292.
    • (2004) Ann. Rev. Biochem , vol.73 , pp. 269-292
    • Toyoshima, C.1    Inesi, G.2
  • 3
    • 0031722958 scopus 로고    scopus 로고
    • Phospholamban: Protein structure, mechanism of action, and role in cardiac function
    • Simmerman, H. K., and Jones, L. R. (1998) Phospholamban: Protein structure, mechanism of action, and role in cardiac function, Physiol. Rev. 78, 921-947.
    • (1998) Physiol. Rev , vol.78 , pp. 921-947
    • Simmerman, H.K.1    Jones, L.R.2
  • 4
    • 0033662769 scopus 로고    scopus 로고
    • Phospholamban and cardiac contractility
    • Frank, K., and Kranias, E. G. (2003) Phospholamban and cardiac contractility, Ann. Med. 32, 572-578.
    • (2003) Ann. Med , vol.32 , pp. 572-578
    • Frank, K.1    Kranias, E.G.2
  • 5
    • 33746108947 scopus 로고    scopus 로고
    • Coil-to-helix transition within phospholamban underlies release of Ca-ATPase inhibition in response to β-adrenergic signaling
    • Bigelow, D. J., and Squier, T. C. (2006) Coil-to-helix transition within phospholamban underlies release of Ca-ATPase inhibition in response to β-adrenergic signaling, Curr. Enzyme Inhib. 2, 19-27.
    • (2006) Curr. Enzyme Inhib , vol.2 , pp. 19-27
    • Bigelow, D.J.1    Squier, T.C.2
  • 6
    • 0036167330 scopus 로고    scopus 로고
    • Dual site phospholamban phosphorylation and its physiological relevance in the heart
    • Hagemann, D., and Xiao, R. P. (2002) Dual site phospholamban phosphorylation and its physiological relevance in the heart, Trends Cardiovasc. Med. 12, 51-56.
    • (2002) Trends Cardiovasc. Med , vol.12 , pp. 51-56
    • Hagemann, D.1    Xiao, R.P.2
  • 7
    • 0035700695 scopus 로고    scopus 로고
    • Phospholamban: A promising therapeutic target in heart failure?
    • Schmidt, A. G., Edes, I., and Kranias, E. G. (2001) Phospholamban: A promising therapeutic target in heart failure? Cardiovasc. Drugs Ther. 15, 387-396.
    • (2001) Cardiovasc. Drugs Ther , vol.15 , pp. 387-396
    • Schmidt, A.G.1    Edes, I.2    Kranias, E.G.3
  • 8
    • 0037216819 scopus 로고    scopus 로고
    • Sarcoplasmic reticulum Ca-ATPase modulates cardiac contraction and relaxation
    • Frank, K. F., Bolck, B., Erdmann, E., and Schwinger, R. H. (2003) Sarcoplasmic reticulum Ca-ATPase modulates cardiac contraction and relaxation, Cardiovasc. Res. 57, 20-27.
    • (2003) Cardiovasc. Res , vol.57 , pp. 20-27
    • Frank, K.F.1    Bolck, B.2    Erdmann, E.3    Schwinger, R.H.4
  • 9
    • 0038464639 scopus 로고    scopus 로고
    • Phospholamban: A crucial regulator of cardiac contractility
    • MacLennan, D. H., and Kranias, E. G. (2003) Phospholamban: A crucial regulator of cardiac contractility, Nat. Rev. Mol. Cell. Biol. 4, 566-577.
    • (2003) Nat. Rev. Mol. Cell. Biol , vol.4 , pp. 566-577
    • MacLennan, D.H.1    Kranias, E.G.2
  • 12
    • 19644369427 scopus 로고    scopus 로고
    • Intermolecular conformational coupling and free energy exchange enhance the catalytic efficiency of cardiac muscle SERCA2a following the relief of phospholamban inhibition
    • Mahaney, J. E., Albers, R. W., Waggoner, J. R., Kutchai, H. C., and Froehlich, J. P. (2005) Intermolecular conformational coupling and free energy exchange enhance the catalytic efficiency of cardiac muscle SERCA2a following the relief of phospholamban inhibition, Biochemistry 44, 7713-7724.
    • (2005) Biochemistry , vol.44 , pp. 7713-7724
    • Mahaney, J.E.1    Albers, R.W.2    Waggoner, J.R.3    Kutchai, H.C.4    Froehlich, J.P.5
  • 13
    • 0033594924 scopus 로고    scopus 로고
    • Rearrangement of domain elements of the Ca-ATPase in cardiac sarcoplasmic reticulum membranes upon phospholamban phosphorylation
    • Negash, S., Huang, S., and Squier, T. C. (1999) Rearrangement of domain elements of the Ca-ATPase in cardiac sarcoplasmic reticulum membranes upon phospholamban phosphorylation, Biochemistry 38, 8150-8158.
    • (1999) Biochemistry , vol.38 , pp. 8150-8158
    • Negash, S.1    Huang, S.2    Squier, T.C.3
  • 15
    • 0037154095 scopus 로고    scopus 로고
    • The inhibitory action of phospholamban involves stabilization of α-helices within the Ca-ATPase
    • Tatulian, S. A., Chen, B., Li, J., Negash, S., Middaugh, C. R., Bigelow, D. J., and Squier, T. C. (2002) The inhibitory action of phospholamban involves stabilization of α-helices within the Ca-ATPase, Biochemistry 41, 741-751.
    • (2002) Biochemistry , vol.41 , pp. 741-751
    • Tatulian, S.A.1    Chen, B.2    Li, J.3    Negash, S.4    Middaugh, C.R.5    Bigelow, D.J.6    Squier, T.C.7
  • 16
    • 3042730955 scopus 로고    scopus 로고
    • Direct detection of phospholamban and sarcoplasmic reticulum Ca-ATPase interaction in membranes using fluorescence resonance energy transfer
    • Mueller, B., Karim, C. B., Negrashov, I. V., Kutchai, H., and Thomas, D. D. (2004) Direct detection of phospholamban and sarcoplasmic reticulum Ca-ATPase interaction in membranes using fluorescence resonance energy transfer, Biochemistry 43, 8754-8765.
    • (2004) Biochemistry , vol.43 , pp. 8754-8765
    • Mueller, B.1    Karim, C.B.2    Negrashov, I.V.3    Kutchai, H.4    Thomas, D.D.5
  • 18
    • 0037008735 scopus 로고    scopus 로고
    • 2+ pump revealed by intermolecular thiol cross-linking
    • 2+ pump revealed by intermolecular thiol cross-linking, J. Biol. Chem. 277, 28319-28329.
    • (2002) J. Biol. Chem , vol.277 , pp. 28319-28329
    • Jones, L.R.1    Cornea, R.L.2    Chen, Z.3
  • 19
    • 0348111454 scopus 로고    scopus 로고
    • 2+ pump revealed with use of heterobifunctional cross-linking agents
    • 2+ pump revealed with use of heterobifunctional cross-linking agents, J. Biol. Chem. 278, 48348-48356.
    • (2003) J. Biol. Chem , vol.278 , pp. 48348-48356
    • Chen, Z.1    Stokes, D.L.2    Rice, W.J.3    Jones, L.R.4
  • 21
    • 12244255136 scopus 로고    scopus 로고
    • A structural model of the complex formed by phospholamban and the calcium pump of sarcoplasmic reticulum obtained by molecular mechanics
    • Hutter, M. C., Krebs, J., Meiler, J., Griesinger, C., Carafoli, E., and Helms, V. (2002) A structural model of the complex formed by phospholamban and the calcium pump of sarcoplasmic reticulum obtained by molecular mechanics, ChemBioChem 3, 1200-1208.
    • (2002) ChemBioChem , vol.3 , pp. 1200-1208
    • Hutter, M.C.1    Krebs, J.2    Meiler, J.3    Griesinger, C.4    Carafoli, E.5    Helms, V.6
  • 23
    • 16344378243 scopus 로고    scopus 로고
    • Mapping the interaction surface of a membrane protein: Unveiling the conformational switch of phospholamban in calcium pump regulation
    • Zamoon, J., Nitu, F., Karim, C., Thomas, D. D., and Veglia, G. (2005) Mapping the interaction surface of a membrane protein: Unveiling the conformational switch of phospholamban in calcium pump regulation, Proc. Natl. Acad. Sci. U.S.A. 102, 4747-4752.
    • (2005) Proc. Natl. Acad. Sci. U.S.A , vol.102 , pp. 4747-4752
    • Zamoon, J.1    Nitu, F.2    Karim, C.3    Thomas, D.D.4    Veglia, G.5
  • 24
    • 0041817968 scopus 로고    scopus 로고
    • Phosphorylation by cAMP-dependent protein kinase modulates the structural coupling between the transmembrane and cytosolic domains of phospholamban
    • Li, J., Bigelow, D. J., and Squier, T. C. (2003) Phosphorylation by cAMP-dependent protein kinase modulates the structural coupling between the transmembrane and cytosolic domains of phospholamban, Biochemistry 42, 10674-10682.
    • (2003) Biochemistry , vol.42 , pp. 10674-10682
    • Li, J.1    Bigelow, D.J.2    Squier, T.C.3
  • 25
    • 0347093477 scopus 로고    scopus 로고
    • Phospholamban binds in a compact and ordered conformation to the Ca-ATPase
    • Li, J., Xiong, Y., Bigelow, D. J., and Squier, T. C. (2004) Phospholamban binds in a compact and ordered conformation to the Ca-ATPase, Biochemistry 43, 455-463.
    • (2004) Biochemistry , vol.43 , pp. 455-463
    • Li, J.1    Xiong, Y.2    Bigelow, D.J.3    Squier, T.C.4
  • 26
    • 1842591777 scopus 로고    scopus 로고
    • Conformational changes within the cytosolic portion of phospholamban upon release of Ca-ATPase inhibition
    • Li, J., Bigelow, D. J., and Squier, T. C. (2004) Conformational changes within the cytosolic portion of phospholamban upon release of Ca-ATPase inhibition, Biochemistry 43, 3870-3879.
    • (2004) Biochemistry , vol.43 , pp. 3870-3879
    • Li, J.1    Bigelow, D.J.2    Squier, T.C.3
  • 27
    • 0034621834 scopus 로고    scopus 로고
    • Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 Å resolution
    • Toyoshima, C., Nakasako, M., Nomura, H., and Ogawa, H. (2000) Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 Å resolution, Nature 405, 647-655.
    • (2000) Nature , vol.405 , pp. 647-655
    • Toyoshima, C.1    Nakasako, M.2    Nomura, H.3    Ogawa, H.4
  • 28
    • 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
  • 29
    • 0033572289 scopus 로고    scopus 로고
    • Phospholamban reduces cardiac Ca-ATPase sensitivity to thapsigargin and cyclopiazonic acid
    • Mahaney, J., Barlow, A., Honaker, B., Huffman, J., and Muchnok, T. (1999) Phospholamban reduces cardiac Ca-ATPase sensitivity to thapsigargin and cyclopiazonic acid, Arch. Biochem. Biophys. 372, 408-413.
    • (1999) Arch. Biochem. Biophys , vol.372 , pp. 408-413
    • Mahaney, J.1    Barlow, A.2    Honaker, B.3    Huffman, J.4    Muchnok, T.5
  • 30
    • 1442289363 scopus 로고    scopus 로고
    • Improved expression and characterization of Ca-ATPase and phospholamban in High-Five cells
    • Waggoner, J. R., Huffman, J., Griffith, B. N., Jones, L. R., and Mahaney, J. E. (2004) Improved expression and characterization of Ca-ATPase and phospholamban in High-Five cells, Protein Expression Purif. 34, 56-67.
    • (2004) Protein Expression Purif , vol.34 , pp. 56-67
    • Waggoner, J.R.1    Huffman, J.2    Griffith, B.N.3    Jones, L.R.4    Mahaney, J.E.5
  • 31
    • 0038240082 scopus 로고    scopus 로고
    • 2+ pump oligomerization and intersubunit free energy exchange leading to activation of cardiac muscle SERCA2a
    • 2+ pump oligomerization and intersubunit free energy exchange leading to activation of cardiac muscle SERCA2a, Ann. N.Y. Acad. Sci. 986, 1-3.
    • (2003) Ann. N.Y. Acad. Sci , vol.986 , pp. 1-3
    • Mahaney, J.E.1    Albers, R.W.2    Kutchai, H.3    Froehlich, J.P.4
  • 32
    • 71849104860 scopus 로고
    • Protein measurement with the Folin phenol reagent
    • Lowry, O., Rosebrough, N., Farr, A., and Randall, R. (1951) Protein measurement with the Folin phenol reagent, J. Biol. Chem. 193, 265-275.
    • (1951) J. Biol. Chem , vol.193 , pp. 265-275
    • Lowry, O.1    Rosebrough, N.2    Farr, A.3    Randall, R.4
  • 33
    • 0018600707 scopus 로고
    • An improved assay for nanomole amounts of inorganic phosphate
    • Lanzetta, P. A., Alvarez, L. J., Reinach, P. S., and Candia, O. A. (1979) An improved assay for nanomole amounts of inorganic phosphate, Anal. Biochem. 100, 95-97.
    • (1979) Anal. Biochem , vol.100 , pp. 95-97
    • Lanzetta, P.A.1    Alvarez, L.J.2    Reinach, P.S.3    Candia, O.A.4
  • 34
    • 0030905733 scopus 로고    scopus 로고
    • 2+ pump and phospholamban in Spodoptera frugiperda (Sf21) cells reveals new insights on ATPase regulation
    • 2+ pump and phospholamban in Spodoptera frugiperda (Sf21) cells reveals new insights on ATPase regulation, J. Biol. Chem. 272, 15872-15880.
    • (1997) J. Biol. Chem , vol.272 , pp. 15872-15880
    • Autry, J.M.1    Jones, L.R.2
  • 35
    • 0020023988 scopus 로고
    • Myosin active-site trapping with vanadate ion
    • Goodno, C. C. (1982) Myosin active-site trapping with vanadate ion, Methods Enzymol. 85, 116-123.
    • (1982) Methods Enzymol , vol.85 , pp. 116-123
    • Goodno, C.C.1
  • 36
    • 0023856789 scopus 로고
    • Conformational changes in the vicinity of the N-iodoacetyl-N′-(5-sulfo-1-naphthyl)-ethylenediamine attached to the specific thiol of sarcoplasmic reticulum Ca-ATPase throughout the catalytic cycle
    • Obara, M., Suzuki, H., and Kanazawa, T. (1988) Conformational changes in the vicinity of the N-iodoacetyl-N′-(5-sulfo-1-naphthyl)-ethylenediamine attached to the specific thiol of sarcoplasmic reticulum Ca-ATPase throughout the catalytic cycle, J. Biol. Chem. 263, 3690-3697.
    • (1988) J. Biol. Chem , vol.263 , pp. 3690-3697
    • Obara, M.1    Suzuki, H.2    Kanazawa, T.3
  • 37
    • 0034090664 scopus 로고    scopus 로고
    • Kinetics studies of the cardiac Ca-ATPase expressed in Sf21 cells: New insights on Ca-ATPase regulation by phospholamban
    • Mahaney, J. E., Autry, J. M., and Jones, L. R. (2000) Kinetics studies of the cardiac Ca-ATPase expressed in Sf21 cells: New insights on Ca-ATPase regulation by phospholamban, Biophys. J. 78, 1306-1323.
    • (2000) Biophys. J , vol.78 , pp. 1306-1323
    • Mahaney, J.E.1    Autry, J.M.2    Jones, L.R.3
  • 40
    • 0028922449 scopus 로고
    • Conformational transitions of the sarcoplasmic reticulum Ca-ATPase studied by time-resolved EPR and quenched-flow kinetics
    • Mahaney, J. E., Froehlich, J. P., and Thomas, D. D. (1995) Conformational transitions of the sarcoplasmic reticulum Ca-ATPase studied by time-resolved EPR and quenched-flow kinetics, Biochemistry 34, 4864-4879.
    • (1995) Biochemistry , vol.34 , pp. 4864-4879
    • Mahaney, J.E.1    Froehlich, J.P.2    Thomas, D.D.3
  • 41
    • 0015791798 scopus 로고
    • Phosphorylation of the sarcoplasmic reticulum membrane by orthophosphate inhibition by calcium ions
    • Masuda, H., and de Meis, L. (1973) Phosphorylation of the sarcoplasmic reticulum membrane by orthophosphate inhibition by calcium ions, Biochemistry 12, 4581-4585.
    • (1973) Biochemistry , vol.12 , pp. 4581-4585
    • Masuda, H.1    de Meis, L.2
  • 42
    • 0015919696 scopus 로고
    • Occurrence and characteristics of a rapid exchange of phosphate oxygens catalyzed by sarcoplasmic reticulum vesicles
    • Kanazawa, T., and Boyer, P. D. (1973) Occurrence and characteristics of a rapid exchange of phosphate oxygens catalyzed by sarcoplasmic reticulum vesicles, J. Biol. Chem. 248, 3163-3172.
    • (1973) J. Biol. Chem , vol.248 , pp. 3163-3172
    • Kanazawa, T.1    Boyer, P.D.2
  • 43
    • 0020479078 scopus 로고
    • The interaction of vanadate ions with the Ca-ATPase from sarcoplasmic reticulum
    • Pick, U. (1982) The interaction of vanadate ions with the Ca-ATPase from sarcoplasmic reticulum, J. Biol. Chem. 257, 6111-6119.
    • (1982) J. Biol. Chem , vol.257 , pp. 6111-6119
    • Pick, U.1
  • 44
    • 0020351903 scopus 로고
    • Vanadate inhibition of the Ca-ATPase activity of sarcoplasmic reticulum vesicles
    • Barrabin, H., and de Meis, L. (1982) Vanadate inhibition of the Ca-ATPase activity of sarcoplasmic reticulum vesicles, An. Acad. Bras. Cienc. 54, 743-751.
    • (1982) An. Acad. Bras. Cienc , vol.54 , pp. 743-751
    • Barrabin, H.1    de Meis, L.2
  • 45
    • 0021289120 scopus 로고
    • i (or vanadate) sites in sarcoplasmic reticulum ATPase
    • i (or vanadate) sites in sarcoplasmic reticulum ATPase, J. Biol. Chem. 259, 996-1003.
    • (1984) J. Biol. Chem , vol.259 , pp. 996-1003
    • Inesi, G.1    Lewis, D.2    Murphy, A.J.3
  • 48
    • 0026700036 scopus 로고
    • Phosphorylation- dependent changes in the spatial relationship between Ca-ATPase polypeptide chains in sarcoplasmic reticulum membranes
    • Bigelow, D. J., Squier, T. C., and Inesi, G. (1992) Phosphorylation- dependent changes in the spatial relationship between Ca-ATPase polypeptide chains in sarcoplasmic reticulum membranes, J. Biol. Chem. 267, 6952-6962.
    • (1992) J. Biol. Chem , vol.267 , pp. 6952-6962
    • Bigelow, D.J.1    Squier, T.C.2    Inesi, G.3
  • 49
    • 0023185517 scopus 로고
    • Localization of site-specific probes on the Ca-ATPase of sarcoplasmic reticulum using fluorescence energy transfer
    • Squier, T. C., Bigelow, D. J., Garcia de Ancos, J., and Inesi, G. (1987) Localization of site-specific probes on the Ca-ATPase of sarcoplasmic reticulum using fluorescence energy transfer, J. Biol. Chem. 262, 4748-4754.
    • (1987) J. Biol. Chem , vol.262 , pp. 4748-4754
    • Squier, T.C.1    Bigelow, D.J.2    Garcia de Ancos, J.3    Inesi, G.4
  • 51
    • 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
  • 53
    • 0016658302 scopus 로고
    • Transient state kinetic studies of sarcoplasmic reticulum adenosine triphosphatase
    • Froehlich, J. P., and Taylor, E. W. (1975) Transient state kinetic studies of sarcoplasmic reticulum adenosine triphosphatase, J. Biol. Chem. 250, 2013-2021.
    • (1975) J. Biol. Chem , vol.250 , pp. 2013-2021
    • Froehlich, J.P.1    Taylor, E.W.2
  • 54
    • 33646112404 scopus 로고    scopus 로고
    • Phosphorylation-dependent conformational switch in spin-labeled 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 spin-labeled 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


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