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Volumn 420, Issue 2, 2012, Pages 236-240

Phospholamban mutants compete with wild type for SERCA binding in living cells

Author keywords

Competition; FRET; HEK; PLB; SERCA

Indexed keywords

CYAN FLUORESCENT PROTEIN; FORSKOLIN; PHOSPHOLAMBAN; SARCOPLASMIC RETICULUM CALCIUM TRANSPORTING ADENOSINE TRIPHOSPHATASE; YELLOW FLUORESCENT PROTEIN;

EID: 84863419025     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2012.02.125     Document Type: Article
Times cited : (22)

References (26)
  • 1
    • 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., Jones L.R. Sequence analysis of phospholamban. Identification of phosphorylation sites and two major structural domains. J. Biol. Chem. 1986, 261:13333-13341.
    • (1986) J. Biol. Chem. , vol.261 , pp. 13333-13341
    • Simmerman, H.K.1    Collins, J.H.2    Theibert, J.L.3    Wegener, A.D.4    Jones, L.R.5
  • 2
    • 0038464639 scopus 로고    scopus 로고
    • Phospholamban: a crucial regulator of cardiac contractility
    • MacLennan D.H., Kranias E.G. Phospholamban: a crucial regulator of cardiac contractility. Nat. Rev. Mol. Cell. Biol. 2003, 4:566-577.
    • (2003) Nat. Rev. Mol. Cell. Biol. , vol.4 , pp. 566-577
    • MacLennan, D.H.1    Kranias, E.G.2
  • 5
    • 80051501873 scopus 로고    scopus 로고
    • Cardiac inotropes: current agents and future directions
    • Hasenfuss G., Teerlink J.R. Cardiac inotropes: current agents and future directions. Eur. Heart J. 2011, 32:1838-1845.
    • (2011) Eur. Heart J. , vol.32 , pp. 1838-1845
    • Hasenfuss, G.1    Teerlink, J.R.2
  • 7
    • 67650710788 scopus 로고    scopus 로고
    • Role of protein phosphatase-1 inhibitor-1 in cardiac physiology and pathophysiology
    • Nicolaou P., Hajjar R.J., Kranias E.G. Role of protein phosphatase-1 inhibitor-1 in cardiac physiology and pathophysiology. J. Mol. Cell. Cardiol. 2009, 47:365-371.
    • (2009) J. Mol. Cell. Cardiol. , vol.47 , pp. 365-371
    • Nicolaou, P.1    Hajjar, R.J.2    Kranias, E.G.3
  • 9
    • 77449089784 scopus 로고    scopus 로고
    • 2+ pump is sufficient to dissociate phospholamban
    • 2+ pump is sufficient to dissociate phospholamban. J. Biol. Chem. 2010, 285:3253-3260.
    • (2010) J. Biol. Chem. , vol.285 , pp. 3253-3260
    • Chen, Z.1    Akin, B.L.2    Jones, L.R.3
  • 11
    • 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., Thomas D.D. Direct detection of phospholamban and sarcoplasmic reticulum Ca-ATPase interaction in membranes using fluorescence resonance energy transfer. Biochemistry 2004, 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
  • 12
    • 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., Thomas D.D. Phosphorylation-dependent conformational switch in spin-labeled phospholamban bound to SERCA. J. Mol. Biol. 2006, 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
  • 13
    • 80053415325 scopus 로고    scopus 로고
    • Phospholamban binds with differential affinity to calcium pump conformers
    • Bidwell P., Blackwell D.J., Hou Z., Zima A.V., Robia S.L. Phospholamban binds with differential affinity to calcium pump conformers. J. Biol. Chem. 2011, 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
  • 14
    • 79955756677 scopus 로고    scopus 로고
    • Functional and physical competition between phospholamban and its mutants provides insight into the molecular mechanism of gene therapy for heart failure
    • Lockamy E.L., Cornea R.L., Karim C.B., Thomas D.D. Functional and physical competition between phospholamban and its mutants provides insight into the molecular mechanism of gene therapy for heart failure. Biochem. Biophys. Res. Commun. 2011, 408:388-392.
    • (2011) Biochem. Biophys. Res. Commun. , vol.408 , pp. 388-392
    • Lockamy, E.L.1    Cornea, R.L.2    Karim, C.B.3    Thomas, D.D.4
  • 16
    • 0024573346 scopus 로고
    • Conformational transitions in the calcium adenosinetriphosphatase studied by time-resolved fluorescence resonance energy transfer
    • Birmachu W., Nisswandt F.L., Thomas D.D. Conformational transitions in the calcium adenosinetriphosphatase studied by time-resolved fluorescence resonance energy transfer. Biochemistry 1989, 28:3940-3947.
    • (1989) Biochemistry , vol.28 , pp. 3940-3947
    • Birmachu, W.1    Nisswandt, F.L.2    Thomas, D.D.3
  • 17
    • 67649219711 scopus 로고    scopus 로고
    • Insulin-dependent rescue from cardiogenic shock is not mediated by phospholamban phosphorylation
    • Ablorh N.A., Nitu F., Engebretsen K., Thomas D.D., Holger J.S. Insulin-dependent rescue from cardiogenic shock is not mediated by phospholamban phosphorylation. Clin. Toxicol. (Phila) 2009, 47:296-302.
    • (2009) Clin. Toxicol. (Phila) , vol.47 , pp. 296-302
    • Ablorh, N.A.1    Nitu, F.2    Engebretsen, K.3    Thomas, D.D.4    Holger, J.S.5
  • 20
    • 45549099461 scopus 로고    scopus 로고
    • Phospholamban oligomerization, quaternary structure, and sarco(endo)plasmic reticulum calcium ATPase binding measured by fluorescence resonance energy transfer in living cells
    • Kelly E.M., Hou Z., Bossuyt J., Bers D.M., Robia S.L. Phospholamban oligomerization, quaternary structure, and sarco(endo)plasmic reticulum calcium ATPase binding measured by fluorescence resonance energy transfer in living cells. J. Biol. Chem. 2008, 283:12202-12211.
    • (2008) J. Biol. Chem. , vol.283 , pp. 12202-12211
    • Kelly, E.M.1    Hou, Z.2    Bossuyt, J.3    Bers, D.M.4    Robia, S.L.5
  • 22
    • 36348985507 scopus 로고    scopus 로고
    • Forster transfer recovery reveals that phospholamban exchanges slowly from pentamers but rapidly from the SERCA regulatory complex
    • Robia S.L., Campbell K.S., Kelly E.M., Hou Z., Winters D.L., Thomas D.D. Forster transfer recovery reveals that phospholamban exchanges slowly from pentamers but rapidly from the SERCA regulatory complex. Circ. Res. 2007, 101:1123-1129.
    • (2007) Circ. Res. , vol.101 , pp. 1123-1129
    • Robia, S.L.1    Campbell, K.S.2    Kelly, E.M.3    Hou, Z.4    Winters, D.L.5    Thomas, D.D.6
  • 23
    • 41949099075 scopus 로고    scopus 로고
    • Interdomain fluorescence resonance energy transfer in SERCA probed by cyan-fluorescent protein fused to the actuator domain
    • Winters D.L., Autry J.M., Svensson B., Thomas D.D. Interdomain fluorescence resonance energy transfer in SERCA probed by cyan-fluorescent protein fused to the actuator domain. Biochemistry 2008, 47:4246-4256.
    • (2008) Biochemistry , vol.47 , pp. 4246-4256
    • Winters, D.L.1    Autry, J.M.2    Svensson, B.3    Thomas, D.D.4
  • 24
    • 0037265584 scopus 로고    scopus 로고
    • Cardiac gene therapy: pumping the heart
    • Crystal R.G. Cardiac gene therapy: pumping the heart. Gene Therapy 2003, 10:2-3.
    • (2003) Gene Therapy , vol.10 , pp. 2-3
    • Crystal, R.G.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.