Solid-state NMR measurements of the kinetics of the interaction between phospholamban and Ca^2 +-ATPase in lipid bilayers

References

• Bers DM. Calcium fluxes involved in control of cardiac myocyte contraction. Circ Res 2000; 87: 275–281
   PubMed Web of Science ®Google Scholar
• Stokes DL, Wagenknecht T. Calcium transport across the sarcoplasmic reticulum: Structure and function of Ca2+-ATPase and the ryanodine receptor. Eur J Biochem 2000; 267: 5274–5279
   Google Scholar
• Mascioni A, Karim C, Barany G, Thomas D, Veglia G. Structure and orientation of sarcolipin in lipid environments. Biochemistry 2002; 41: 475–482
   Google Scholar
• Lee AG. How phospholamban could affect the apparent affinity of Ca2+-ATPase for Ca2+ in kinetic experiments. FEBS Letters 2003; 551: 37–41
   Google Scholar
• Tada M, Katz AM. Phosphorylation of the sarcoplasmic-reticulum and sarcolemma. Ann Rev Physiol 1982; 44: 401–423
   PubMed Web of Science ®Google Scholar
• Asahi M, Green NM, Kurzydlowski K, Tada M, MacLennan DH. Phospholamban domain IB forms an interaction site with the loop between transmembrane helices M6 and M7 of sarco(endo)plasmic reticulum Ca2+ ATPases. Proc Natl Acad Sci USA 2001; 98: 10061–10066
   Google Scholar
• Cornea RL, Jones LR, Autry JM, Thomas DD. Mutation and phosphorylation change the oligomeric structure of phospholamban in lipid bilayers. Biochemistry 1997; 36: 2960–2967
   Google Scholar
• Li M, Reddy LG, Bennett R, Silva ND, Jones LR, Thomas DD. A fluorescence energy transfer method for analyzing protein oligomeric structure: Application to phospholamban. Biophys J 1999; 76: 2587–2599
   Google Scholar
• Karim CB, Marquardt CG, Stamm JD, Barany G, Thomas DD. Synthetic null-cysteine phospholamban analogue and the corresponding transmembrane domain inhibit the Ca-ATPase. Biochemistry 2000; 39: 10892–10897
   Google Scholar
• Autry JM, Jones LR. Functional co-expression of the canine cardiac Ca2+ pump and phospholamban in Spodoptera frugiperda (Sf21) cells reveals new insights on ATPase regulation. J Biol Chem 1997; 272: 15872–15880
   PubMedGoogle Scholar
• Kimura Y, Kurzydlowski K, Tada M, MacLennan DH. Phospholamban inhibitory function is activated by depolymerization. J Biol Chem 1997; 272: 15061–15064
   PubMedGoogle Scholar
• Reddy LG, Autry JM, Jones LR, Thomas DD. Co-reconstitution of phospholamban mutants with the Ca-ATPase reveals dependence of inhibitory function on phospholamban structure. J Biol Chem 1999; 274: 7649–7655
   Google Scholar
• Chen Z, Stokes DL, Rice WJ, Jones LR. Spatial and dynamic interactions between phospholamban and the canine cardiac Ca2+ pump revealed with use of heterobifunctional cross-linking agents. J Biol Chem 2003; 278: 48348–48356
   Google Scholar
• James P, Inui M, Tada M, Chiesi M, Carafoli E. Nature and site of phospholamban regulation of the Ca-2+ pump of sarcoplasmic-reticulum. Nature 1989; 342: 90–92
   PubMed Web of Science ®Google Scholar
• Jones LR, Cornea RL, Chen ZH. Close proximity between residue 30 of phospholamban and cysteine 318 of the cardiac Ca2+ pump revealed by intermolecular thiol cross-linking. J Biol Chem 2002; 277: 28319–28329
   Google Scholar
• Asahi M, McKenna E, Kurzydlowski K, Tada M, MacLennan DH. Physical interactions between phospholamban and sarco(endo)plasmic reticulum Ca2 + -ATPases are dissociated by elevated Ca2+, but not by phospholamban phosphorylation, vanadate, or thapsigargin, and are enhanced by ATP. J Biol Chem 2000; 275: 15034–15038
   PubMed Web of Science ®Google Scholar
• Negash S, Yao Q, Sun HY, Li JH, Bigelow DJ, Squier TC. Phospholamban remains associated with the Ca2+- and Mg2+-dependent ATPase following phosphorylation by cAMP-dependent protein kinase. Biochem J 2000; 351: 195–205
   Google Scholar
• Zhai J, Schmidt AG, Hoit BD, Kimura Y, MacLennan DH, Kranias EG. Cardiac-specific overexpression of a superinhibitory pentameric phospholamban mutant enhances inhibition of cardiac function in vivo. J Biol Chem 2000; 275: 10538–10544
   PubMedGoogle Scholar
• Li JH, Bigelow DJ, Squier TC. Conformational changes within the cytosolic portion of phospholamban upon release of Ca-ATPase inhibition. Biochemistry 2004; 43: 3870–3879
   Google Scholar
• Mueller B, Karim CB, Negrashov IV, Kutchai H, Thomas DD. Direct detection of phospholamban and sarcoplasmic reticulum Ca-ATPase interaction in membranes using fluorescence resonance energy transfers. Biochemistry 2004; 43: 8754–8765
   Google Scholar
• Li JH, Xiong YJ, Bigelow DJ, Squier TC. Phospholamban binds in a compact and ordered conformation to the Ca-ATPase. Biochemistry 2004; 43: 455–463
   Google Scholar
• East JM, Lee AG. Lipid selectivity of the Ca2+ and Mg2+ ion dependent adenosinetriphosphate studied with fluorescence quenching by a bromine phospholipid. Biochemistry 1982; 21: 4144–4151
   PubMed Web of Science ®Google Scholar
• Dalton KA, Pilot JD, Mall S, East JM, Lee AG. Anionic phospholipids decrease the rate of slippage on the Ca2 + -ATPase of sarcoplasmic reticulum. Biochem J 1999; 342: 431–438
   Google Scholar
• Reddy LG, Jones LR, Thomas DD. Depolymerization of phospholamban in the presence of calcium pump: A fluorescence energy transfer study. Biochemistry 1999; 38: 3954–3962
   Google Scholar
• Waterborg JH, Matthews HR. The Lowry method for protein quantitation. The protein protocols handbook, JM Walker. Humana press, New Jersey 1996; 7–9
   Google Scholar
• Tatulian SA, Chen B, Li J, Negash S, Middaugh CR, Bigelow DJ, Squier TC. The inhibitory action of phospholamban involves stabilization of a-helices within the Ca-ATPase. Biochemistry 2002; 41: 741–751
   Google Scholar
• Hong M, Gross JD, Griffin RG. Site-resolved determination of peptide torsion angle phi from the relative orientations of backbone N-H and C-H bonds by solid-state NMR. J Phys Chem B 1997; 101: 5869–5874
   Web of Science ®Google Scholar
• Bennett AE, Rienstra CM, Auger M, Lakshmi KV, Griffin RG. Heteronuclear decoupling in rotating solids. J Chem Phys 1995; 103: 6951–6958
   Web of Science ®Google Scholar
• Toyofuku T, Kurzydlowski K, Tada M, Maclennan DH. Amino-acids Glu(2) to Ile(18) in the cytoplasmic domain of phospholamban are essential for functional association with the Ca2+-ATPase of sarcoplasmic-reticulum. J Biol Chem 1994; 269: 3088–3094
   PubMed Web of Science ®Google Scholar
• Reddy LG, Jones LR, Cala SE, Obrian JJ, Tatulian SA, Stokes DL. Functional reconstitution of recombinant phospholamban with rabbit skeletal Ca2 + -Atpase. J Biol Chem 1995; 270: 9390–9397
   PubMedGoogle Scholar
• Hughes, E (2005) , Clayton, J, Middleton, DA. In press. Probing the oligomeric state of phospholamban variants in phospholipid bilayers from solid-state NMR measurements of rotational diffusion rates. Biochemistry. ;44:4055–4066.
   Google Scholar
• Ahmed Z, Reid DG, Watts A, Middleton DA. A solid-state NMR study of the phospholamban transmembrane domain: Local structure and interactions with Ca2 + -ATPase. Biochim Biophys Acta 2000; 1468: 187–198
   Google Scholar
• Karim CB, Kirby TL, Zhang Z, Nesmelov Y, Thomas DD. Phospholamban structural dynamics in lipid bilayers probed by a spin label rigidly coupled to the peptide backbone. PNAS 2004; 101: 14437–14442
   PubMed Web of Science ®Google Scholar
• Huster D, Xiao L, Hong M. Solid-state NMR investigation of the dynamics of the soluble and membrane-bound colicin Ia channel-forming domain. Biochemistry 2001; 40: 7662–7674
   Google Scholar
• Patching SG, Brough AR, Herbert RB, Rajakarier JA, Henderson PJF, Middleton DA. Substrate affinities for membrane transport proteins determined by C-13 cross-polarization magic-angle spinning nuclear magnetic resonance spectroscopy. J Am Chem Soc 2004; 126: 3072–3080
   PubMed Web of Science ®Google Scholar
• Metcalfe EE, Traaseth NJ, Veglia G. Serine 16 phosphorylation induces an order-to-disorder transition in monomeric phospholamban. Biochemistry 2005; 44: 4386–4396
   Google Scholar
• Asahi M, Kimura Y, Kurzydlowski K, Tada M, MacLennan DH. Transmembrane helix M6 in sarco(endo)plasmic reticulum Ca2 + -ATPase forms a functional interaction site with phospholamban. Evidence for physical interactions at other sites. J Biol Chem 1999; 274: 32855–32862
   PubMedGoogle Scholar
• Toyoshima C, Asahi M, Sugita Y, Khanna R, Tsuda T, MacLennan DH. Inaugural article: Modeling of the inhibitory interaction of phospholamban with the Ca2+ ATPase. Proc Natl Acad Sci USA 2003; 100: 467–472
   PubMed Web of Science ®Google Scholar
• Schmidt A, Edes I, Kranias EG. Phospholamban: A promising therapeutic target in heart failure?. Cardiovasc Drugs Ther 2001; 15: 387–396
   Google Scholar