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Volumn 358, Issue 2, 2006, Pages 420-429

Defining the Intramembrane Binding Mechanism of Sarcolipin to Calcium ATPase Using Solution NMR Spectroscopy

Author keywords

Ca ATPase; phospholamban; sarcolipin; SERCA; solution NMR

Indexed keywords

ADENOSINE TRIPHOSPHATASE (CALCIUM); DODECYLPHOSPHORYLCHOLINE; MEMBRANE PROTEIN; SARCOLIPIN; UNCLASSIFIED DRUG;

EID: 33646110094     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2006.02.005     Document Type: Article
Times cited : (45)

References (46)
  • 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. Sarcolipin, the "proteolipid" of skeletal muscle sarcoplasmic reticulum, is a unique, amphipathic, 31-residue peptide. Arch. Biochem. Biophys. 298 (1992) 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
  • 2
    • 0031281867 scopus 로고    scopus 로고
    • Characterization of the gene encoding human sarcolipin (SLN), a proteolipid associated with SERCA1: absence of structural mutations in five patients with Brody disease
    • Odermatt A., Taschner P.E.M., Schere S.W., Beatty B., Khanna V.K., Cornblath D.R., et al. Characterization of the gene encoding human sarcolipin (SLN), a proteolipid associated with SERCA1: absence of structural mutations in five patients with Brody disease. Genomics 45 (1997) 541-553
    • (1997) Genomics , vol.45 , pp. 541-553
    • Odermatt, A.1    Taschner, P.E.M.2    Schere, S.W.3    Beatty, B.4    Khanna, V.K.5    Cornblath, D.R.6
  • 4
    • 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. Sequence analysis of phospholamban. Identification of phosphorylation sites and two major structural domains. J. Biol. Chem. 261 (1986) 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
  • 5
    • 22144491856 scopus 로고    scopus 로고
    • Sarcolipin and phospholamban mRNA and protein expression in cardiac and skeletal muscle of different species
    • Vangheluwe P., Schuermans M., Zador E., Raeymaekers L., and Wuytack F. Sarcolipin and phospholamban mRNA and protein expression in cardiac and skeletal muscle of different species. Biochem. J. 389 (2005) 151-159
    • (2005) Biochem. J. , vol.389 , pp. 151-159
    • Vangheluwe, P.1    Schuermans, M.2    Zador, E.3    Raeymaekers, L.4    Wuytack, F.5
  • 6
    • 0034656175 scopus 로고    scopus 로고
    • Corticosteroids decrease mRNA levels of SERCA pumps, whereas they increase sarcolipin mRNA in the rat diaphragm
    • Gayan-Ramirez G., Vanzeir L., Wuytack F., and Decramer M. Corticosteroids decrease mRNA levels of SERCA pumps, whereas they increase sarcolipin mRNA in the rat diaphragm. J. Physiol. 524 (2000) 387-397
    • (2000) J. Physiol. , vol.524 , pp. 387-397
    • Gayan-Ramirez, G.1    Vanzeir, L.2    Wuytack, F.3    Decramer, M.4
  • 8
    • 0038237303 scopus 로고    scopus 로고
    • Atrial chamber-specific expression of sarcolipin is regulated during development and hypertrophic remodeling
    • Minamisawa S., Wang Y., Chen J., Ishikawa Y., Chien K.R., and Matsuoka R. Atrial chamber-specific expression of sarcolipin is regulated during development and hypertrophic remodeling. J. Biol. Chem. 278 (2003) 9570-9575
    • (2003) J. Biol. Chem. , vol.278 , pp. 9570-9575
    • Minamisawa, S.1    Wang, Y.2    Chen, J.3    Ishikawa, Y.4    Chien, K.R.5    Matsuoka, R.6
  • 11
    • 0036667745 scopus 로고    scopus 로고
    • A calcium pump made visible
    • Lee A.G. A calcium pump made visible. Curr. Opin. Struct. Biol. 12 (2002) 547-554
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 547-554
    • Lee, A.G.1
  • 16
    • 0038239932 scopus 로고    scopus 로고
    • The regulation of SERCA-type pumps by phospholamban and sarcolipin
    • MacLennan D.H., Asahi M., and Tupling A.R. The regulation of SERCA-type pumps by phospholamban and sarcolipin. Ann. N.Y. Acad. Sci. 986 (2003) 472-480
    • (2003) Ann. N.Y. Acad. Sci. , vol.986 , pp. 472-480
    • MacLennan, D.H.1    Asahi, M.2    Tupling, A.R.3
  • 17
    • 0141530952 scopus 로고    scopus 로고
    • NMR solution structure and topological orientation of monomeric phospholamban in dodecylphosphocholine micelles
    • Zamoon J., Mascioni A., Thomas D.D., and Veglia G. NMR solution structure and topological orientation of monomeric phospholamban in dodecylphosphocholine micelles. Biophys. J. 85 (2003) 2589-2598
    • (2003) Biophys. J. , vol.85 , pp. 2589-2598
    • Zamoon, J.1    Mascioni, A.2    Thomas, D.D.3    Veglia, G.4
  • 18
    • 0042069902 scopus 로고    scopus 로고
    • Overexpression, purification, and characterization of recombinant Ca-ATPase regulators for high-resolution solution and solid-state NMR studies
    • Buck B., Zamoon J., Kirby T.L., DeSilva T.M., Karim C., Thomas D., and Veglia G. Overexpression, purification, and characterization of recombinant Ca-ATPase regulators for high-resolution solution and solid-state NMR studies. Protein Express. Purif. 30 (2003) 253-261
    • (2003) Protein Express. Purif. , vol.30 , 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
  • 19
    • 0037080181 scopus 로고    scopus 로고
    • Structure and orientation of sarcolipin in lipid environments
    • Mascioni A., Karim C., Thomas D.D., and Veglia G. Structure and orientation of sarcolipin in lipid environments. Biochemistry 41 (2001) 475-482
    • (2001) Biochemistry , vol.41 , pp. 475-482
    • Mascioni, A.1    Karim, C.2    Thomas, D.D.3    Veglia, G.4
  • 20
    • 16344378243 scopus 로고    scopus 로고
    • Mapping the interaction surface of a membrane protein: unveiling the conformational switch of phopholamban in calcium pump regulation
    • Zamoon J., Nitu F., Karim C., Thomas D.D., and Veglia G. Mapping the interaction surface of a membrane protein: unveiling the conformational switch of phopholamban in calcium pump regulation. Proc. Natl Acad. Sci. USA 102 (2005) 4747-4752
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 4747-4752
    • Zamoon, J.1    Nitu, F.2    Karim, C.3    Thomas, D.D.4    Veglia, G.5
  • 21
    • 0026410969 scopus 로고
    • Relationship between nuclear magnetic resonance chemical shift and protein secondary structure
    • Wishart D.S., Sykes B.D., and Richards F.M. Relationship between nuclear magnetic resonance chemical shift and protein secondary structure. J. Mol. Biol. 222 (1991) 311-333
    • (1991) J. Mol. Biol. , vol.222 , pp. 311-333
    • Wishart, D.S.1    Sykes, B.D.2    Richards, F.M.3
  • 22
    • 0026597879 scopus 로고
    • The chemical shift index: a fast and simple method for the assignment of protein secondary structure through NMR spectroscopy
    • Wishart D.S., and Sykes B.D. The chemical shift index: a fast and simple method for the assignment of protein secondary structure through NMR spectroscopy. Biochemistry 31 (1992) 1647-1651
    • (1992) Biochemistry , vol.31 , pp. 1647-1651
    • Wishart, D.S.1    Sykes, B.D.2
  • 23
    • 15544370248 scopus 로고    scopus 로고
    • Serine 16 phosphorylation induces an order-to-disorder transition in monomeric phospholamban
    • Metcalfe E.E., Traaseth N.J., and Veglia G. Serine 16 phosphorylation induces an order-to-disorder transition in monomeric phospholamban. Biochemistry 44 (2005) 4386-4396
    • (2005) Biochemistry , vol.44 , pp. 4386-4396
    • Metcalfe, E.E.1    Traaseth, N.J.2    Veglia, G.3
  • 24
    • 0036217488 scopus 로고    scopus 로고
    • Deuterium/hydrogen exchange factors measured by solution nuclear magnetic resonance spectroscopy as indicators of the structure and topology of membrane proteins
    • Veglia G., Zeri A.C., Ma C., and Opella S.J. Deuterium/hydrogen exchange factors measured by solution nuclear magnetic resonance spectroscopy as indicators of the structure and topology of membrane proteins. Biophys. J. 82 (2002) 2176-2183
    • (2002) Biophys. J. , vol.82 , pp. 2176-2183
    • Veglia, G.1    Zeri, A.C.2    Ma, C.3    Opella, S.J.4
  • 25
    • 0037134535 scopus 로고    scopus 로고
    • 2+-ATPase with tightly bound fluoride and magnesium against detergent induced denaturation
    • 2+-ATPase with tightly bound fluoride and magnesium against detergent induced denaturation. J. Biol. Chem. 277 (2002) 13615-13619
    • (2002) J. Biol. Chem. , vol.277 , pp. 13615-13619
    • Yamasaki, K.1    Daito, T.2    Suzuki, H.3
  • 29
    • 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 (1997) 15872-15880
    • (1997) J. Biol. Chem. , vol.272 , pp. 15872-15880
    • Autry, J.M.1    Jones, L.R.2
  • 33
    • 0033610476 scopus 로고    scopus 로고
    • Identification by NMR spectroscopy of residues at contact surfaces in large, slowly exchanging macromolecular complexes
    • Matsuo H., Walters K.J., Teruya K., Tanaka T., Gassner G.T., Lippard S.J., et al. Identification by NMR spectroscopy of residues at contact surfaces in large, slowly exchanging macromolecular complexes. J. Am. Chem. Soc. 121 (1999) 9903-9904
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 9903-9904
    • Matsuo, H.1    Walters, K.J.2    Teruya, K.3    Tanaka, T.4    Gassner, G.T.5    Lippard, S.J.6
  • 34
    • 33845552240 scopus 로고
    • Hydrogen bond length and proton NMR chemical shifts in proteins
    • Wagner G., Pardi A., and Wuthrich K. Hydrogen bond length and proton NMR chemical shifts in proteins. J. Am. Chem. Soc. 105 (1983) 5948-5949
    • (1983) J. Am. Chem. Soc. , vol.105 , pp. 5948-5949
    • Wagner, G.1    Pardi, A.2    Wuthrich, K.3
  • 35
    • 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., Moroders L., and Engel J. Sarcolipin, the shorter homologue of phospholamban, forms oligomeric structures in detergent micelles and in liposomes. J. Biol. Chem. 276 (2001) 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    Moroders, L.6    Engel, J.7
  • 36
    • 4143073485 scopus 로고    scopus 로고
    • 15N heteronuclear NMR spectroscopy shows four dynamic domains for phospholamban reconstituted in dodecylphosphocholine micelles
    • 15N heteronuclear NMR spectroscopy shows four dynamic domains for phospholamban reconstituted in dodecylphosphocholine micelles. Biophys. J. 87 (2004) 1-10
    • (2004) Biophys. J. , vol.87 , pp. 1-10
    • Metcalfe, E.E.1    Zamoon, J.2    Thomas, D.D.3    Veglia, G.4
  • 37
    • 15544370248 scopus 로고    scopus 로고
    • Serine 16 phosphorylation induces an order-to-disorder transition in monomeric phospholamban
    • Metcalfe E.E., Traaseth N.J., and Veglia G. Serine 16 phosphorylation induces an order-to-disorder transition in monomeric phospholamban. Biochemistry 44 (2005) 4386-4396
    • (2005) Biochemistry , vol.44 , pp. 4386-4396
    • Metcalfe, E.E.1    Traaseth, N.J.2    Veglia, G.3
  • 38
    • 23344441824 scopus 로고    scopus 로고
    • The structure of phospholamban pentamer reveals a channel-like architecture in membranes
    • Oxenoid K., and Chou J.J. The structure of phospholamban pentamer reveals a channel-like architecture in membranes. Proc. Natl Acad. Sci. USA 102 (2005) 10870-10875
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 10870-10875
    • Oxenoid, K.1    Chou, J.J.2
  • 41
    • 34249765651 scopus 로고
    • NMRView a computer program for the visualization and analysis of NMR data
    • Johnson B.A., and Blevins R.A. NMRView a computer program for the visualization and analysis of NMR data. J. Biomol. NMR 4 (1994) 603-614
    • (1994) J. Biomol. NMR , vol.4 , pp. 603-614
    • Johnson, B.A.1    Blevins, R.A.2
  • 42
    • 0024285896 scopus 로고
    • Determination of three-dimensional structures of proteins from interproton distance data by hybrid distance geometry-dynamical simulated annealing calculations
    • Nilges M.C., GM, and Gronenborn A.M. Determination of three-dimensional structures of proteins from interproton distance data by hybrid distance geometry-dynamical simulated annealing calculations. FEBS Letters 229 (1988) 317-324
    • (1988) FEBS Letters , vol.229 , pp. 317-324
    • Nilges, M.C.1    GM2    Gronenborn, A.M.3
  • 44
    • 0030339738 scopus 로고    scopus 로고
    • AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR
    • Laskowski R.A., Rullmann J.A.C., MacArthur M.W., Kaptein R., and Thornton J.M. AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR. J. Biomol. NMR 8 (1996) 477-486
    • (1996) J. Biomol. NMR , vol.8 , pp. 477-486
    • Laskowski, R.A.1    Rullmann, J.A.C.2    MacArthur, M.W.3    Kaptein, R.4    Thornton, J.M.5


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