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Volumn 7, Issue 6, 2012, Pages

A two-stage model for lipid modulation of the activity of integral membrane proteins

Author keywords

[No Author keywords available]

Indexed keywords

8 ANILINO 1 NAPHTHALENESULFONIC ACID; ADENOSINE TRIPHOSPHATASE (CALCIUM); AMPHOPHILE; MEMBRANE PROTEIN; PHOSPHOLIPID;

EID: 84862577500     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0039255     Document Type: Article
Times cited : (17)

References (47)
  • 1
    • 0015514472 scopus 로고
    • The fluid mosaic model of the structure of cell membranes
    • Singer SJ, Nicolson GL, (1972) The fluid mosaic model of the structure of cell membranes. Science 175: 720-731.
    • (1972) Science , vol.175 , pp. 720-731
    • Singer, S.J.1    Nicolson, G.L.2
  • 2
    • 66249083118 scopus 로고    scopus 로고
    • Emerging roles for lipids in shaping membrane-protein function
    • Phillips R, Ursell T, Wiggins P, Sens P, (2009) Emerging roles for lipids in shaping membrane-protein function. Nature 459: 379-385.
    • (2009) Nature , vol.459 , pp. 379-385
    • Phillips, R.1    Ursell, T.2    Wiggins, P.3    Sens, P.4
  • 3
    • 80052345585 scopus 로고    scopus 로고
    • Biological membranes: the importance of molecular detail
    • Lee AG, (2011) Biological membranes: the importance of molecular detail. Trends in Biochemical Sciences 36: 493-500.
    • (2011) Trends in Biochemical Sciences , vol.36 , pp. 493-500
    • Lee, A.G.1
  • 4
    • 79751537491 scopus 로고    scopus 로고
    • Lipid-binding surfaces of membrane proteins: Evidence from evolutionary and structural analysis
    • Adamian L, Naveed H, Liang J, (2011) Lipid-binding surfaces of membrane proteins: Evidence from evolutionary and structural analysis. Biochim Biophys Acta 1808: 1092-1102.
    • (2011) Biochim Biophys Acta , vol.1808 , pp. 1092-1102
    • Adamian, L.1    Naveed, H.2    Liang, J.3
  • 5
    • 49749095639 scopus 로고    scopus 로고
    • Lipids and membrane protein structures
    • Hunte C, Richers S, (2008) Lipids and membrane protein structures. Curr Op Struct Biol 18: 406-411.
    • (2008) Curr Op Struct Biol , vol.18 , pp. 406-411
    • Hunte, C.1    Richers, S.2
  • 7
    • 55649110254 scopus 로고    scopus 로고
    • Electron spin resonance in membrane research: Protein-lipid interactions
    • Marsh D, (2008) Electron spin resonance in membrane research: Protein-lipid interactions. Methods 46: 83-96.
    • (2008) Methods , vol.46 , pp. 83-96
    • Marsh, D.1
  • 8
    • 0018814507 scopus 로고
    • The lipid-protein interface in biological membranes
    • Jost PC, Griffith OH, (1980) The lipid-protein interface in biological membranes. Ann N Y Acad Sci 348: 391-407.
    • (1980) Ann N Y Acad Sci , vol.348 , pp. 391-407
    • Jost, P.C.1    Griffith, O.H.2
  • 9
    • 7044241302 scopus 로고    scopus 로고
    • How lipids affect the activities of integral membrane proteins
    • Lee AG, (2004) How lipids affect the activities of integral membrane proteins. Biochim Biophys Acta 1666: 62-87.
    • (2004) Biochim Biophys Acta , vol.1666 , pp. 62-87
    • Lee, A.G.1
  • 10
    • 0025270741 scopus 로고
    • Peptide sequence analysis and molecular cloning reveal two calcium pump isoforms in the human erythrocyte membrane
    • Strehler EE, James P, Fischer R, Heim R, Vorherr T, et al. (1990) Peptide sequence analysis and molecular cloning reveal two calcium pump isoforms in the human erythrocyte membrane. J Biol Chem 265: 2835-2842.
    • (1990) J Biol Chem , vol.265 , pp. 2835-2842
    • Strehler, E.E.1    James, P.2    Fischer, R.3    Heim, R.4    Vorherr, T.5
  • 12
    • 0028352661 scopus 로고
    • Identification of transmembrane domains of the red cell calcium pump with a new photoactivatable phospholipidic probe
    • Castello PR, Caride AJ, González Flecha FL, Fernández HN, Rossi JP, et al. (1994) Identification of transmembrane domains of the red cell calcium pump with a new photoactivatable phospholipidic probe. Biochem Biophys Res Commun 201: 194-200.
    • (1994) Biochem Biophys Res Commun , vol.201 , pp. 194-200
    • Castello, P.R.1    Caride, A.J.2    González Flecha, F.L.3    Fernández, H.N.4    Rossi, J.P.5
  • 14
    • 0024990746 scopus 로고
    • 2++-ATPase in ghost membranes and after purification
    • 2++-ATPase in ghost membranes and after purification. Mol Cell Biochem 99: 75-81.
    • (1990) Mol Cell Biochem , vol.99 , pp. 75-81
    • Kosk-Kosicka, D.1
  • 15
    • 0028113894 scopus 로고
    • Biogenesis: plasma membrane calcium ATPase: 15 years of work on the purified enzyme
    • Carafoli E, (1994) Biogenesis: plasma membrane calcium ATPase: 15 years of work on the purified enzyme. FASEB J 8: 993-1002.
    • (1994) FASEB J , vol.8 , pp. 993-1002
    • Carafoli, E.1
  • 16
    • 0034142076 scopus 로고    scopus 로고
    • Thermal stability of the plasma membrane calcium pump. Quantitative analysis of its dependence on lipid-protein interactions
    • Levi V, Rossi JP, Echarte MM, Castello PR, González Flecha FL, (2000) Thermal stability of the plasma membrane calcium pump. Quantitative analysis of its dependence on lipid-protein interactions. J Membr Biol 173: 215-225.
    • (2000) J Membr Biol , vol.173 , pp. 215-225
    • Levi, V.1    Rossi, J.P.2    Echarte, M.M.3    Castello, P.R.4    González Flecha, F.L.5
  • 20
    • 0037591275 scopus 로고    scopus 로고
    • 2++-ATPase by ATP and acidic phospholipids
    • 2++-ATPase by ATP and acidic phospholipids. J Biol Chem 278: 22265-22271.
    • (2003) J Biol Chem , vol.278 , pp. 22265-22271
    • Filomatori, C.V.1    Rega, A.F.2
  • 21
    • 84755160699 scopus 로고    scopus 로고
    • Ice-induced partial unfolding and aggregation of an integral membrane protein
    • Garber Cohen IP, Castello PR, González Flecha FL, (2010) Ice-induced partial unfolding and aggregation of an integral membrane protein. Biochim Biophys Acta 1798: 2040-2047.
    • (2010) Biochim Biophys Acta , vol.1798 , pp. 2040-2047
    • Garber Cohen, I.P.1    Castello, P.R.2    González Flecha, F.L.3
  • 22
    • 0036219942 scopus 로고    scopus 로고
    • Structural significance of the plasma membrane calcium pump oligomerization
    • Levi V, Rossi JP, Castello PR, González Flecha FL, (2002) Structural significance of the plasma membrane calcium pump oligomerization. Biophys J 82: 437-446.
    • (2002) Biophys J , vol.82 , pp. 437-446
    • Levi, V.1    Rossi, J.P.2    Castello, P.R.3    González Flecha, F.L.4
  • 24
    • 78650191386 scopus 로고    scopus 로고
    • CD spectroscopy of peptides and proteins bound to large unilamellar vesicles
    • Ladokhin AS, Fernández-Vidal M, White SH, (2010) CD spectroscopy of peptides and proteins bound to large unilamellar vesicles. J Membr Biol 236: 247-253.
    • (2010) J Membr Biol , vol.236 , pp. 247-253
    • Ladokhin, A.S.1    Fernández-Vidal, M.2    White, S.H.3
  • 25
    • 39749200245 scopus 로고    scopus 로고
    • Thermal stability of CopA, a polytopic membrane protein from the hyperthermophile Archaeoglobus fulgidus
    • Cattoni DI, González Flecha FL, Argüello JM, (2008) Thermal stability of CopA, a polytopic membrane protein from the hyperthermophile Archaeoglobus fulgidus. Arch Biochem Biophys 471: 198-206.
    • (2008) Arch Biochem Biophys , vol.471 , pp. 198-206
    • Cattoni, D.I.1    González Flecha, F.L.2    Argüello, J.M.3
  • 26
    • 84858301114 scopus 로고    scopus 로고
    • The use of circular dichroism methods to monitor unfolding transitions in peptides, globular and membrane proteins
    • In: Rodgers DS, editors, editor
    • Roman EA, Santos J, González Flecha FL, (2012) The use of circular dichroism methods to monitor unfolding transitions in peptides, globular and membrane proteins. In: Rodgers DS, editors. pp. 217-254 editor. Circular Dichroism: Theory and Spectroscopy. New York: Nova Publishers.
    • (2012) , pp. 217-254
    • Roman, E.A.1    Santos, J.2    González Flecha, F.L.3
  • 27
    • 0032552880 scopus 로고    scopus 로고
    • The preference of tryptophan for membrane interfaces
    • Yau WM, Wimley WC, Gawrisch K, White SH, (1998) The preference of tryptophan for membrane interfaces. Biochemistry 37: 14713-14718.
    • (1998) Biochemistry , vol.37 , pp. 14713-14718
    • Yau, W.M.1    Wimley, W.C.2    Gawrisch, K.3    White, S.H.4
  • 28
    • 0034693172 scopus 로고    scopus 로고
    • Oligomerization of the plasma membrane calcium pump involves two regions with different thermal stability
    • Levi V, Rossi JPFC, Castello PR, González Flecha FL, (2000) Oligomerization of the plasma membrane calcium pump involves two regions with different thermal stability. FEBS Letters 483: 99-103.
    • (2000) FEBS Letters , vol.483 , pp. 99-103
    • Levi, V.1    Rossi, J.P.F.C.2    Castello, P.R.3    González Flecha, F.L.4
  • 29
    • 80053162595 scopus 로고    scopus 로고
    • Site-directed tryptophan fluorescence reveals two essential conformational changes in the Na+/H+ antiporter NhaA
    • Kozachkov L, Padan E, (2011) Site-directed tryptophan fluorescence reveals two essential conformational changes in the Na+/H+ antiporter NhaA. Proc Nat Acad Sci USA 108: 15769-15774.
    • (2011) Proc Nat Acad Sci USA , vol.108 , pp. 15769-15774
    • Kozachkov, L.1    Padan, E.2
  • 30
    • 70249089273 scopus 로고    scopus 로고
    • Kinetics and thermodynamics of the interaction of 1-anilino-naphthalene-8-sulfonate with proteins
    • Cattoni DI, Kaufman SB, González Flecha FL, (2009) Kinetics and thermodynamics of the interaction of 1-anilino-naphthalene-8-sulfonate with proteins. Biochim Biophys Acta 1794: 1700-1708.
    • (2009) Biochim Biophys Acta , vol.1794 , pp. 1700-1708
    • Cattoni, D.I.1    Kaufman, S.B.2    González Flecha, F.L.3
  • 31
    • 0013913906 scopus 로고
    • Cooperative effects in binding by bovine serum albumin. I. The binding of 1-anilino-8-naphthalenesulfonate. Fluorimetric titrations
    • Daniel E, Weber G, (1966) Cooperative effects in binding by bovine serum albumin. I. The binding of 1-anilino-8-naphthalenesulfonate. Fluorimetric titrations. Biochemistry 5: 1893-1900.
    • (1966) Biochemistry , vol.5 , pp. 1893-1900
    • Daniel, E.1    Weber, G.2
  • 32
    • 77349083921 scopus 로고    scopus 로고
    • Reversible unfolding of a thermophilic membrane protein in phospholipid/detergent mixed micelles
    • Roman EA, Argüello JM, González Flecha FL, (2010) Reversible unfolding of a thermophilic membrane protein in phospholipid/detergent mixed micelles. J Mol Biol 397: 550-559.
    • (2010) J Mol Biol , vol.397 , pp. 550-559
    • Roman, E.A.1    Argüello, J.M.2    González Flecha, F.L.3
  • 33
    • 45449105164 scopus 로고    scopus 로고
    • Protein modulation of lipids, and vice-versa, in membranes
    • Marsh D, (2008) Protein modulation of lipids, and vice-versa, in membranes. Biochim Biophys Acta 1778: 1545-1575.
    • (2008) Biochim Biophys Acta , vol.1778 , pp. 1545-1575
    • Marsh, D.1
  • 35
    • 0037958570 scopus 로고    scopus 로고
    • Quantitative analysis of membrane protein-amphiphile interactions using resonance energy transfer
    • Levi V, Rossi JP, Castello PR, González Flecha FL, (2003) Quantitative analysis of membrane protein-amphiphile interactions using resonance energy transfer. Anal Biochem 317: 171-179.
    • (2003) Anal Biochem , vol.317 , pp. 171-179
    • Levi, V.1    Rossi, J.P.2    Castello, P.R.3    González Flecha, F.L.4
  • 36
    • 77952093185 scopus 로고    scopus 로고
    • Quantification of protein-lipid selectivity using FRET
    • Loura LM, Prieto M, Fernandes F, (2010) Quantification of protein-lipid selectivity using FRET. Eur Biophys J 39: 565-578.
    • (2010) Eur Biophys J , vol.39 , pp. 565-578
    • Loura, L.M.1    Prieto, M.2    Fernandes, F.3
  • 37
    • 0344437689 scopus 로고
    • The application of the logistic function to experimental data
    • Reed LJ, Berkson J, (1928) The application of the logistic function to experimental data. J Phys Chem 33: 760-779.
    • (1928) J Phys Chem , vol.33 , pp. 760-779
    • Reed, L.J.1    Berkson, J.2
  • 38
    • 0033798841 scopus 로고    scopus 로고
    • Selectivity in lipid binding to the bacterial outer membrane protein OmpF
    • O'Keeffe AH, East JM, Lee AG, (2000) Selectivity in lipid binding to the bacterial outer membrane protein OmpF. Biophys J 79: 2066-2074.
    • (2000) Biophys J , vol.79 , pp. 2066-2074
    • O'Keeffe, A.H.1    East, J.M.2    Lee, A.G.3
  • 39
    • 80052765949 scopus 로고    scopus 로고
    • Tolerance to changes in membrane lipid composition as a selected trait of membrane proteins
    • Sanders CR, Mittendorf KF, (2011) Tolerance to changes in membrane lipid composition as a selected trait of membrane proteins. Biochemistry 50: 7858-7867.
    • (2011) Biochemistry , vol.50 , pp. 7858-7867
    • Sanders, C.R.1    Mittendorf, K.F.2
  • 40
    • 0023035961 scopus 로고
    • sn-1,2-Diacylglycerol kinase of Escherichia coli. Structural and kinetic analysis of the lipid cofactor dependence
    • Walsh JP, Bell RM, (1986) sn-1,2-Diacylglycerol kinase of Escherichia coli. Structural and kinetic analysis of the lipid cofactor dependence. J Biol Chem 261: 15062-15069.
    • (1986) J Biol Chem , vol.261 , pp. 15062-15069
    • Walsh, J.P.1    Bell, R.M.2
  • 42
    • 56049106110 scopus 로고    scopus 로고
    • Effects of phosphatidylethanolamine glycation on lipid-protein interactions and membrane protein thermal stability
    • Levi V, Villamil Giraldo AM, Castello PR, Rossi JP, González Flecha FL, (2008) Effects of phosphatidylethanolamine glycation on lipid-protein interactions and membrane protein thermal stability. Biochem J 416: 145-152.
    • (2008) Biochem J , vol.416 , pp. 145-152
    • Levi, V.1    Villamil Giraldo, A.M.2    Castello, P.R.3    Rossi, J.P.4    González Flecha, F.L.5
  • 43
    • 34248679167 scopus 로고    scopus 로고
    • Tricine-SDS-PAGE
    • Schägger H, (2006) Tricine-SDS-PAGE. Nat Protoc 1: 16-22.
    • (2006) Nat Protoc , vol.1 , pp. 16-22
    • Schägger, H.1
  • 44
    • 23644444909 scopus 로고    scopus 로고
    • Refractive index-based determination of detergent concentration and its application to the study of membrane proteins
    • Strop P, Brunger AT, (2005) Refractive index-based determination of detergent concentration and its application to the study of membrane proteins. Protein Sci 14: 2207-2211.
    • (2005) Protein Sci , vol.14 , pp. 2207-2211
    • Strop, P.1    Brunger, A.T.2
  • 46
    • 0027278564 scopus 로고
    • Determination of the aggregation number of detergent micelles using steady-state fluorescence quenching
    • Tummino PJ, Gafni A, (1993) Determination of the aggregation number of detergent micelles using steady-state fluorescence quenching. Biophys J 64: 1580-1587.
    • (1993) Biophys J , vol.64 , pp. 1580-1587
    • Tummino, P.J.1    Gafni, A.2


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