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Volumn 130, Issue 1-2, 2010, Pages 2-12

Rafts and the battleships of defense: The multifaceted microdomains for positive and negative signals in immune cells

Author keywords

Cellular immunity; Co receptors; Cytokine receptors; Downstream signaling; Humoral immunity; Immune receptors; Inflammation; Lipid rafts; Membrane microdomains; Phagocytosis; Raft targeting therapies

Indexed keywords

CD16 ANTIGEN; CD28 ANTIGEN; CD45 ANTIGEN; CD64 ANTIGEN; FAS ANTIGEN; FC RECEPTOR IIA; INTERLEUKIN 15; INTERLEUKIN 2; LAT PROTEIN; LIPOPOLYSACCHARIDE; LIPOTEICHOIC ACID; PROTEIN KINASE LCK; PROTEIN KINASE LYN; RAC1 PROTEIN;

EID: 77950946913     PISSN: 01652478     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.imlet.2009.12.016     Document Type: Review
Times cited : (13)

References (185)
  • 1
    • 0015514472 scopus 로고
    • The fluid mosaic model of the structure of cell membranes
    • Singer S.J., Nicolson G.L. The fluid mosaic model of the structure of cell membranes. Science 1972, 175:720-731.
    • (1972) Science , vol.175 , pp. 720-731
    • Singer, S.J.1    Nicolson, G.L.2
  • 2
    • 0030949124 scopus 로고    scopus 로고
    • Functional rafts in cell membranes
    • Simons K., Ikonen E. Functional rafts in cell membranes. Nature 1997, 387:569-572.
    • (1997) Nature , vol.387 , pp. 569-572
    • Simons, K.1    Ikonen, E.2
  • 3
    • 0034304851 scopus 로고    scopus 로고
    • Lipid rafts and signal transduction
    • Simons K., Toomre D. Lipid rafts and signal transduction. Nat Rev Mol Cell Biol 2000, 1:31-39.
    • (2000) Nat Rev Mol Cell Biol , vol.1 , pp. 31-39
    • Simons, K.1    Toomre, D.2
  • 4
    • 0031965054 scopus 로고    scopus 로고
    • Sphingolipid organization in biomembranes: what physical studies of model membranes reveal
    • Brown R.E. Sphingolipid organization in biomembranes: what physical studies of model membranes reveal. J Cell Sci 1998, 111(Pt 1):1-9.
    • (1998) J Cell Sci , vol.111 , Issue.PART 1 , pp. 1-9
    • Brown, R.E.1
  • 5
    • 0026512314 scopus 로고
    • Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface
    • Brown D.A., Rose J.K. Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface. Cell 1992, 68:533-544.
    • (1992) Cell , vol.68 , pp. 533-544
    • Brown, D.A.1    Rose, J.K.2
  • 6
    • 0028151351 scopus 로고
    • Interactions between saturated acyl chains confer detergent resistance on lipids and glycosylphosphatidylinositol (GPI)-anchored proteins: GPI-anchored proteins in liposomes and cells show similar behavior
    • Schroeder R., London E., Brown D.A. Interactions between saturated acyl chains confer detergent resistance on lipids and glycosylphosphatidylinositol (GPI)-anchored proteins: GPI-anchored proteins in liposomes and cells show similar behavior. Proc Natl Acad Sci USA 1994, 91:12130-12134.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 12130-12134
    • Schroeder, R.1    London, E.2    Brown, D.A.3
  • 7
    • 0032527642 scopus 로고    scopus 로고
    • Structure and origin of ordered lipid domains in biological membranes
    • Brown D.A., London E. Structure and origin of ordered lipid domains in biological membranes. J Membr Biol 1998, 164:103-114.
    • (1998) J Membr Biol , vol.164 , pp. 103-114
    • Brown, D.A.1    London, E.2
  • 9
    • 0028325756 scopus 로고
    • Truncation mutants define and locate cytoplasmic barriers to lateral mobility of membrane glycoproteins
    • Edidin M., Zuniga M.C., Sheetz M.P. Truncation mutants define and locate cytoplasmic barriers to lateral mobility of membrane glycoproteins. Proc Natl Acad Sci USA 1994, 91:3378-3382.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 3378-3382
    • Edidin, M.1    Zuniga, M.C.2    Sheetz, M.P.3
  • 10
    • 12944328730 scopus 로고    scopus 로고
    • Cholesterol-dependent clustering of IL-2Rα and its colocalization with HLA and CD48 on T lymphoma cells suggest their functional association with lipid rafts
    • Vereb G., Matkó J., Vámosi G., Ibrahim S.M., Magyar E., Varga S., et al. Cholesterol-dependent clustering of IL-2Rα and its colocalization with HLA and CD48 on T lymphoma cells suggest their functional association with lipid rafts. Proc Natl Acad Sci USA 2000, 97:6013-6018.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 6013-6018
    • Vereb, G.1    Matkó, J.2    Vámosi, G.3    Ibrahim, S.M.4    Magyar, E.5    Varga, S.6
  • 11
    • 0035195023 scopus 로고    scopus 로고
    • Cell fusion experiments reveal distinctly different association characteristics of cell-surface receptors
    • Nagy P., Mátyus L., Jenei A., Panyi G., Varga S., Matkó J., et al. Cell fusion experiments reveal distinctly different association characteristics of cell-surface receptors. J Cell Sci 2001, 114:4063-4071.
    • (2001) J Cell Sci , vol.114 , pp. 4063-4071
    • Nagy, P.1    Mátyus, L.2    Jenei, A.3    Panyi, G.4    Varga, S.5    Matkó, J.6
  • 12
    • 16644374278 scopus 로고    scopus 로고
    • Cytometry of fluorescence resonance energy transfer
    • Vereb G., Matkó J., Szöllosi J. Cytometry of fluorescence resonance energy transfer. Methods Cell Biol 2004, 75:105-152.
    • (2004) Methods Cell Biol , vol.75 , pp. 105-152
    • Vereb, G.1    Matkó, J.2    Szöllosi, J.3
  • 13
    • 33846000599 scopus 로고    scopus 로고
    • Novel anti-cholesterol monoclonal immunoglobulin G antibodies as probes and potential modulators of membrane raft-dependent immune functions
    • Biro A., Cervenak L., Balogh A., Lorincz A., Uray K., Horváth A., et al. Novel anti-cholesterol monoclonal immunoglobulin G antibodies as probes and potential modulators of membrane raft-dependent immune functions. J Lipid Res 2007, 48:19-29.
    • (2007) J Lipid Res , vol.48 , pp. 19-29
    • Biro, A.1    Cervenak, L.2    Balogh, A.3    Lorincz, A.4    Uray, K.5    Horváth, A.6
  • 14
    • 40049101970 scopus 로고    scopus 로고
    • Some new faces of membrane microdomains: a complex confocal fluorescence, differential polarization, and FCS imaging study on live immune cells
    • Gombos I., Steinbach G., Pomozi I., Balogh A., Vámosi G., Gansen A., et al. Some new faces of membrane microdomains: a complex confocal fluorescence, differential polarization, and FCS imaging study on live immune cells. Cytometry A 2008, 73:220-229.
    • (2008) Cytometry A , vol.73 , pp. 220-229
    • Gombos, I.1    Steinbach, G.2    Pomozi, I.3    Balogh, A.4    Vámosi, G.5    Gansen, A.6
  • 15
    • 1342306818 scopus 로고    scopus 로고
    • Nanoscale organization of multiple GPI-anchored proteins in living cell membranes
    • Sharma P., Varma R., Sarasij R.C., Ira, Gousset K., Krishnamoorthy G., et al. Nanoscale organization of multiple GPI-anchored proteins in living cell membranes. Cell 2004, 116:577-589.
    • (2004) Cell , vol.116 , pp. 577-589
    • Sharma, P.1    Varma, R.2    Sarasij, R.C.3    Ira4    Gousset, K.5    Krishnamoorthy, G.6
  • 16
    • 0035142949 scopus 로고    scopus 로고
    • Pulse EPR detection of lipid exchange between protein-rich raft and bulk domains in the membrane: methodology development and its application to studies of influenza viral membrane
    • Kawasaki K., Yin J.J., Subczynski W.K., Hyde J.S., Kusumi A. Pulse EPR detection of lipid exchange between protein-rich raft and bulk domains in the membrane: methodology development and its application to studies of influenza viral membrane. Biophys J 2001, 80:738-748.
    • (2001) Biophys J , vol.80 , pp. 738-748
    • Kawasaki, K.1    Yin, J.J.2    Subczynski, W.K.3    Hyde, J.S.4    Kusumi, A.5
  • 17
    • 33746581138 scopus 로고    scopus 로고
    • Dynamic molecular confinement in the plasma membrane by microdomains and the cytoskeleton meshwork
    • Lenne P.F., Wawrezinieck L., Conchonaud F., Wurtz O., Boned A., Guo X.J., et al. Dynamic molecular confinement in the plasma membrane by microdomains and the cytoskeleton meshwork. Embo J 2006, 25:3245-3256.
    • (2006) Embo J , vol.25 , pp. 3245-3256
    • Lenne, P.F.1    Wawrezinieck, L.2    Conchonaud, F.3    Wurtz, O.4    Boned, A.5    Guo, X.J.6
  • 18
    • 61349094652 scopus 로고    scopus 로고
    • Direct observation of the nanoscale dynamics of membrane lipids in a living cell
    • Eggeling C., Ringemann C., Medda R., Schwarzmann G., Sandhoff K., Polyakova S., et al. Direct observation of the nanoscale dynamics of membrane lipids in a living cell. Nature 2009, 457:1159-1162.
    • (2009) Nature , vol.457 , pp. 1159-1162
    • Eggeling, C.1    Ringemann, C.2    Medda, R.3    Schwarzmann, G.4    Sandhoff, K.5    Polyakova, S.6
  • 19
    • 0032552054 scopus 로고    scopus 로고
    • GPI-anchored proteins are organized in submicron domains at the cell surface
    • Varma R., Mayor S. GPI-anchored proteins are organized in submicron domains at the cell surface. Nature 1998, 394:798-801.
    • (1998) Nature , vol.394 , pp. 798-801
    • Varma, R.1    Mayor, S.2
  • 20
    • 0034611005 scopus 로고    scopus 로고
    • Sphingolipid-cholesterol rafts diffuse as small entities in the plasma membrane of mammalian cells
    • Pralle A., Keller P., Florin E.L., Simons K., Horber J.K. Sphingolipid-cholesterol rafts diffuse as small entities in the plasma membrane of mammalian cells. J Cell Biol 2000, 148:997-1008.
    • (2000) J Cell Biol , vol.148 , pp. 997-1008
    • Pralle, A.1    Keller, P.2    Florin, E.L.3    Simons, K.4    Horber, J.K.5
  • 21
    • 33751547691 scopus 로고    scopus 로고
    • Nanoscale organization of nicotinic acetylcholine receptors revealed by stimulated emission depletion microscopy
    • Kellner R.R., Baier C.J., Willig K.I., Hell S.W., Barrantes F.J. Nanoscale organization of nicotinic acetylcholine receptors revealed by stimulated emission depletion microscopy. Neuroscience 2007, 144:135-143.
    • (2007) Neuroscience , vol.144 , pp. 135-143
    • Kellner, R.R.1    Baier, C.J.2    Willig, K.I.3    Hell, S.W.4    Barrantes, F.J.5
  • 22
    • 0037112996 scopus 로고    scopus 로고
    • Lipid rafts and the local density of ErbB proteins influence the biological role of homo- and heteroassociations of ErbB2
    • Nagy P., Vereb G., Sebestyén Z., Horváth G., Lockett S.J., Damjanovich S., et al. Lipid rafts and the local density of ErbB proteins influence the biological role of homo- and heteroassociations of ErbB2. J Cell Sci 2002, 115:4251-4262.
    • (2002) J Cell Sci , vol.115 , pp. 4251-4262
    • Nagy, P.1    Vereb, G.2    Sebestyén, Z.3    Horváth, G.4    Lockett, S.J.5    Damjanovich, S.6
  • 23
    • 54049146208 scopus 로고    scopus 로고
    • Quantitative microscopy and systems biology: seeing the whole picture
    • Verveer P.J., Bastiaens P.I.H. Quantitative microscopy and systems biology: seeing the whole picture. Histochem Cell Biol 2008, 130:833-843.
    • (2008) Histochem Cell Biol , vol.130 , pp. 833-843
    • Verveer, P.J.1    Bastiaens, P.I.H.2
  • 24
    • 0034075971 scopus 로고    scopus 로고
    • High-resolution FRET microscopy of cholera toxin B-subunit and GPI-anchored proteins in cell plasma membranes
    • Kenworthy A.K., Petranova N., Edidin M. High-resolution FRET microscopy of cholera toxin B-subunit and GPI-anchored proteins in cell plasma membranes. Mol Biol Cell 2000, 11:1645-1655.
    • (2000) Mol Biol Cell , vol.11 , pp. 1645-1655
    • Kenworthy, A.K.1    Petranova, N.2    Edidin, M.3
  • 25
    • 33645241165 scopus 로고    scopus 로고
    • Identifying optimal lipid raft characteristics required to promote nanoscale protein-protein interactions on the plasma membrane
    • Nicolau D.V., Burrage K., Parton R.G., Hancock J.F. Identifying optimal lipid raft characteristics required to promote nanoscale protein-protein interactions on the plasma membrane. Mol Cell Biol 2006, 26:313-323.
    • (2006) Mol Cell Biol , vol.26 , pp. 313-323
    • Nicolau, D.V.1    Burrage, K.2    Parton, R.G.3    Hancock, J.F.4
  • 26
    • 0031750335 scopus 로고    scopus 로고
    • Lipid domain structure of the plasma membrane revealed by patching of membrane components
    • Harder T., Scheiffele P., Verkade P., Simons K. Lipid domain structure of the plasma membrane revealed by patching of membrane components. J Cell Biol 1998, 141:929-942.
    • (1998) J Cell Biol , vol.141 , pp. 929-942
    • Harder, T.1    Scheiffele, P.2    Verkade, P.3    Simons, K.4
  • 27
    • 0035041672 scopus 로고    scopus 로고
    • Cross-correlation analysis of inner-leaflet-anchored green fluorescent protein co-redistributed with IgE receptors and outer leaflet lipid raft components
    • Pyenta P.S., Holowka D., Baird B. Cross-correlation analysis of inner-leaflet-anchored green fluorescent protein co-redistributed with IgE receptors and outer leaflet lipid raft components. Biophys J 2001, 80:2120-2132.
    • (2001) Biophys J , vol.80 , pp. 2120-2132
    • Pyenta, P.S.1    Holowka, D.2    Baird, B.3
  • 28
    • 17844364513 scopus 로고    scopus 로고
    • Paradigm shift of the plasma membrane concept from the two-dimensional continuum fluid to the partitioned fluid: high-speed single-molecule tracking of membrane molecules
    • Kusumi A., Nakada C., Ritchie K., Murase K., Suzuki K., Murakoshi H., et al. Paradigm shift of the plasma membrane concept from the two-dimensional continuum fluid to the partitioned fluid: high-speed single-molecule tracking of membrane molecules. Annu Rev Biophys Biomol Struct 2005, 34:351-378.
    • (2005) Annu Rev Biophys Biomol Struct , vol.34 , pp. 351-378
    • Kusumi, A.1    Nakada, C.2    Ritchie, K.3    Murase, K.4    Suzuki, K.5    Murakoshi, H.6
  • 29
    • 33745801153 scopus 로고    scopus 로고
    • Lipid rafts: contentious only from simplistic standpoints
    • Hancock J.F. Lipid rafts: contentious only from simplistic standpoints. Nat Rev Mol Cell Biol 2006, 7:456-462.
    • (2006) Nat Rev Mol Cell Biol , vol.7 , pp. 456-462
    • Hancock, J.F.1
  • 30
    • 0038492661 scopus 로고    scopus 로고
    • Dynamic, yet structured: the cell membrane three decades after the Singer-Nicolson model
    • Vereb G., Szöllosi J., Matkó J., Nagy P., Farkas T., Vígh L., et al. Dynamic, yet structured: the cell membrane three decades after the Singer-Nicolson model. Proc Natl Acad Sci USA 2003, 100:8053-8058.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 8053-8058
    • Vereb, G.1    Szöllosi, J.2    Matkó, J.3    Nagy, P.4    Farkas, T.5    Vígh, L.6
  • 31
    • 20444404267 scopus 로고    scopus 로고
    • Single-molecule microscopy reveals plasma membrane microdomains created by protein-protein networks that exclude or trap signaling molecules in T cells
    • Douglass A.D., Vale R.D. Single-molecule microscopy reveals plasma membrane microdomains created by protein-protein networks that exclude or trap signaling molecules in T cells. Cell 2005, 121:937-950.
    • (2005) Cell , vol.121 , pp. 937-950
    • Douglass, A.D.1    Vale, R.D.2
  • 32
    • 3543071011 scopus 로고    scopus 로고
    • Transmembrane adaptor proteins: organizers of immunoreceptor signalling
    • Hořejší V., Zhang W., Schraven B. Transmembrane adaptor proteins: organizers of immunoreceptor signalling. Nat Rev Immunol 2004, 4:603-616.
    • (2004) Nat Rev Immunol , vol.4 , pp. 603-616
    • Hořejší, V.1    Zhang, W.2    Schraven, B.3
  • 33
    • 33845901815 scopus 로고    scopus 로고
    • Lipid rafts: at a crossroad between cell biology and physics
    • Jacobson K., Mouritsen O.G., Anderson R.G.W. Lipid rafts: at a crossroad between cell biology and physics. Nat Cell Biol 2007, 9:7-14.
    • (2007) Nat Cell Biol , vol.9 , pp. 7-14
    • Jacobson, K.1    Mouritsen, O.G.2    Anderson, R.G.W.3
  • 35
    • 58149518413 scopus 로고    scopus 로고
    • Flotillin-1 stabilizes caveolin-1 in intestinal epithelial cells
    • Vassilieva E.V., Ivanov A.I., Nusrat A. Flotillin-1 stabilizes caveolin-1 in intestinal epithelial cells. Biochem Biophys Res Commun 2009, 379:460-465.
    • (2009) Biochem Biophys Res Commun , vol.379 , pp. 460-465
    • Vassilieva, E.V.1    Ivanov, A.I.2    Nusrat, A.3
  • 36
    • 0034625373 scopus 로고    scopus 로고
    • Structure and function of sphingolipid- and cholesterol-rich membrane rafts
    • Brown D.A., London E. Structure and function of sphingolipid- and cholesterol-rich membrane rafts. J Biol Chem 2000, 275:17221-17224.
    • (2000) J Biol Chem , vol.275 , pp. 17221-17224
    • Brown, D.A.1    London, E.2
  • 37
    • 9644280899 scopus 로고    scopus 로고
    • Loss of GM1 surface expression precedes annexin V-phycoerythrin binding of neutrophils undergoing spontaneous apoptosis during in vitro aging
    • Sheriff A., Gaipl U.S., Franz S., Heyder P., Voll R.E., Kalden J.R., et al. Loss of GM1 surface expression precedes annexin V-phycoerythrin binding of neutrophils undergoing spontaneous apoptosis during in vitro aging. Cytometry A 2004, 62:75-80.
    • (2004) Cytometry A , vol.62 , pp. 75-80
    • Sheriff, A.1    Gaipl, U.S.2    Franz, S.3    Heyder, P.4    Voll, R.E.5    Kalden, J.R.6
  • 38
    • 46449085498 scopus 로고    scopus 로고
    • Cytometry of raft and caveola membrane microdomains: from flow and imaging techniques to high throughput screening assays
    • Kiss E., Nagy P., Balogh A., Szöllosi J., Matkó J. Cytometry of raft and caveola membrane microdomains: from flow and imaging techniques to high throughput screening assays. Cytometry A 2008, 73:599-614.
    • (2008) Cytometry A , vol.73 , pp. 599-614
    • Kiss, E.1    Nagy, P.2    Balogh, A.3    Szöllosi, J.4    Matkó, J.5
  • 39
    • 0036775765 scopus 로고    scopus 로고
    • Selectins: lectins that initiate cell adhesion under flow
    • McEver R.P. Selectins: lectins that initiate cell adhesion under flow. Curr Opin Cell Biol 2002, 14:581-586.
    • (2002) Curr Opin Cell Biol , vol.14 , pp. 581-586
    • McEver, R.P.1
  • 40
    • 0028788963 scopus 로고
    • Leukocyte rolling in vivo is mediated by P-selectin glycoprotein ligand-1
    • Norman K.E., Moore K.L., McEver R.P., Ley K. Leukocyte rolling in vivo is mediated by P-selectin glycoprotein ligand-1. Blood 1995, 86:4417-4421.
    • (1995) Blood , vol.86 , pp. 4417-4421
    • Norman, K.E.1    Moore, K.L.2    McEver, R.P.3    Ley, K.4
  • 41
    • 0038190854 scopus 로고    scopus 로고
    • P-selectin glycoprotein ligand-1 mediates L-selectin-dependent leukocyte rolling in venules
    • Sperandio M., Smith M.L., Forlow S.B., Olson T.S., Xia L., McEver R.P., et al. P-selectin glycoprotein ligand-1 mediates L-selectin-dependent leukocyte rolling in venules. J Exp Med 2003, 197:1355-1363.
    • (2003) J Exp Med , vol.197 , pp. 1355-1363
    • Sperandio, M.1    Smith, M.L.2    Forlow, S.B.3    Olson, T.S.4    Xia, L.5    McEver, R.P.6
  • 42
    • 33751178598 scopus 로고    scopus 로고
    • Lipid raft adhesion receptors and Syk regulate selectin-dependent rolling under flow conditions
    • Abbal C., Lambelet M., Bertaggia D., Gerbex C., Martinez M., Arcaro A., et al. Lipid raft adhesion receptors and Syk regulate selectin-dependent rolling under flow conditions. Blood 2006, 108:3352-3359.
    • (2006) Blood , vol.108 , pp. 3352-3359
    • Abbal, C.1    Lambelet, M.2    Bertaggia, D.3    Gerbex, C.4    Martinez, M.5    Arcaro, A.6
  • 43
    • 0029018182 scopus 로고
    • Granules and secretory vesicles of the human neutrophil
    • Borregaard N., Kjeldsen L., Lollike K., Sengelov H. Granules and secretory vesicles of the human neutrophil. Clin Exp Immunol 1995, 101(Suppl 1):6-9.
    • (1995) Clin Exp Immunol , vol.101 , Issue.SUPPL. 1 , pp. 6-9
    • Borregaard, N.1    Kjeldsen, L.2    Lollike, K.3    Sengelov, H.4
  • 45
    • 0034677925 scopus 로고    scopus 로고
    • Identification and characterization of human SLP-2, a novel homologue of stomatin (band 7.2b) present in erythrocytes and other tissues
    • Wang Y., Morrow J.S. Identification and characterization of human SLP-2, a novel homologue of stomatin (band 7.2b) present in erythrocytes and other tissues. J Biol Chem 2000, 275:8062-8071.
    • (2000) J Biol Chem , vol.275 , pp. 8062-8071
    • Wang, Y.1    Morrow, J.S.2
  • 47
    • 4744349398 scopus 로고    scopus 로고
    • Structure and regulation of the neutrophil respiratory burst oxidase: comparison with nonphagocyte oxidases
    • Quinn M.T., Gauss K.A. Structure and regulation of the neutrophil respiratory burst oxidase: comparison with nonphagocyte oxidases. J Leukoc Biol 2004, 76:760-781.
    • (2004) J Leukoc Biol , vol.76 , pp. 760-781
    • Quinn, M.T.1    Gauss, K.A.2
  • 48
    • 0141939841 scopus 로고    scopus 로고
    • Lipid rafts determine efficiency of NADPH oxidase activation in neutrophils
    • Shao D., Segal A.W., Dekker L.V. Lipid rafts determine efficiency of NADPH oxidase activation in neutrophils. FEBS Lett 2003, 550:101-106.
    • (2003) FEBS Lett , vol.550 , pp. 101-106
    • Shao, D.1    Segal, A.W.2    Dekker, L.V.3
  • 49
    • 61449111932 scopus 로고    scopus 로고
    • Inhibition of spontaneous neutrophil apoptosis by parabutoporin acts independently of NADPH oxidase inhibition but by lipid raft-dependent stimulation of Akt
    • Remijsen Q., Vanden Berghe T., Parthoens E., Asselbergh B., Vandenabeele P., Willems J. Inhibition of spontaneous neutrophil apoptosis by parabutoporin acts independently of NADPH oxidase inhibition but by lipid raft-dependent stimulation of Akt. J Leukoc Biol 2009, 85:497-507.
    • (2009) J Leukoc Biol , vol.85 , pp. 497-507
    • Remijsen, Q.1    Vanden Berghe, T.2    Parthoens, E.3    Asselbergh, B.4    Vandenabeele, P.5    Willems, J.6
  • 51
    • 0028245643 scopus 로고
    • Neutrophil apoptosis is associated with a reduction in CD16 (FcγRIII) expression
    • Dransfield I., Buckle A.M., Savill J.S., McDowall A., Haslett C., Hogg N. Neutrophil apoptosis is associated with a reduction in CD16 (FcγRIII) expression. J Immunol 1994, 153:1254-1263.
    • (1994) J Immunol , vol.153 , pp. 1254-1263
    • Dransfield, I.1    Buckle, A.M.2    Savill, J.S.3    McDowall, A.4    Haslett, C.5    Hogg, N.6
  • 52
    • 67649213025 scopus 로고    scopus 로고
    • Association of FcγRIIa (CD32a) with lipid rafts regulates ligand binding activity
    • Bournazos S., Hart S.P., Chamberlain L.H., Glennie M.J., Dransfield I. Association of FcγRIIa (CD32a) with lipid rafts regulates ligand binding activity. J Immunol 2009, 182:8026-8036.
    • (2009) J Immunol , vol.182 , pp. 8026-8036
    • Bournazos, S.1    Hart, S.P.2    Chamberlain, L.H.3    Glennie, M.J.4    Dransfield, I.5
  • 53
    • 41649098497 scopus 로고    scopus 로고
    • Mast cell functions in the innate skin immune system
    • Metz M., Siebenhaar F., Maurer M. Mast cell functions in the innate skin immune system. Immunobiology 2008, 213:251-260.
    • (2008) Immunobiology , vol.213 , pp. 251-260
    • Metz, M.1    Siebenhaar, F.2    Maurer, M.3
  • 55
    • 24344469627 scopus 로고    scopus 로고
    • Ultrastructural studies of human basophils and mast cells
    • Dvorak A.M. Ultrastructural studies of human basophils and mast cells. J Histochem Cytochem 2005, 53:1043-1070.
    • (2005) J Histochem Cytochem , vol.53 , pp. 1043-1070
    • Dvorak, A.M.1
  • 57
    • 0030891168 scopus 로고    scopus 로고
    • Leukocyte protein tyrosine kinases: potential targets for drug discovery
    • Bolen J.B., Brugge J.S. Leukocyte protein tyrosine kinases: potential targets for drug discovery. Annu Rev Immunol 1997, 15:371-404.
    • (1997) Annu Rev Immunol , vol.15 , pp. 371-404
    • Bolen, J.B.1    Brugge, J.S.2
  • 58
    • 0032983905 scopus 로고    scopus 로고
    • Membrane organization in immunoglobulin E receptor signaling
    • Sheets E.D., Holowka D., Baird B. Membrane organization in immunoglobulin E receptor signaling. Curr Opin Chem Biol 1999, 3:95-99.
    • (1999) Curr Opin Chem Biol , vol.3 , pp. 95-99
    • Sheets, E.D.1    Holowka, D.2    Baird, B.3
  • 59
    • 0022396578 scopus 로고
    • Noncovalently and covalently bound lipid on the receptor for immunoglobulin E
    • Kinet J.P., Quarto R., Perez-Montfort R., Metzger H. Noncovalently and covalently bound lipid on the receptor for immunoglobulin E. Biochemistry 1985, 24:7342-7348.
    • (1985) Biochemistry , vol.24 , pp. 7342-7348
    • Kinet, J.P.1    Quarto, R.2    Perez-Montfort, R.3    Metzger, H.4
  • 60
    • 0034069892 scopus 로고    scopus 로고
    • Interactions between Fce{open}RI and lipid raft components are regulated by the actin cytoskeleton
    • Holowka D., Sheets E.D., Baird B. Interactions between Fce{open}RI and lipid raft components are regulated by the actin cytoskeleton. J Cell Sci 2000, 113(Pt 6):1009-1019.
    • (2000) J Cell Sci , vol.113 , Issue.PART 6 , pp. 1009-1019
    • Holowka, D.1    Sheets, E.D.2    Baird, B.3
  • 61
    • 0033782836 scopus 로고    scopus 로고
    • Mutant RBL mast cells defective in Fce{open}RI signaling and lipid raft biosynthesis are reconstituted by activated Rho-family GTPases
    • Field K.A., Apgar J.R., Hong-Geller E., Siraganian R.P., Baird B., Holowka D. Mutant RBL mast cells defective in Fce{open}RI signaling and lipid raft biosynthesis are reconstituted by activated Rho-family GTPases. Mol Biol Cell 2000, 11:3661-3673.
    • (2000) Mol Biol Cell , vol.11 , pp. 3661-3673
    • Field, K.A.1    Apgar, J.R.2    Hong-Geller, E.3    Siraganian, R.P.4    Baird, B.5    Holowka, D.6
  • 62
    • 0033961923 scopus 로고    scopus 로고
    • RING for destruction?
    • Freemont P.S. RING for destruction?. Curr Biol 2000, 10:R84-R87.
    • (2000) Curr Biol , vol.10
    • Freemont, P.S.1
  • 63
    • 0035853045 scopus 로고    scopus 로고
    • Raft-partitioning of the ubiquitin ligases Cbl and Nedd4 upon IgE-triggered cell signaling
    • Lafont F., Simons K. Raft-partitioning of the ubiquitin ligases Cbl and Nedd4 upon IgE-triggered cell signaling. Proc Natl Acad Sci USA 2001, 98:3180-3184.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 3180-3184
    • Lafont, F.1    Simons, K.2
  • 65
    • 5444265929 scopus 로고    scopus 로고
    • Cholesterol sensitivity of detergent resistance: a rapid flow cytometric test for detecting constitutive or induced raft association of membrane proteins
    • Gombos I., Bacsó Z., Detre C., Nagy H., Goda K., Andrásfalvy M., et al. Cholesterol sensitivity of detergent resistance: a rapid flow cytometric test for detecting constitutive or induced raft association of membrane proteins. Cytometry A 2004, 61:117-126.
    • (2004) Cytometry A , vol.61 , pp. 117-126
    • Gombos, I.1    Bacsó, Z.2    Detre, C.3    Nagy, H.4    Goda, K.5    Andrásfalvy, M.6
  • 66
    • 33845980546 scopus 로고    scopus 로고
    • Membrane order and molecular dynamics associated with IgE receptor cross-linking in mast cells
    • Davey A.M., Walvick R.P., Liu Y.X., Heikal A.A., Sheets E.D. Membrane order and molecular dynamics associated with IgE receptor cross-linking in mast cells. Biophys J 2007, 92:343-355.
    • (2007) Biophys J , vol.92 , pp. 343-355
    • Davey, A.M.1    Walvick, R.P.2    Liu, Y.X.3    Heikal, A.A.4    Sheets, E.D.5
  • 67
    • 34548161721 scopus 로고    scopus 로고
    • FcepsilonRI and Thy-1 domains have unique protein and lipid compositions
    • Surviladze Z., Harrison K.A., Murphy R.C., Wilson B.S. FcepsilonRI and Thy-1 domains have unique protein and lipid compositions. J Lipid Res 2007, 48:1325-1335.
    • (2007) J Lipid Res , vol.48 , pp. 1325-1335
    • Surviladze, Z.1    Harrison, K.A.2    Murphy, R.C.3    Wilson, B.S.4
  • 69
    • 0032738604 scopus 로고    scopus 로고
    • Role of CD14 in cellular recognition of bacterial lipopolysaccharides
    • Kitchens R.L. Role of CD14 in cellular recognition of bacterial lipopolysaccharides. Chem Immunol 2000, 74:61-82.
    • (2000) Chem Immunol , vol.74 , pp. 61-82
    • Kitchens, R.L.1
  • 70
    • 0033631344 scopus 로고    scopus 로고
    • Soluble CD14-mediated cellular responses to lipopolysaccharide
    • Tapping R.I., Tobias P.S. Soluble CD14-mediated cellular responses to lipopolysaccharide. Chem Immunol 2000, 74:108-121.
    • (2000) Chem Immunol , vol.74 , pp. 108-121
    • Tapping, R.I.1    Tobias, P.S.2
  • 72
    • 33847639221 scopus 로고    scopus 로고
    • Expression of GM1, a marker of lipid rafts, defines two subsets of human monocytes with differential endocytic capacity and lipopolysaccharide responsiveness
    • Moreno-Altamirano M.M., Aguilar-Carmona I., Sanchez-Garcia F.J. Expression of GM1, a marker of lipid rafts, defines two subsets of human monocytes with differential endocytic capacity and lipopolysaccharide responsiveness. Immunology 2007, 120:536-543.
    • (2007) Immunology , vol.120 , pp. 536-543
    • Moreno-Altamirano, M.M.1    Aguilar-Carmona, I.2    Sanchez-Garcia, F.J.3
  • 73
    • 0022462376 scopus 로고
    • Isolation of a lipopolysaccharide-binding acute phase reactant from rabbit serum
    • Tobias P.S., Soldau K., Ulevitch R.J. Isolation of a lipopolysaccharide-binding acute phase reactant from rabbit serum. J Exp Med 1986, 164:777-793.
    • (1986) J Exp Med , vol.164 , pp. 777-793
    • Tobias, P.S.1    Soldau, K.2    Ulevitch, R.J.3
  • 74
    • 0035191769 scopus 로고    scopus 로고
    • Lipopolysaccharide and ceramide docking to CD14 provokes ligand-specific receptor clustering in rafts
    • Pfeiffer A., Bottcher A., Orso E., Kapinsky M., Nagy P., Bodnár A., et al. Lipopolysaccharide and ceramide docking to CD14 provokes ligand-specific receptor clustering in rafts. Eur J Immunol 2001, 31:3153-3164.
    • (2001) Eur J Immunol , vol.31 , pp. 3153-3164
    • Pfeiffer, A.1    Bottcher, A.2    Orso, E.3    Kapinsky, M.4    Nagy, P.5    Bodnár, A.6
  • 75
    • 34447136077 scopus 로고    scopus 로고
    • Monocyte cholesterol homeostasis correlates with the presence of detergent resistant membrane microdomains
    • Wolf Z., Orso E., Werner T., Klunemann H.H., Schmitz G. Monocyte cholesterol homeostasis correlates with the presence of detergent resistant membrane microdomains. Cytometry A 2007, 71:486-494.
    • (2007) Cytometry A , vol.71 , pp. 486-494
    • Wolf, Z.1    Orso, E.2    Werner, T.3    Klunemann, H.H.4    Schmitz, G.5
  • 76
    • 0037096172 scopus 로고    scopus 로고
    • Mediators of innate immune recognition of bacteria concentrate in lipid rafts and facilitate lipopolysaccharide-induced cell activation
    • Triantafilou M., Miyake K., Golenbock D.T., Triantafilou K. Mediators of innate immune recognition of bacteria concentrate in lipid rafts and facilitate lipopolysaccharide-induced cell activation. J Cell Sci 2002, 115:2603-2611.
    • (2002) J Cell Sci , vol.115 , pp. 2603-2611
    • Triantafilou, M.1    Miyake, K.2    Golenbock, D.T.3    Triantafilou, K.4
  • 77
    • 4143087484 scopus 로고    scopus 로고
    • PKCζ is essential for endotoxin-induced macrophage activation
    • Cuschieri J., Umanskiy K., Solomkin J. PKCζ is essential for endotoxin-induced macrophage activation. J Surg Res 2004, 121:76-83.
    • (2004) J Surg Res , vol.121 , pp. 76-83
    • Cuschieri, J.1    Umanskiy, K.2    Solomkin, J.3
  • 79
    • 32644441610 scopus 로고    scopus 로고
    • Exogenous heat shock protein 70 binds macrophage lipid raft microdomain and stimulates phagocytosis, processing, and MHC-II presentation of antigens
    • Wang R., Kovalchin J.T., Muhlenkamp P., Chandawarkar R.Y. Exogenous heat shock protein 70 binds macrophage lipid raft microdomain and stimulates phagocytosis, processing, and MHC-II presentation of antigens. Blood 2006, 107:1636-1642.
    • (2006) Blood , vol.107 , pp. 1636-1642
    • Wang, R.1    Kovalchin, J.T.2    Muhlenkamp, P.3    Chandawarkar, R.Y.4
  • 80
    • 46949110639 scopus 로고    scopus 로고
    • Lysophospholipid metabolism facilitates Toll-like receptor 4 membrane translocation to regulate the inflammatory response
    • Jackson S.K., Abate W., Parton J., Jones S., Harwood J.L. Lysophospholipid metabolism facilitates Toll-like receptor 4 membrane translocation to regulate the inflammatory response. J Leukoc Biol 2008, 84:86-92.
    • (2008) J Leukoc Biol , vol.84 , pp. 86-92
    • Jackson, S.K.1    Abate, W.2    Parton, J.3    Jones, S.4    Harwood, J.L.5
  • 81
    • 0036180692 scopus 로고    scopus 로고
    • Cytokine induction by purified lipoteichoic acids from various bacterial species-role of LBP, sCD14, CD14 and failure to induce IL-12 and subsequent IFNγ release
    • Hermann C., Spreitzer I., Schroder N.W., Morath S., Lehner M.D., Fischer W., et al. Cytokine induction by purified lipoteichoic acids from various bacterial species-role of LBP, sCD14, CD14 and failure to induce IL-12 and subsequent IFNγ release. Eur J Immunol 2002, 32:541-551.
    • (2002) Eur J Immunol , vol.32 , pp. 541-551
    • Hermann, C.1    Spreitzer, I.2    Schroder, N.W.3    Morath, S.4    Lehner, M.D.5    Fischer, W.6
  • 82
    • 4644331827 scopus 로고    scopus 로고
    • Lipoteichoic acid and toll-like receptor 2 internalization and targeting to the Golgi are lipid raft-dependent
    • Triantafilou M., Manukyan M., Mackie A., Morath S., Hartung T., Heine H., et al. Lipoteichoic acid and toll-like receptor 2 internalization and targeting to the Golgi are lipid raft-dependent. J Biol Chem 2004, 279:40882-40889.
    • (2004) J Biol Chem , vol.279 , pp. 40882-40889
    • Triantafilou, M.1    Manukyan, M.2    Mackie, A.3    Morath, S.4    Hartung, T.5    Heine, H.6
  • 83
    • 0034780463 scopus 로고    scopus 로고
    • Differential roles of Toll-like receptors in the elicitation of proinflammatory responses by macrophages
    • Jones B.W., Heldwein K.A., Means T.K., Saukkonen J.J., Fenton M.J. Differential roles of Toll-like receptors in the elicitation of proinflammatory responses by macrophages. Ann Rheum Dis 2001, 60(Suppl 3):iii6-iii12.
    • (2001) Ann Rheum Dis , vol.60 , Issue.SUPPL. 3
    • Jones, B.W.1    Heldwein, K.A.2    Means, T.K.3    Saukkonen, J.J.4    Fenton, M.J.5
  • 85
    • 61449162968 scopus 로고    scopus 로고
    • Transglutaminase 2 is needed for the formation of an efficient phagocyte portal in macrophages engulfing apoptotic cells
    • Tóth B., Garabuczi E., Sarang Z., Vereb G., Vámosi G., Aeschlimann D., et al. Transglutaminase 2 is needed for the formation of an efficient phagocyte portal in macrophages engulfing apoptotic cells. J Immunol 2009, 182:2084-2092.
    • (2009) J Immunol , vol.182 , pp. 2084-2092
    • Tóth, B.1    Garabuczi, E.2    Sarang, Z.3    Vereb, G.4    Vámosi, G.5    Aeschlimann, D.6
  • 86
    • 70249137178 scopus 로고    scopus 로고
    • Over-expression of integrin β3 can partially overcome the defect of integrin β3 signaling in transglutaminase 2 null macrophages
    • Tóth B., Sarang Z., Vereb G., Zhang A., Tanaka S., Melino G., et al. Over-expression of integrin β3 can partially overcome the defect of integrin β3 signaling in transglutaminase 2 null macrophages. Immunol Lett 2009, 126:22-28.
    • (2009) Immunol Lett , vol.126 , pp. 22-28
    • Tóth, B.1    Sarang, Z.2    Vereb, G.3    Zhang, A.4    Tanaka, S.5    Melino, G.6
  • 87
    • 33645905424 scopus 로고    scopus 로고
    • E-LDL and Ox-LDL differentially regulate ceramide and cholesterol raft microdomains in human Macrophages
    • Grandl M., Bared S.M., Liebisch G., Werner T., Barlage S., Schmitz G. E-LDL and Ox-LDL differentially regulate ceramide and cholesterol raft microdomains in human Macrophages. Cytometry A 2006, 69:189-191.
    • (2006) Cytometry A , vol.69 , pp. 189-191
    • Grandl, M.1    Bared, S.M.2    Liebisch, G.3    Werner, T.4    Barlage, S.5    Schmitz, G.6
  • 89
    • 8444242462 scopus 로고    scopus 로고
    • Regulated recruitment of MHC class II and costimulatory molecules to lipid rafts in dendritic cells
    • Meyer zum Bueschenfelde C.O., Unternaehrer J., Mellman I., Bottomly K. Regulated recruitment of MHC class II and costimulatory molecules to lipid rafts in dendritic cells. J Immunol 2004, 173:6119-6124.
    • (2004) J Immunol , vol.173 , pp. 6119-6124
    • Meyer zum Bueschenfelde, C.O.1    Unternaehrer, J.2    Mellman, I.3    Bottomly, K.4
  • 90
    • 0037069690 scopus 로고    scopus 로고
    • Rho GTPases in cell biology
    • Etienne-Manneville S., Hall A. Rho GTPases in cell biology. Nature 2002, 420:629-635.
    • (2002) Nature , vol.420 , pp. 629-635
    • Etienne-Manneville, S.1    Hall, A.2
  • 91
    • 0035883040 scopus 로고    scopus 로고
    • Configuration of human dendritic cell cytoskeleton by Rho GTPases, the WAS protein, and differentiation
    • Burns S., Thrasher A.J., Blundell M.P., Machesky L., Jones G.E. Configuration of human dendritic cell cytoskeleton by Rho GTPases, the WAS protein, and differentiation. Blood 2001, 98:1142-1149.
    • (2001) Blood , vol.98 , pp. 1142-1149
    • Burns, S.1    Thrasher, A.J.2    Blundell, M.P.3    Machesky, L.4    Jones, G.E.5
  • 92
    • 0034577944 scopus 로고    scopus 로고
    • Toll-like receptor 2-mediated NFκB activation requires a Rac1-dependent pathway
    • Arbibe L., Mira J.P., Teusch N., Kline L., Guha M., Mackman N., et al. Toll-like receptor 2-mediated NFκB activation requires a Rac1-dependent pathway. Nat Immunol 2000, 1:533-540.
    • (2000) Nat Immunol , vol.1 , pp. 533-540
    • Arbibe, L.1    Mira, J.P.2    Teusch, N.3    Kline, L.4    Guha, M.5    Mackman, N.6
  • 93
    • 0033538574 scopus 로고    scopus 로고
    • The immunological synapse: a molecular machine controlling T cell activation
    • Grakoui A., Bromley S.K., Sumen C., Davis M.M., Shaw A.S., Allen P.M., et al. The immunological synapse: a molecular machine controlling T cell activation. Science 1999, 285:221-227.
    • (1999) Science , vol.285 , pp. 221-227
    • Grakoui, A.1    Bromley, S.K.2    Sumen, C.3    Davis, M.M.4    Shaw, A.S.5    Allen, P.M.6
  • 94
    • 0034252971 scopus 로고    scopus 로고
    • Concentration of MHC class II molecules in lipid rafts facilitates antigen presentation
    • Anderson H.A., Hiltbold E.M., Roche P.A. Concentration of MHC class II molecules in lipid rafts facilitates antigen presentation. Nat Immunol 2000, 1:156-162.
    • (2000) Nat Immunol , vol.1 , pp. 156-162
    • Anderson, H.A.1    Hiltbold, E.M.2    Roche, P.A.3
  • 95
    • 33644856731 scopus 로고    scopus 로고
    • Location of major histocompatibility complex class II molecules in rafts on dendritic cells enhances the efficiency of T-cell activation and proliferation
    • Eren E., Yates J., Cwynarski K., Preston S., Dong R., Germain C., et al. Location of major histocompatibility complex class II molecules in rafts on dendritic cells enhances the efficiency of T-cell activation and proliferation. Scand J Immunol 2006, 63:7-16.
    • (2006) Scand J Immunol , vol.63 , pp. 7-16
    • Eren, E.1    Yates, J.2    Cwynarski, K.3    Preston, S.4    Dong, R.5    Germain, C.6
  • 96
    • 0037306407 scopus 로고    scopus 로고
    • The roles of membrane microdomains (rafts) in T cell activation
    • Hořejší V. The roles of membrane microdomains (rafts) in T cell activation. Immunol Rev 2003, 191:148-164.
    • (2003) Immunol Rev , vol.191 , pp. 148-164
    • Hořejší, V.1
  • 97
    • 15244348270 scopus 로고    scopus 로고
    • Lipid rafts and their roles in T-cell activation
    • Hořejší V. Lipid rafts and their roles in T-cell activation. Microbes Infect 2005, 7:310-316.
    • (2005) Microbes Infect , vol.7 , pp. 310-316
    • Hořejší, V.1
  • 99
    • 13844296663 scopus 로고    scopus 로고
    • Immunological synapses are versatile structures enabling selective T cell polarization
    • Depoil D., Zaru R., Guiraud M., Chauveau A., Harriague J., Bismuth G., et al. Immunological synapses are versatile structures enabling selective T cell polarization. Immunity 2005, 22:185-194.
    • (2005) Immunity , vol.22 , pp. 185-194
    • Depoil, D.1    Zaru, R.2    Guiraud, M.3    Chauveau, A.4    Harriague, J.5    Bismuth, G.6
  • 100
    • 0019489786 scopus 로고
    • Cell surface characterization of malignant T cells from lymphoblastic lymphoma using monoclonal antibodies: evidence for phenotypic differences between malignant T cells from patients with acute lymphoblastic leukemia and lymphoblastic lymphoma
    • Bernard A., Boumsell L., Reinherz E.L., Nadler L.M., Ritz J., Coppin H., et al. Cell surface characterization of malignant T cells from lymphoblastic lymphoma using monoclonal antibodies: evidence for phenotypic differences between malignant T cells from patients with acute lymphoblastic leukemia and lymphoblastic lymphoma. Blood 1981, 57:1105-1110.
    • (1981) Blood , vol.57 , pp. 1105-1110
    • Bernard, A.1    Boumsell, L.2    Reinherz, E.L.3    Nadler, L.M.4    Ritz, J.5    Coppin, H.6
  • 102
    • 4544233317 scopus 로고    scopus 로고
    • Qualitatively differential regulation of T cell activation and apoptosis by T cell receptor ζ chain ITAMs and their tyrosine residues
    • Chae W.J., Lee H.K., Han J.H., Kim S.W., Bothwell A.L., Morio T., et al. Qualitatively differential regulation of T cell activation and apoptosis by T cell receptor ζ chain ITAMs and their tyrosine residues. Int Immunol 2004, 16:1225-1236.
    • (2004) Int Immunol , vol.16 , pp. 1225-1236
    • Chae, W.J.1    Lee, H.K.2    Han, J.H.3    Kim, S.W.4    Bothwell, A.L.5    Morio, T.6
  • 103
    • 0026705903 scopus 로고
    • Genetic evidence for the involvement of the lck tyrosine kinase in signal transduction through the T cell antigen receptor
    • Straus D.B., Weiss A. Genetic evidence for the involvement of the lck tyrosine kinase in signal transduction through the T cell antigen receptor. Cell 1992, 70:585-593.
    • (1992) Cell , vol.70 , pp. 585-593
    • Straus, D.B.1    Weiss, A.2
  • 104
    • 0032559586 scopus 로고    scopus 로고
    • Cytoskeletal polarization of T cells is regulated by an immunoreceptor tyrosine-based activation motif-dependent mechanism
    • Lowin-Kropf B., Shapiro V.S., Weiss A. Cytoskeletal polarization of T cells is regulated by an immunoreceptor tyrosine-based activation motif-dependent mechanism. J Cell Biol 1998, 140:861-871.
    • (1998) J Cell Biol , vol.140 , pp. 861-871
    • Lowin-Kropf, B.1    Shapiro, V.S.2    Weiss, A.3
  • 105
    • 0031918006 scopus 로고    scopus 로고
    • Genetic evidence of a role for Lck in T-cell receptor function independent or downstream of ZAP-70/Syk protein tyrosine kinases
    • Wong J., Straus D., Chan A.C. Genetic evidence of a role for Lck in T-cell receptor function independent or downstream of ZAP-70/Syk protein tyrosine kinases. Mol Cell Biol 1998, 18:2855-2866.
    • (1998) Mol Cell Biol , vol.18 , pp. 2855-2866
    • Wong, J.1    Straus, D.2    Chan, A.C.3
  • 106
    • 0029031806 scopus 로고
    • Binding of ZAP-70 to phosphorylated T-cell receptor ζ and η enhances its autophosphorylation and generates specific binding sites for SH2 domain-containing proteins
    • Neumeister E.N., Zhu Y., Richard S., Terhorst C., Chan A.C., Shaw A.S. Binding of ZAP-70 to phosphorylated T-cell receptor ζ and η enhances its autophosphorylation and generates specific binding sites for SH2 domain-containing proteins. Mol Cell Biol 1995, 15:3171-3178.
    • (1995) Mol Cell Biol , vol.15 , pp. 3171-3178
    • Neumeister, E.N.1    Zhu, Y.2    Richard, S.3    Terhorst, C.4    Chan, A.C.5    Shaw, A.S.6
  • 107
    • 36749064485 scopus 로고    scopus 로고
    • Single-molecule level analysis of the subunit composition of the T cell receptor on live T cells
    • James J.R., White S.S., Clarke R.W., Johansen A.M., Dunne P.D., Sleep D.L., et al. Single-molecule level analysis of the subunit composition of the T cell receptor on live T cells. Proc Natl Acad Sci USA 2007, 104:17662-17667.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 17662-17667
    • James, J.R.1    White, S.S.2    Clarke, R.W.3    Johansen, A.M.4    Dunne, P.D.5    Sleep, D.L.6
  • 108
    • 27644508227 scopus 로고    scopus 로고
    • Separation of a cholesterol-enriched microdomain involved in T-cell signal transduction
    • Shimada Y., Inomata M., Suzuki H., Hayashi M., Waheed A.A., Ohno-Iwashita Y. Separation of a cholesterol-enriched microdomain involved in T-cell signal transduction. Febs J 2005, 272:5454-5463.
    • (2005) Febs J , vol.272 , pp. 5454-5463
    • Shimada, Y.1    Inomata, M.2    Suzuki, H.3    Hayashi, M.4    Waheed, A.A.5    Ohno-Iwashita, Y.6
  • 109
    • 34250856231 scopus 로고    scopus 로고
    • Recombinant anti-CD4 antibody 13B8.2 blocks membrane-proximal events by excluding the Zap70 molecule and downstream targets SLP-76, PLCγ1, and Vav-1 from the CD4-segregated Brij 98 detergent-resistant raft domains
    • Chentouf M., Ghannam S., Bes C., Troadec S., Cerutti M., Chardes T. Recombinant anti-CD4 antibody 13B8.2 blocks membrane-proximal events by excluding the Zap70 molecule and downstream targets SLP-76, PLCγ1, and Vav-1 from the CD4-segregated Brij 98 detergent-resistant raft domains. J Immunol 2007, 179:409-420.
    • (2007) J Immunol , vol.179 , pp. 409-420
    • Chentouf, M.1    Ghannam, S.2    Bes, C.3    Troadec, S.4    Cerutti, M.5    Chardes, T.6
  • 110
    • 9644284452 scopus 로고    scopus 로고
    • Single-molecule tracking of membrane molecules: plasma membrane compartmentalization and dynamic assembly of raft-philic signaling molecules
    • Kusumi A., Ike H., Nakada C., Murase K., Fujiwara T. Single-molecule tracking of membrane molecules: plasma membrane compartmentalization and dynamic assembly of raft-philic signaling molecules. Semin Immunol 2005, 17:3-21.
    • (2005) Semin Immunol , vol.17 , pp. 3-21
    • Kusumi, A.1    Ike, H.2    Nakada, C.3    Murase, K.4    Fujiwara, T.5
  • 111
    • 0034675889 scopus 로고    scopus 로고
    • Selective accumulation of raft-associated membrane protein LAT in T cell receptor signaling assemblies
    • Harder T., Kuhn M. Selective accumulation of raft-associated membrane protein LAT in T cell receptor signaling assemblies. J Cell Biol 2000, 151:199-208.
    • (2000) J Cell Biol , vol.151 , pp. 199-208
    • Harder, T.1    Kuhn, M.2
  • 112
    • 0032101348 scopus 로고    scopus 로고
    • Membrane compartmentation is required for efficient T cell activation
    • Xavier R., Brennan T., Li Q., McCormack C., Seed B. Membrane compartmentation is required for efficient T cell activation. Immunity 1998, 8:723-732.
    • (1998) Immunity , vol.8 , pp. 723-732
    • Xavier, R.1    Brennan, T.2    Li, Q.3    McCormack, C.4    Seed, B.5
  • 114
    • 1842814045 scopus 로고    scopus 로고
    • Transmembrane adaptor proteins in membrane microdomains: important regulators of immunoreceptor signaling
    • Hořejší V. Transmembrane adaptor proteins in membrane microdomains: important regulators of immunoreceptor signaling. Immunol Lett 2004, 92:43-49.
    • (2004) Immunol Lett , vol.92 , pp. 43-49
    • Hořejší, V.1
  • 115
    • 0032498231 scopus 로고    scopus 로고
    • LAT: the ZAP-70 tyrosine kinase substrate that links T cell receptor to cellular activation
    • Zhang W., Sloan-Lancaster J., Kitchen J., Trible R.P., Samelson L.E. LAT: the ZAP-70 tyrosine kinase substrate that links T cell receptor to cellular activation. Cell 1998, 92:83-92.
    • (1998) Cell , vol.92 , pp. 83-92
    • Zhang, W.1    Sloan-Lancaster, J.2    Kitchen, J.3    Trible, R.P.4    Samelson, L.E.5
  • 116
    • 0035976967 scopus 로고    scopus 로고
    • Docking protein Gab2 is phosphorylated by ZAP-70 and negatively regulates T cell receptor signaling by recruitment of inhibitory molecules
    • Yamasaki S., Nishida K., Hibi M., Sakuma M., Shiina R., Takeuchi A., et al. Docking protein Gab2 is phosphorylated by ZAP-70 and negatively regulates T cell receptor signaling by recruitment of inhibitory molecules. J Biol Chem 2001, 276:45175-45183.
    • (2001) J Biol Chem , vol.276 , pp. 45175-45183
    • Yamasaki, S.1    Nishida, K.2    Hibi, M.3    Sakuma, M.4    Shiina, R.5    Takeuchi, A.6
  • 117
    • 23644435473 scopus 로고    scopus 로고
    • Role of the LAT adaptor in T-cell development and Th2 differentiation
    • Malissen B., Aguado E., Malissen M. Role of the LAT adaptor in T-cell development and Th2 differentiation. Adv Immunol 2005, 87:1-25.
    • (2005) Adv Immunol , vol.87 , pp. 1-25
    • Malissen, B.1    Aguado, E.2    Malissen, M.3
  • 118
    • 33646568738 scopus 로고    scopus 로고
    • Impaired activation and localization of LAT in anergic T cells as a consequence of a selective palmitoylation defect
    • Hundt M., Tabata H., Jeon M.S., Hayashi K., Tanaka Y., Krishna R., et al. Impaired activation and localization of LAT in anergic T cells as a consequence of a selective palmitoylation defect. Immunity 2006, 24:513-522.
    • (2006) Immunity , vol.24 , pp. 513-522
    • Hundt, M.1    Tabata, H.2    Jeon, M.S.3    Hayashi, K.4    Tanaka, Y.5    Krishna, R.6
  • 119
    • 0038719674 scopus 로고    scopus 로고
    • Combined spatial and enzymatic regulation of Csk by cAMP and protein kinase a inhibits T cell receptor signaling
    • Vang T., Abrahamsen H., Myklebust S., Hořejší V., Tasken K. Combined spatial and enzymatic regulation of Csk by cAMP and protein kinase a inhibits T cell receptor signaling. J Biol Chem 2003, 278:17597-17600.
    • (2003) J Biol Chem , vol.278 , pp. 17597-17600
    • Vang, T.1    Abrahamsen, H.2    Myklebust, S.3    Hořejší, V.4    Tasken, K.5
  • 120
    • 0037370491 scopus 로고    scopus 로고
    • Phosphorylation-dependent regulation of T-cell activation by PAG/Cbp, a lipid raft-associated transmembrane adaptor
    • Davidson D., Bakinowski M., Thomas M.L., Hořejší V., Veillette A. Phosphorylation-dependent regulation of T-cell activation by PAG/Cbp, a lipid raft-associated transmembrane adaptor. Mol Cell Biol 2003, 23:2017-2028.
    • (2003) Mol Cell Biol , vol.23 , pp. 2017-2028
    • Davidson, D.1    Bakinowski, M.2    Thomas, M.L.3    Hořejší, V.4    Veillette, A.5
  • 121
    • 0027997103 scopus 로고
    • Specific interaction of the CD45 protein-tyrosine phosphatase with tyrosine-phosphorylated CD3 ζ chain
    • Furukawa T., Itoh M., Krueger N.X., Streuli M., Saito H. Specific interaction of the CD45 protein-tyrosine phosphatase with tyrosine-phosphorylated CD3 ζ chain. Proc Natl Acad Sci USA 1994, 91:10928-10932.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 10928-10932
    • Furukawa, T.1    Itoh, M.2    Krueger, N.X.3    Streuli, M.4    Saito, H.5
  • 122
    • 0033558102 scopus 로고    scopus 로고
    • Cutting edge: the CD45 tyrosine phosphatase is an inhibitor of Lck activity in thymocytes
    • D'Oro U., Ashwell J.D. Cutting edge: the CD45 tyrosine phosphatase is an inhibitor of Lck activity in thymocytes. J Immunol 1999, 162:1879-1883.
    • (1999) J Immunol , vol.162 , pp. 1879-1883
    • D'Oro, U.1    Ashwell, J.D.2
  • 123
    • 0030453582 scopus 로고    scopus 로고
    • Exclusion of CD45 inhibits activity of p56lck associated with glycolipid-enriched membrane domains
    • Rodgers W., Rose J.K. Exclusion of CD45 inhibits activity of p56lck associated with glycolipid-enriched membrane domains. J Cell Biol 1996, 135:1515-1523.
    • (1996) J Cell Biol , vol.135 , pp. 1515-1523
    • Rodgers, W.1    Rose, J.K.2
  • 124
    • 0036839104 scopus 로고    scopus 로고
    • Dynamic association of CD45 with detergent-insoluble microdomains in T lymphocytes
    • Edmonds S.D., Ostergaard H.L. Dynamic association of CD45 with detergent-insoluble microdomains in T lymphocytes. J Immunol 2002, 169:5036-5042.
    • (2002) J Immunol , vol.169 , pp. 5036-5042
    • Edmonds, S.D.1    Ostergaard, H.L.2
  • 125
    • 10744225431 scopus 로고    scopus 로고
    • LIME: a new membrane Raft-associated adaptor protein involved in CD4 and CD8 coreceptor signaling
    • Brdičkova N., Brdička T., Angelisová P., Horváth O., Špička J., Hilgert I., et al. LIME: a new membrane Raft-associated adaptor protein involved in CD4 and CD8 coreceptor signaling. J Exp Med 2003, 198:1453-1462.
    • (2003) J Exp Med , vol.198 , pp. 1453-1462
    • Brdičkova, N.1    Brdička, T.2    Angelisová, P.3    Horváth, O.4    Špička, J.5    Hilgert, I.6
  • 126
    • 73149121261 scopus 로고    scopus 로고
    • A major lipid raft protein raftlin modulates T cell receptor signaling and enhances Th17-mediated autoimmune responses
    • Saeki K., Fukuyama S., Ayada T., Nakaya M., Aki D., Takaesu G., et al. A major lipid raft protein raftlin modulates T cell receptor signaling and enhances Th17-mediated autoimmune responses. J Immunol 2009, 182:5929-5937.
    • (2009) J Immunol , vol.182 , pp. 5929-5937
    • Saeki, K.1    Fukuyama, S.2    Ayada, T.3    Nakaya, M.4    Aki, D.5    Takaesu, G.6
  • 127
    • 0027403299 scopus 로고
    • The role of the CD28 receptor during T cell responses to antigen
    • Linsley P.S., Ledbetter J.A. The role of the CD28 receptor during T cell responses to antigen. Annu Rev Immunol 1993, 11:191-212.
    • (1993) Annu Rev Immunol , vol.11 , pp. 191-212
    • Linsley, P.S.1    Ledbetter, J.A.2
  • 128
    • 0035803552 scopus 로고    scopus 로고
    • Cytotoxic T lymphocyte antigen 4 and CD28 modulate cell surface raft expression in their regulation of T cell function
    • Martin M., Schneider H., Azouz A., Rudd C.E. Cytotoxic T lymphocyte antigen 4 and CD28 modulate cell surface raft expression in their regulation of T cell function. J Exp Med 2001, 194:1675-1681.
    • (2001) J Exp Med , vol.194 , pp. 1675-1681
    • Martin, M.1    Schneider, H.2    Azouz, A.3    Rudd, C.E.4
  • 129
    • 29144456697 scopus 로고    scopus 로고
    • Ligation of CD28 by its natural ligand CD86 in the absence of TCR stimulation induces lipid raft polarization in human CD4 T cells
    • Kovacs B., Parry R.V., Ma Z., Fan E., Shivers D.K., Freiberg B.A., et al. Ligation of CD28 by its natural ligand CD86 in the absence of TCR stimulation induces lipid raft polarization in human CD4 T cells. J Immunol 2005, 175:7848-7854.
    • (2005) J Immunol , vol.175 , pp. 7848-7854
    • Kovacs, B.1    Parry, R.V.2    Ma, Z.3    Fan, E.4    Shivers, D.K.5    Freiberg, B.A.6
  • 130
    • 13644268540 scopus 로고    scopus 로고
    • Dlgh1 coordinates actin polymerization, synaptic T cell receptor and lipid raft aggregation, and effector function in T cells
    • Round J.L., Tomassian T., Zhang M., Patel V., Schoenberger S.P., Miceli M.C. Dlgh1 coordinates actin polymerization, synaptic T cell receptor and lipid raft aggregation, and effector function in T cells. J Exp Med 2005, 201:419-430.
    • (2005) J Exp Med , vol.201 , pp. 419-430
    • Round, J.L.1    Tomassian, T.2    Zhang, M.3    Patel, V.4    Schoenberger, S.P.5    Miceli, M.C.6
  • 131
    • 33750533178 scopus 로고    scopus 로고
    • CD28 interaction with filamin-A controls lipid raft accumulation at the T-cell immunological synapse
    • Tavano R., Contento R.L., Baranda S.J., Soligo M., Tuosto L., Manes S., et al. CD28 interaction with filamin-A controls lipid raft accumulation at the T-cell immunological synapse. Nat Cell Biol 2006, 8:1270-1276.
    • (2006) Nat Cell Biol , vol.8 , pp. 1270-1276
    • Tavano, R.1    Contento, R.L.2    Baranda, S.J.3    Soligo, M.4    Tuosto, L.5    Manes, S.6
  • 132
    • 49149091747 scopus 로고    scopus 로고
    • The tumor suppressor death-associated protein kinase targets to TCR-stimulated NFκB activation
    • Chuang Y.T., Fang L.W., Lin-Feng M.H., Chen R.H., Lai M.Z. The tumor suppressor death-associated protein kinase targets to TCR-stimulated NFκB activation. J Immunol 2008, 180:3238-3249.
    • (2008) J Immunol , vol.180 , pp. 3238-3249
    • Chuang, Y.T.1    Fang, L.W.2    Lin-Feng, M.H.3    Chen, R.H.4    Lai, M.Z.5
  • 133
    • 12344309068 scopus 로고    scopus 로고
    • T cell receptor-induced lipid raft recruitment of the IκB kinase complex is necessary and sufficient for NFκB activation occurring in the cytosol
    • Sebald A., Mattioli I., Schmitz M.L. T cell receptor-induced lipid raft recruitment of the IκB kinase complex is necessary and sufficient for NFκB activation occurring in the cytosol. Eur J Immunol 2005, 35:318-325.
    • (2005) Eur J Immunol , vol.35 , pp. 318-325
    • Sebald, A.1    Mattioli, I.2    Schmitz, M.L.3
  • 134
    • 0842320992 scopus 로고    scopus 로고
    • Kv1.3 potassium channels are localized in the immunological synapse formed between cytotoxic and target cells
    • Panyi G., Vámosi G., Bacsó Z., Bagdány M., Bodnár A., Varga Z., et al. Kv1.3 potassium channels are localized in the immunological synapse formed between cytotoxic and target cells. Proc Natl Acad Sci USA 2004, 101:1285-1290.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 1285-1290
    • Panyi, G.1    Vámosi, G.2    Bacsó, Z.3    Bagdány, M.4    Bodnár, A.5    Varga, Z.6
  • 135
    • 67649964254 scopus 로고    scopus 로고
    • Functional consequences of Kv1.3 ion channel rearrangement into the immunological synapse
    • Tóth Á., Szilágyi O., Krasznai Z., Panyi G., Hajdu P. Functional consequences of Kv1.3 ion channel rearrangement into the immunological synapse. Immunol Lett 2009, 125:15-21.
    • (2009) Immunol Lett , vol.125 , pp. 15-21
    • Tóth, Á.1    Szilágyi, O.2    Krasznai, Z.3    Panyi, G.4    Hajdu, P.5
  • 136
    • 33745156093 scopus 로고    scopus 로고
    • K+ channel blockers: novel tools to inhibit T cell activation leading to specific immunosuppression
    • Panyi G., Possani L.D., Rodriguez de la Vega R.C., Gáspár R., Varga Z. K+ channel blockers: novel tools to inhibit T cell activation leading to specific immunosuppression. Curr Pharm Des 2006, 12:2199-2220.
    • (2006) Curr Pharm Des , vol.12 , pp. 2199-2220
    • Panyi, G.1    Possani, L.D.2    Rodriguez de la Vega, R.C.3    Gáspár, R.4    Varga, Z.5
  • 137
    • 62049084949 scopus 로고    scopus 로고
    • Accumulation of raft lipids in T-cell plasma membrane domains engaged in TCR signalling
    • Zech T., Ejsing C.S., Gaus K., de Wet B., Shevchenko A., Simons K., et al. Accumulation of raft lipids in T-cell plasma membrane domains engaged in TCR signalling. Embo J 2009, 28:466-476.
    • (2009) Embo J , vol.28 , pp. 466-476
    • Zech, T.1    Ejsing, C.S.2    Gaus, K.3    de Wet, B.4    Shevchenko, A.5    Simons, K.6
  • 138
    • 34447508103 scopus 로고    scopus 로고
    • Single-molecule microscopy reveals heterogeneous dynamics of lipid raft components upon TCR engagement
    • Drbal K., Moertelmaier M., Holzhauser C., Muhammad A., Fuertbauer E., Howorka S., et al. Single-molecule microscopy reveals heterogeneous dynamics of lipid raft components upon TCR engagement. Int Immunol 2007, 19:675-684.
    • (2007) Int Immunol , vol.19 , pp. 675-684
    • Drbal, K.1    Moertelmaier, M.2    Holzhauser, C.3    Muhammad, A.4    Fuertbauer, E.5    Howorka, S.6
  • 140
    • 0013851832 scopus 로고
    • A lymphocyte-stimulating factor produced in vitro
    • Gordon J., MacLean L.D. A lymphocyte-stimulating factor produced in vitro. Nature 1965, 208:795-796.
    • (1965) Nature , vol.208 , pp. 795-796
    • Gordon, J.1    MacLean, L.D.2
  • 141
    • 0028286627 scopus 로고
    • Heterodimerization of the IL-2 receptor beta- and gamma-chain cytoplasmic domains is required for signalling
    • Nakamura Y., Russell S.M., Mess S.A., Friedmann M., Erdos M., Francois C., et al. Heterodimerization of the IL-2 receptor beta- and gamma-chain cytoplasmic domains is required for signalling. Nature 1994, 369:330-333.
    • (1994) Nature , vol.369 , pp. 330-333
    • Nakamura, Y.1    Russell, S.M.2    Mess, S.A.3    Friedmann, M.4    Erdos, M.5    Francois, C.6
  • 142
    • 0030695442 scopus 로고    scopus 로고
    • Preassembly of interleukin 2 (IL-2) receptor subunits on resting Kit 225 K6 T cells and their modulation by IL-2, IL-7, and IL-15: a fluorescence resonance energy transfer study
    • Damjanovich S., Bene L., Matkó J., Alileche A., Goldman C.K., Sharrow S., et al. Preassembly of interleukin 2 (IL-2) receptor subunits on resting Kit 225 K6 T cells and their modulation by IL-2, IL-7, and IL-15: a fluorescence resonance energy transfer study. Proc Natl Acad Sci USA 1997, 94:13134-13139.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 13134-13139
    • Damjanovich, S.1    Bene, L.2    Matkó, J.3    Alileche, A.4    Goldman, C.K.5    Sharrow, S.6
  • 143
    • 3342924000 scopus 로고    scopus 로고
    • IL-2 and IL-15 receptor alpha-subunits are coexpressed in a supramolecular receptor cluster in lipid rafts of T cells
    • Vámosi G., Bodnár A., Vereb G., Jenei A., Goldman C.K., Langowski J., et al. IL-2 and IL-15 receptor alpha-subunits are coexpressed in a supramolecular receptor cluster in lipid rafts of T cells. Proc Natl Acad Sci USA 2004, 101:11082-11087.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 11082-11087
    • Vámosi, G.1    Bodnár, A.2    Vereb, G.3    Jenei, A.4    Goldman, C.K.5    Langowski, J.6
  • 144
    • 18244402689 scopus 로고    scopus 로고
    • GPI-microdomains (membrane rafts) and signaling of the multi-chain interleukin-2 receptor in human lymphoma/leukemia T cell lines
    • Matkó J., Bodnár A., Vereb G., Bene L., Vámosi G., Szentesi G., et al. GPI-microdomains (membrane rafts) and signaling of the multi-chain interleukin-2 receptor in human lymphoma/leukemia T cell lines. Eur J Biochem 2002, 269:1199-1208.
    • (2002) Eur J Biochem , vol.269 , pp. 1199-1208
    • Matkó, J.1    Bodnár, A.2    Vereb, G.3    Bene, L.4    Vámosi, G.5    Szentesi, G.6
  • 145
    • 0036658748 scopus 로고    scopus 로고
    • Differential localization of IL-2- and -15 receptor chains in membrane rafts of human T cells
    • Goebel J., Forrest K., Morford L., Roszman T.L. Differential localization of IL-2- and -15 receptor chains in membrane rafts of human T cells. J Leukoc Biol 2002, 72:199-206.
    • (2002) J Leukoc Biol , vol.72 , pp. 199-206
    • Goebel, J.1    Forrest, K.2    Morford, L.3    Roszman, T.L.4
  • 146
    • 40349103692 scopus 로고    scopus 로고
    • A biophysical approach to IL-2 and IL-15 receptor function: localization, conformation and interactions
    • Bodnár A., Nizsalóczki E., Mocsár G., Szalóki N., Waldmann T.A., Damjanovich S., et al. A biophysical approach to IL-2 and IL-15 receptor function: localization, conformation and interactions. Immunol Lett 2008, 116:117-125.
    • (2008) Immunol Lett , vol.116 , pp. 117-125
    • Bodnár, A.1    Nizsalóczki, E.2    Mocsár, G.3    Szalóki, N.4    Waldmann, T.A.5    Damjanovich, S.6
  • 147
    • 77950958441 scopus 로고    scopus 로고
    • Trans-presentation: a novel mechanism regulating IL-15 delivery and responses
    • Stonier S.W., Schluns K.S. Trans-presentation: a novel mechanism regulating IL-15 delivery and responses. Immunol Lett 2009.
    • (2009) Immunol Lett
    • Stonier, S.W.1    Schluns, K.S.2
  • 148
    • 0035102242 scopus 로고    scopus 로고
    • Contrasting roles of IL-2 and IL-15 in the life and death of lymphocytes: implications for immunotherapy
    • Waldmann T.A., Dubois S., Tagaya Y. Contrasting roles of IL-2 and IL-15 in the life and death of lymphocytes: implications for immunotherapy. Immunity 2001, 14:105-110.
    • (2001) Immunity , vol.14 , pp. 105-110
    • Waldmann, T.A.1    Dubois, S.2    Tagaya, Y.3
  • 151
    • 77950949849 scopus 로고    scopus 로고
    • B cell activation versus anergy; the antigen receptor as a molecular switch
    • Cambier J.C., Getahun A. B cell activation versus anergy; the antigen receptor as a molecular switch. Immunol Lett 2009.
    • (2009) Immunol Lett
    • Cambier, J.C.1    Getahun, A.2
  • 152
    • 33645310982 scopus 로고    scopus 로고
    • ITAM-mediated tonic signalling through pre-BCR and BCR complexes
    • Monroe J.G. ITAM-mediated tonic signalling through pre-BCR and BCR complexes. Nat Rev Immunol 2006, 6:283-294.
    • (2006) Nat Rev Immunol , vol.6 , pp. 283-294
    • Monroe, J.G.1
  • 153
    • 0028783322 scopus 로고
    • Syk tyrosine kinase required for mouse viability and B-cell development
    • Cheng A.M., Rowley B., Pao W., Hayday A., Bolen J.B., Pawson T. Syk tyrosine kinase required for mouse viability and B-cell development. Nature 1995, 378:303-306.
    • (1995) Nature , vol.378 , pp. 303-306
    • Cheng, A.M.1    Rowley, B.2    Pao, W.3    Hayday, A.4    Bolen, J.B.5    Pawson, T.6
  • 154
    • 1842681652 scopus 로고    scopus 로고
    • Feedback regulation of lymphocyte signalling
    • Reth M., Brummer T. Feedback regulation of lymphocyte signalling. Nat Rev Immunol 2004, 4:269-277.
    • (2004) Nat Rev Immunol , vol.4 , pp. 269-277
    • Reth, M.1    Brummer, T.2
  • 156
    • 33744494534 scopus 로고    scopus 로고
    • Quantitative proteomic analysis of B cell lipid rafts reveals that ezrin regulates antigen receptor-mediated lipid raft dynamics
    • Gupta N., Wollscheid B., Watts J.D., Scheer B., Aebersold R., DeFranco A.L. Quantitative proteomic analysis of B cell lipid rafts reveals that ezrin regulates antigen receptor-mediated lipid raft dynamics. Nat Immunol 2006, 7:625-633.
    • (2006) Nat Immunol , vol.7 , pp. 625-633
    • Gupta, N.1    Wollscheid, B.2    Watts, J.D.3    Scheer, B.4    Aebersold, R.5    DeFranco, A.L.6
  • 157
    • 33845891584 scopus 로고    scopus 로고
    • Activation-induced endocytosis of the raft-associated transmembrane adaptor protein LAB/NTAL in B lymphocytes: evidence for a role in internalization of the B cell receptor
    • Mutch C.M., Sanyal R., Unruh T.L., Grigoriou L., Zhu M., Zhang W., et al. Activation-induced endocytosis of the raft-associated transmembrane adaptor protein LAB/NTAL in B lymphocytes: evidence for a role in internalization of the B cell receptor. Int Immunol 2007, 19:19-30.
    • (2007) Int Immunol , vol.19 , pp. 19-30
    • Mutch, C.M.1    Sanyal, R.2    Unruh, T.L.3    Grigoriou, L.4    Zhu, M.5    Zhang, W.6
  • 158
    • 2542629731 scopus 로고    scopus 로고
    • NFAM1, an immunoreceptor tyrosine-based activation motif-bearing molecule that regulates B cell development and signaling
    • Ohtsuka M., Arase H., Takeuchi A., Yamasaki S., Shiina R., Suenaga T., et al. NFAM1, an immunoreceptor tyrosine-based activation motif-bearing molecule that regulates B cell development and signaling. Proc Natl Acad Sci USA 2004, 101:8126-8131.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 8126-8131
    • Ohtsuka, M.1    Arase, H.2    Takeuchi, A.3    Yamasaki, S.4    Shiina, R.5    Suenaga, T.6
  • 161
    • 0036344276 scopus 로고    scopus 로고
    • PKCβ controls IκB kinase lipid raft recruitment and activation in response to BCR signaling
    • Su T.T., Guo B., Kawakami Y., Sommer K., Chae K., Humphries L.A., et al. PKCβ controls IκB kinase lipid raft recruitment and activation in response to BCR signaling. Nat Immunol 2002, 3:780-786.
    • (2002) Nat Immunol , vol.3 , pp. 780-786
    • Su, T.T.1    Guo, B.2    Kawakami, Y.3    Sommer, K.4    Chae, K.5    Humphries, L.A.6
  • 162
    • 18844395578 scopus 로고    scopus 로고
    • Regulation of B lymphocyte activation by complement C3 and the B cell coreceptor complex
    • Rickert R.C. Regulation of B lymphocyte activation by complement C3 and the B cell coreceptor complex. Curr Opin Immunol 2005, 17:237-243.
    • (2005) Curr Opin Immunol , vol.17 , pp. 237-243
    • Rickert, R.C.1
  • 163
    • 0347994950 scopus 로고    scopus 로고
    • The tetraspanin CD81 is necessary for partitioning of coligated CD19/CD21-B cell antigen receptor complexes into signaling-active lipid rafts
    • Cherukuri A., Shoham T., Sohn H.W., Levy S., Brooks S., Carter R., et al. The tetraspanin CD81 is necessary for partitioning of coligated CD19/CD21-B cell antigen receptor complexes into signaling-active lipid rafts. J Immunol 2004, 172:370-380.
    • (2004) J Immunol , vol.172 , pp. 370-380
    • Cherukuri, A.1    Shoham, T.2    Sohn, H.W.3    Levy, S.4    Brooks, S.5    Carter, R.6
  • 165
    • 0142180086 scopus 로고    scopus 로고
    • Store-operated cation entry mediated by CD20 in membrane rafts
    • Li H., Ayer L.M., Lytton J., Deans J.P. Store-operated cation entry mediated by CD20 in membrane rafts. J Biol Chem 2003, 278:42427-42434.
    • (2003) J Biol Chem , vol.278 , pp. 42427-42434
    • Li, H.1    Ayer, L.M.2    Lytton, J.3    Deans, J.P.4
  • 166
    • 0030267031 scopus 로고    scopus 로고
    • Supramolecular complexes of MHC class I, MHC class II, CD20, and tetraspan molecules (CD53, CD81, and CD82) at the surface of a B cell line JY
    • Szöllosi J., Hořejší V., Bene L., Angelisová P., Damjanovich S. Supramolecular complexes of MHC class I, MHC class II, CD20, and tetraspan molecules (CD53, CD81, and CD82) at the surface of a B cell line JY. J Immunol 1996, 157:2939-2946.
    • (1996) J Immunol , vol.157 , pp. 2939-2946
    • Szöllosi, J.1    Hořejší, V.2    Bene, L.3    Angelisová, P.4    Damjanovich, S.5
  • 169
    • 0032055485 scopus 로고    scopus 로고
    • SHIP modulates immune receptor responses by regulating membrane association of Btk
    • Bolland S., Pearse R.N., Kurosaki T., Ravetch J.V. SHIP modulates immune receptor responses by regulating membrane association of Btk. Immunity 1998, 8:509-516.
    • (1998) Immunity , vol.8 , pp. 509-516
    • Bolland, S.1    Pearse, R.N.2    Kurosaki, T.3    Ravetch, J.V.4
  • 170
    • 26444593959 scopus 로고    scopus 로고
    • FcγRIIB Ile232Thr transmembrane polymorphism associated with human systemic lupus erythematosus decreases affinity to lipid rafts and attenuates inhibitory effects on B cell receptor signaling
    • Kono H., Kyogoku C., Suzuki T., Tsuchiya N., Honda H., Yamamoto K., et al. FcγRIIB Ile232Thr transmembrane polymorphism associated with human systemic lupus erythematosus decreases affinity to lipid rafts and attenuates inhibitory effects on B cell receptor signaling. Hum Mol Genet 2005, 14:2881-2892.
    • (2005) Hum Mol Genet , vol.14 , pp. 2881-2892
    • Kono, H.1    Kyogoku, C.2    Suzuki, T.3    Tsuchiya, N.4    Honda, H.5    Yamamoto, K.6
  • 171
    • 58149214308 scopus 로고    scopus 로고
    • Altered B cell receptor signaling in human systemic lupus erythematosus
    • Jenks S.A., Sanz I. Altered B cell receptor signaling in human systemic lupus erythematosus. Autoimmun Rev 2009, 8:209-213.
    • (2009) Autoimmun Rev , vol.8 , pp. 209-213
    • Jenks, S.A.1    Sanz, I.2
  • 172
    • 40449097937 scopus 로고    scopus 로고
    • Live cell imaging reveals that the inhibitory FcγRIIB destabilizes B cell receptor membrane-lipid interactions and blocks immune synapse formation
    • Sohn H.W., Pierce S.K., Tzeng S.J. Live cell imaging reveals that the inhibitory FcγRIIB destabilizes B cell receptor membrane-lipid interactions and blocks immune synapse formation. J Immunol 2008, 180:793-799.
    • (2008) J Immunol , vol.180 , pp. 793-799
    • Sohn, H.W.1    Pierce, S.K.2    Tzeng, S.J.3
  • 173
    • 0028799667 scopus 로고
    • Structural hierarchy in the clustering of HLA class I molecules in the plasma membrane of human lymphoblastoid cells
    • Damjanovich S., Vereb G., Schaper A., Jenei A., Matkó J., Starink J.P., et al. Structural hierarchy in the clustering of HLA class I molecules in the plasma membrane of human lymphoblastoid cells. Proc Natl Acad Sci USA 1995, 92:1122-1126.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 1122-1126
    • Damjanovich, S.1    Vereb, G.2    Schaper, A.3    Jenei, A.4    Matkó, J.5    Starink, J.P.6
  • 174
    • 0030566663 scopus 로고    scopus 로고
    • Modification of membrane cholesterol level affects expression and clustering of class I HLA molecules at the surface of JY human lymphoblasts
    • Bodnár A., Jenei A., Bene L., Damjanovich S., Matkó J. Modification of membrane cholesterol level affects expression and clustering of class I HLA molecules at the surface of JY human lymphoblasts. Immunol Lett 1996, 54:221-226.
    • (1996) Immunol Lett , vol.54 , pp. 221-226
    • Bodnár, A.1    Jenei, A.2    Bene, L.3    Damjanovich, S.4    Matkó, J.5
  • 175
    • 12644304905 scopus 로고    scopus 로고
    • HLA class I and II antigens are partially co-clustered in the plasma membrane of human lymphoblastoid cells
    • Jenei A., Varga S., Bene L., Mátyus L., Bodnár A., Bacsó Z., et al. HLA class I and II antigens are partially co-clustered in the plasma membrane of human lymphoblastoid cells. Proc Natl Acad Sci USA 1997, 94:7269-7274.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 7269-7274
    • Jenei, A.1    Varga, S.2    Bene, L.3    Mátyus, L.4    Bodnár, A.5    Bacsó, Z.6
  • 176
    • 0036775527 scopus 로고    scopus 로고
    • Lipid rafts, major histocompatibility complex molecules, and immune regulation
    • Goebel J., Forrest K., Flynn D., Rao R., Roszman T.L. Lipid rafts, major histocompatibility complex molecules, and immune regulation. Hum Immunol 2002, 63:813-820.
    • (2002) Hum Immunol , vol.63 , pp. 813-820
    • Goebel, J.1    Forrest, K.2    Flynn, D.3    Rao, R.4    Roszman, T.L.5
  • 177
    • 1842713125 scopus 로고    scopus 로고
    • Rafting MHC-II domains in the APC (presynaptic) plasma membrane and the thresholds for T-cell activation and immunological synapse formation
    • Gombos I., Detre C., Vámosi G., Matkó J. Rafting MHC-II domains in the APC (presynaptic) plasma membrane and the thresholds for T-cell activation and immunological synapse formation. Immunol Lett 2004, 92:117-124.
    • (2004) Immunol Lett , vol.92 , pp. 117-124
    • Gombos, I.1    Detre, C.2    Vámosi, G.3    Matkó, J.4
  • 178
    • 33644695558 scopus 로고    scopus 로고
    • Cholesterol and sphingolipids as lipid organizers of the immune cells' plasma membrane: their impact on the functions of MHC molecules, effector T-lymphocytes and T-cell death
    • Gombos I., Kiss E., Detre C., László G., Matkó J. Cholesterol and sphingolipids as lipid organizers of the immune cells' plasma membrane: their impact on the functions of MHC molecules, effector T-lymphocytes and T-cell death. Immunol Lett 2006, 104:59-69.
    • (2006) Immunol Lett , vol.104 , pp. 59-69
    • Gombos, I.1    Kiss, E.2    Detre, C.3    László, G.4    Matkó, J.5
  • 179
    • 33646885101 scopus 로고    scopus 로고
    • Clustering class I MHC modulates sensitivity of T cell recognition
    • Fooksman D.R., Gronvall G.K., Tang Q., Edidin M. Clustering class I MHC modulates sensitivity of T cell recognition. J Immunol 2006, 176:6673-6680.
    • (2006) J Immunol , vol.176 , pp. 6673-6680
    • Fooksman, D.R.1    Gronvall, G.K.2    Tang, Q.3    Edidin, M.4
  • 181
    • 16344370063 scopus 로고    scopus 로고
    • Simvastatin inhibits T-cell activation by selectively impairing the function of Ras superfamily GTPases
    • Ghittoni R., Patrussi L., Pirozzi K., Pellegrini M., Lazzerini P.E., Capecchi P.L., et al. Simvastatin inhibits T-cell activation by selectively impairing the function of Ras superfamily GTPases. Faseb J 2005, 19:605-607.
    • (2005) Faseb J , vol.19 , pp. 605-607
    • Ghittoni, R.1    Patrussi, L.2    Pirozzi, K.3    Pellegrini, M.4    Lazzerini, P.E.5    Capecchi, P.L.6
  • 182
    • 33947137220 scopus 로고    scopus 로고
    • Statins inhibit NK cell cytotoxicity by membrane raft depletion rather than inhibition of isoprenylation
    • Hillyard D.Z., Nutt C.D., Thomson J., McDonald K.J., Wan R.K., Cameron A.J., et al. Statins inhibit NK cell cytotoxicity by membrane raft depletion rather than inhibition of isoprenylation. Atherosclerosis 2007, 191:319-325.
    • (2007) Atherosclerosis , vol.191 , pp. 319-325
    • Hillyard, D.Z.1    Nutt, C.D.2    Thomson, J.3    McDonald, K.J.4    Wan, R.K.5    Cameron, A.J.6
  • 183
    • 30644466209 scopus 로고    scopus 로고
    • Membrane-lipid therapy: a new approach in molecular medicine
    • Escriba P.V. Membrane-lipid therapy: a new approach in molecular medicine. Trends in Molecular Medicine 2006, 12:34-43.
    • (2006) Trends in Molecular Medicine , vol.12 , pp. 34-43
    • Escriba, P.V.1
  • 184
    • 77949503413 scopus 로고    scopus 로고
    • New cholesterol-specific antibodies remodel HIV-1 target cells' surface and inhibit their in vitro virus production
    • Balogh A., Beck Z., Kis A., Izsepi E., Cervenák L., Lászlo G., et al. New cholesterol-specific antibodies remodel HIV-1 target cells' surface and inhibit their in vitro virus production. J Lipid Res 2010, 51. 10.1194/jlr.M000372.
    • (2010) J Lipid Res , pp. 51
    • Balogh, A.1    Beck, Z.2    Kis, A.3    Izsepi, E.4    Cervenák, L.5    Lászlo, G.6
  • 185
    • 63049132796 scopus 로고    scopus 로고
    • HIV: a raft-targeting approach for prevention and therapy using plant-derived compounds (review)
    • Verma S.P. HIV: a raft-targeting approach for prevention and therapy using plant-derived compounds (review). Curr Drug Targets 2009, 10:51-59.
    • (2009) Curr Drug Targets , vol.10 , pp. 51-59
    • Verma, S.P.1


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