메뉴 건너뛰기




Volumn 23, Issue 1, 2006, Pages 49-57

Lipid rafts in T cell receptor signalling (review)

Author keywords

Kinase; Lipid rafts; Microdomains; Phosphatase; T cell receptor

Indexed keywords

PROTEIN KINASE LCK; T LYMPHOCYTE RECEPTOR;

EID: 33645295218     PISSN: 09687688     EISSN: 14645203     Source Type: Journal    
DOI: 10.1080/09687860500453673     Document Type: Review
Times cited : (127)

References (82)
  • 2
    • 0027399703 scopus 로고
    • Functional characterization of a signal transducing motif present in the T cell antigen receptor zeta chain
    • Irving BA, Chan AC, Weiss A. Functional characterization of a signal transducing motif present in the T cell antigen receptor zeta chain. J Exp Med 1993;177:1093-1103.
    • (1993) J Exp Med , vol.177 , pp. 1093-1103
    • Irving, B.A.1    Chan, A.C.2    Weiss, A.3
  • 3
    • 0028986925 scopus 로고
    • CD3ε and CD3ζ cytoplasmic domains can independently generate signals for T cell development and function
    • Shinkai Y, Ma A, Cheng H-L, Alt FW. CD3ε and CD3ζ cytoplasmic domains can independently generate signals for T cell development and function. Immunity 1995;2:401-411.
    • (1995) Immunity , vol.2 , pp. 401-411
    • Shinkai, Y.1    Ma, A.2    Cheng, H.-L.3    Alt, F.W.4
  • 4
    • 0023737931 scopus 로고
    • The CD4 and CD8 T cell surface antigens are associated with the internal membrane tyrosine-protein kinase p56lck
    • Veillette A, Bookman MA, Horak EM, Bolen JB. The CD4 and CD8 T cell surface antigens are associated with the internal membrane tyrosine-protein kinase p56lck. Cell 1988;55:301-308.
    • (1988) Cell , vol.55 , pp. 301-308
    • Veillette, A.1    Bookman, M.A.2    Horak, E.M.3    Bolen, J.B.4
  • 5
    • 0029874657 scopus 로고    scopus 로고
    • T cell antigen receptor signal transduction pathways
    • Cantrell D. T cell antigen receptor signal transduction pathways. Annu Rev Immunol 1996;14:259-274.
    • (1996) Annu Rev Immunol , vol.14 , pp. 259-274
    • Cantrell, D.1
  • 6
    • 0035367576 scopus 로고    scopus 로고
    • Proximal protein tyrosine kinases in immunoreceptor signaling
    • Latour S, Veillette A. Proximal protein tyrosine kinases in immunoreceptor signaling. Curr Opin Immunol 2001;13:299-306.
    • (2001) Curr Opin Immunol , vol.13 , pp. 299-306
    • Latour, S.1    Veillette, A.2
  • 8
    • 0026612411 scopus 로고
    • pp59fyn mutant mice display differential signaling in thymocytes and peripheral T cells
    • Stein PL, Lee H-M, Rich S, Soriano P. pp59fyn mutant mice display differential signaling in thymocytes and peripheral T cells. Cell 1992;70:741-750.
    • (1992) Cell , vol.70 , pp. 741-750
    • Stein, P.L.1    Lee, H.-M.2    Rich, S.3    Soriano, P.4
  • 9
    • 0026705903 scopus 로고
    • Genetic evidence for the involvement of the lck tyrosine kinase in signal transduction through the T cell antigen receptor
    • Straus DB, 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
  • 11
    • 0025297050 scopus 로고
    • Tyrosine phosphatase CD45 is essential for coupling T-cell antigen receptor to the phosphatidyinositol pathway
    • Koretzky GA, Picus J, Thomas ML, Weiss A. Tyrosine phosphatase CD45 is essential for coupling T-cell antigen receptor to the phosphatidyinositol pathway. Nature 1990;346:66-68.
    • (1990) Nature , vol.346 , pp. 66-68
    • Koretzky, G.A.1    Picus, J.2    Thomas, M.L.3    Weiss, A.4
  • 12
    • 0025303196 scopus 로고
    • Dephosphorylation and activation of the T cell tyrosine kinase pp56lck by the leukocyte common antigen (CD45)
    • Mustelin T, Altman A. Dephosphorylation and activation of the T cell tyrosine kinase pp56lck by the leukocyte common antigen (CD45). Oncogene 1990;5:809-813.
    • (1990) Oncogene , vol.5 , pp. 809-813
    • Mustelin, T.1    Altman, A.2
  • 13
    • 0026483786 scopus 로고
    • ZAP-70: A 70 kd protein-tyrosine kinase that associates with the TCR zeta chain
    • Chan AC, Iwashima M, Turck CW, Weiss A. ZAP-70: a 70 kd protein-tyrosine kinase that associates with the TCR zeta chain. Cell 1992;71:649-662.
    • (1992) Cell , vol.71 , pp. 649-662
    • Chan, A.C.1    Iwashima, M.2    Turck, C.W.3    Weiss, A.4
  • 14
    • 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 RP, Samelson LE. 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
  • 15
    • 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
  • 16
    • 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
  • 17
    • 0030822255 scopus 로고    scopus 로고
    • Lipid microdomains in cell surface membranes
    • Edidin M. Lipid microdomains in cell surface membranes. Curr Opin Struct Biol 1997;7:528-532.
    • (1997) Curr Opin Struct Biol , vol.7 , pp. 528-532
    • Edidin, M.1
  • 18
    • 0032421354 scopus 로고    scopus 로고
    • Functions of lipid rafts in biological membranes
    • Brown DA, London E. Functions of lipid rafts in biological membranes. Annu Rev Cell Dev Biol 1998;14:111-136.
    • (1998) Annu Rev Cell Dev Biol , vol.14 , pp. 111-136
    • Brown, D.A.1    London, E.2
  • 20
    • 0031965054 scopus 로고    scopus 로고
    • Sphingolipid organization in biomembranes: What physical studies of model membranes reveal
    • Brown RE. Sphingolipid organization in biomembranes: what physical studies of model membranes reveal. J Cell Sci 1998;111:1-9.
    • (1998) J Cell Sci , vol.111 , pp. 1-9
    • Brown, R.E.1
  • 21
    • 0344585437 scopus 로고    scopus 로고
    • Lipid rafts: Elusive or illusive?
    • Munro S. Lipid rafts: elusive or illusive? Cell 2003;115:377-388.
    • (2003) Cell , vol.115 , pp. 377-388
    • Munro, S.1
  • 22
    • 0036841874 scopus 로고    scopus 로고
    • Triton promotes domain formation in lipid raft mixtures
    • Heerklotz H. Triton promotes domain formation in lipid raft mixtures. Biophys J 2002;83:2693-2701.
    • (2002) Biophys J , vol.83 , pp. 2693-2701
    • Heerklotz, H.1
  • 23
    • 0037947831 scopus 로고    scopus 로고
    • Unbiased quantitative proteomics of lipid rafts reveals high specificity for signaling factors
    • USA
    • Foster LJ, De Hoog CL, Mann M. Unbiased quantitative proteomics of lipid rafts reveals high specificity for signaling factors. Proc Natl Acad Sci USA 2003;100:5813-5818.
    • (2003) Proc Natl Acad Sci , vol.100 , pp. 5813-5818
    • Foster, L.J.1    De Hoog, C.L.2    Mann, M.3
  • 24
    • 0035433580 scopus 로고    scopus 로고
    • Mass spectrometric characterization of proteins extracted from Jurkat T cell detergent-resistant membrane domains
    • von Haller PD, Donohoe S, Goodlett DR, Aebersold R, Watts JD. Mass spectrometric characterization of proteins extracted from Jurkat T cell detergent-resistant membrane domains. Proteomics 2001;1:1010-1021.
    • (2001) Proteomics , vol.1 , pp. 1010-1021
    • Von Haller, P.D.1    Donohoe, S.2    Goodlett, D.R.3    Aebersold, R.4    Watts, J.D.5
  • 28
    • 0038788003 scopus 로고    scopus 로고
    • Mechanism of Lck recruitment to the T-cell receptor cluster as studied by single-molecule-fluorescence video imaging
    • Ike H, Kosugi A, Kato A, Iino R, Hirano H, Fujiwara T, Ritchie K, Kusumi A. Mechanism of Lck recruitment to the T-cell receptor cluster as studied by single-molecule-fluorescence video imaging. Chemphyschem 2003;4:620-626.
    • (2003) Chemphyschem , vol.4 , pp. 620-626
    • Ike, H.1    Kosugi, A.2    Kato, A.3    Iino, R.4    Hirano, H.5    Fujiwara, T.6    Ritchie, K.7    Kusumi, A.8
  • 29
    • 0031452274 scopus 로고    scopus 로고
    • Structures of Src-family tyrosine kinases
    • Sicheri F, Kuriyan J. Structures of Src-family tyrosine kinases. Curr Opin Struct Biol 1997;7:777-785.
    • (1997) Curr Opin Struct Biol , vol.7 , pp. 777-785
    • Sicheri, F.1    Kuriyan, J.2
  • 30
    • 0027493485 scopus 로고
    • Palmitylation of an amino-terminal cysteine motif of protein tyrosine kinases p56lck and p59fyn mediates interaction with glycosyl- phosphatidylinositol-anchored proteins
    • Shenoy-Scaria AM, Gauen LKT, Kwong J, Shaw AS, Lublin DM. Palmitylation of an amino-terminal cysteine motif of protein tyrosine kinases p56lck and p59fyn mediates interaction with glycosyl-phosphatidylinositol-anchored proteins. Mol Cell Biol 1993;13:6385-6392.
    • (1993) Mol Cell Biol , vol.13 , pp. 6385-6392
    • Shenoy-Scaria, A.M.1    Gauen, L.K.T.2    Kwong, J.3    Shaw, A.S.4    Lublin, D.M.5
  • 31
    • 0028145334 scopus 로고
    • Signals determining protein tyrosine kinase and glycosyl- phosphatidylinositol-anchored protein targeting to a glycolipid-enriched membrane fraction
    • Rodgers W, Crise B, Rose JK. Signals determining protein tyrosine kinase and glycosyl-phosphatidylinositol-anchored protein targeting to a glycolipid-enriched membrane fraction. Mol Cell Biol 1994;14:5384-5391.
    • (1994) Mol Cell Biol , vol.14 , pp. 5384-5391
    • Rodgers, W.1    Crise, B.2    Rose, J.K.3
  • 32
    • 0030746106 scopus 로고    scopus 로고
    • S-acylation of LCK protein tyrosine kinase is essential for its signalling function in T lymphocytes
    • Kabouridis PS, Magee AI, Ley SC. S-acylation of LCK protein tyrosine kinase is essential for its signalling function in T lymphocytes. EMBO J 1997;16:4983-4998.
    • (1997) EMBO J , vol.16 , pp. 4983-4998
    • Kabouridis, P.S.1    Magee, A.I.2    Ley, S.C.3
  • 33
    • 0026730381 scopus 로고
    • Functional analysis of the SH2 and SH3 domains of the lck tyrosine protein kinase
    • Reynolds PJ, Hurley TR, Sefton BM. Functional analysis of the SH2 and SH3 domains of the lck tyrosine protein kinase. Oncogene 1992;7:1949-1955.
    • (1992) Oncogene , vol.7 , pp. 1949-1955
    • Reynolds, P.J.1    Hurley, T.R.2    Sefton, B.M.3
  • 34
    • 0033001789 scopus 로고    scopus 로고
    • Crystal structures of c-Src reveal features of its autoinhibitory mechanism
    • Xu W, Doshi A, Lei M, Eck MJ, Harrison SC. Crystal structures of c-Src reveal features of its autoinhibitory mechanism. Mol Cell 1999;3:629-638.
    • (1999) Mol Cell , vol.3 , pp. 629-638
    • Xu, W.1    Doshi, A.2    Lei, M.3    Eck, M.J.4    Harrison, S.C.5
  • 35
    • 16144364951 scopus 로고    scopus 로고
    • Structural basis for activation of human lymphocyte kinase Lck upon tyrosine phosphorylation
    • Yamaguchi H, Hendrickson WA. Structural basis for activation of human lymphocyte kinase Lck upon tyrosine phosphorylation. Nature 1996;384:484-489.
    • (1996) Nature , vol.384 , pp. 484-489
    • Yamaguchi, H.1    Hendrickson, W.A.2
  • 38
    • 0033558102 scopus 로고    scopus 로고
    • Cutting edge: The CD45 tyrosine phosphatase is an inhibitor of Lck activity in thymocytes
    • D'Oro U, Ashwell JD. 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
  • 40
    • 0033998793 scopus 로고    scopus 로고
    • The role of lipid rafts in T cell antigen receptor (TCR) signalling
    • Janes PW, Ley SC, Magee AI, Kabouridis PS. The role of lipid rafts in T cell antigen receptor (TCR) signalling. Sem Immunol 2000;12:23-34.
    • (2000) Sem Immunol , vol.12 , pp. 23-34
    • Janes, P.W.1    Ley, S.C.2    Magee, A.I.3    Kabouridis, P.S.4
  • 41
    • 0037012578 scopus 로고    scopus 로고
    • The oxygen-substituted palmitic acid analogue, 13-oxypalmitic acid, inhibits Lck localization to lipid rafts and T cell signaling
    • Hawash IY, Hu XE, Adal A, Cassady JM, Geahlen RL, Harrison ML. The oxygen-substituted palmitic acid analogue, 13-oxypalmitic acid, inhibits Lck localization to lipid rafts and T cell signaling. Biochim Biophys Acta 2002;1589:140-150.
    • (2002) Biochim Biophys Acta , vol.1589 , pp. 140-150
    • Hawash, I.Y.1    Hu, X.E.2    Adal, A.3    Cassady, J.M.4    Geahlen, R.L.5    Harrison, M.L.6
  • 42
    • 0032142953 scopus 로고    scopus 로고
    • LAT palmitoylation: Its essential role in membrane microdomain targeting and tyrosine phosphorylation during T cell activation
    • Zhang W, Trible RP, Samelson LE. LAT palmitoylation: Its essential role in membrane microdomain targeting and tyrosine phosphorylation during T cell activation. Immunity 1998;9:239-246.
    • (1998) Immunity , vol.9 , pp. 239-246
    • Zhang, W.1    Trible, R.P.2    Samelson, L.E.3
  • 43
    • 10844280748 scopus 로고    scopus 로고
    • Cutting edge: Localization of linker for activation of T cells to lipid rafts is not essential in T cell activation and development
    • Zhu M, Shen S, Liu Y, Granillo O, Zhang W. Cutting edge: Localization of linker for activation of T cells to lipid rafts is not essential in T cell activation and development. J Immunol 2005;174:31-35.
    • (2005) J Immunol , vol.174 , pp. 31-35
    • Zhu, M.1    Shen, S.2    Liu, Y.3    Granillo, O.4    Zhang, W.5
  • 47
    • 0345138999 scopus 로고    scopus 로고
    • LIME, a novel transmembrane adaptor protein, associates with p56lck and mediates T cell activation
    • Hur EM, Son M, Lee OH, Choi YB, Park C, Lee H, Yun Y. LIME, a novel transmembrane adaptor protein, associates with p56lck and mediates T cell activation. J Exp Med 2003;198:1463-1473.
    • (2003) J Exp Med , vol.198 , pp. 1463-1473
    • Hur, E.M.1    Son, M.2    Lee, O.H.3    Choi, Y.B.4    Park, C.5    Lee, H.6    Yun, Y.7
  • 48
    • 0030453582 scopus 로고    scopus 로고
    • Exclusion of CD45 inhibits activity of p56lck associated with glycolipid-enriched membrane domains
    • Rodgers W, Rose JK. 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
  • 49
    • 0033993454 scopus 로고    scopus 로고
    • Cholesterol depletion disrupts lipid rafts and modulates the activity of multiple signaling pathways in T lymphocytes
    • Kabouridis PS, Janzen J, Magee AL, Ley SC. Cholesterol depletion disrupts lipid rafts and modulates the activity of multiple signaling pathways in T lymphocytes. Eur J Immunol 2000;30:954-963.
    • (2000) Eur J Immunol , vol.30 , pp. 954-963
    • Kabouridis, P.S.1    Janzen, J.2    Magee, A.L.3    Ley, S.C.4
  • 50
    • 0034948374 scopus 로고    scopus 로고
    • Involvement of SHP-1 tyrosine phosphatase in TCR-mediated signaling pathways in lipid rafts
    • Kosugi A, Sakakura J, Yasuda K, Ogata M, Hamaoka T. Involvement of SHP-1 tyrosine phosphatase in TCR-mediated signaling pathways in lipid rafts. Immunity 2001;14:669-680.
    • (2001) Immunity , vol.14 , pp. 669-680
    • Kosugi, A.1    Sakakura, J.2    Yasuda, K.3    Ogata, M.4    Hamaoka, T.5
  • 51
    • 0038363406 scopus 로고    scopus 로고
    • Selective interaction of LAT (linker of activated T cells) with the open-active form of Lck in lipid rafts reveals a new mechanism for the regulation of Lck in T cells
    • Kabouridis PS. Selective interaction of LAT (linker of activated T cells) with the open-active form of Lck in lipid rafts reveals a new mechanism for the regulation of Lck in T cells. Biochem J 2003;371:907-915.
    • (2003) Biochem J , vol.371 , pp. 907-915
    • Kabouridis, P.S.1
  • 53
    • 27144509762 scopus 로고    scopus 로고
    • Regulation of expression and function of Lck tyrosine kinase by high cell density
    • Ozegbe P, Chernajovsky Y, Kabouridis PS. Regulation of expression and function of Lck tyrosine kinase by high cell density. Mol Membr Biol 2005;22:363-372.
    • (2005) Mol Membr Biol , vol.22 , pp. 363-372
    • Ozegbe, P.1    Chernajovsky, Y.2    Kabouridis, P.S.3
  • 54
    • 0037105622 scopus 로고    scopus 로고
    • Fyn is essential for tyrosine phosphorylation of Csk-binding protein/phosphoprotein associated with glycolipid-enriched microdomains in lipid rafts in resting T cells
    • Yasuda K, Nagafuku M, Shima T, Okada M, Yagi T, Yamada T, Minaki Y, Kato A, Tani-Ichi S, Hamaoka T, Kosugi A. Fyn is essential for tyrosine phosphorylation of Csk-binding protein/phosphoprotein associated with glycolipid-enriched microdomains in lipid rafts in resting T cells. J Immunol 2002;169:2813-2817.
    • (2002) J Immunol , vol.169 , pp. 2813-2817
    • Yasuda, K.1    Nagafuku, M.2    Shima, T.3    Okada, M.4    Yagi, T.5    Yamada, T.6    Minaki, Y.7    Kato, A.8    Tani-Ichi, S.9    Hamaoka, T.10    Kosugi, A.11
  • 56
    • 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;8:356-360.
    • (1998) Immunity , vol.8 , pp. 356-360
    • Xavier, R.1    Brennan, T.2    Li, Q.3    McCormack, C.4    Seed, B.5
  • 58
    • 0035800835 scopus 로고    scopus 로고
    • Release from tonic inhibition of T cell activation through transient displacement of C-terminal Src kinase (Csk) from lipid rafts
    • Torgersen KM, Vang T, Abrahamsen H, Yaqub S, Horejsi V, Schraven B, Rolstad B, Mustelin T, Tasken K. Release from tonic inhibition of T cell activation through transient displacement of C-terminal Src kinase (Csk) from lipid rafts. J Biol Chem 2001;276:29313-29318.
    • (2001) J Biol Chem , vol.276 , pp. 29313-29318
    • Torgersen, K.M.1    Vang, T.2    Abrahamsen, H.3    Yaqub, S.4    Horejsi, V.5    Schraven, B.6    Rolstad, B.7    Mustelin, T.8    Tasken, K.9
  • 59
    • 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 ML, Horejsi 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    Horejsi, V.4    Veillette, A.5
  • 60
    • 0037392883 scopus 로고    scopus 로고
    • Positive and negative regulation of T-cell activation through kinases and phosphatases
    • Mustelin T, Tasken K. Positive and negative regulation of T-cell activation through kinases and phosphatases. Biochem J 2003;371:15-27.
    • (2003) Biochem J , vol.371 , pp. 15-27
    • Mustelin, T.1    Tasken, K.2
  • 61
    • 0034948337 scopus 로고    scopus 로고
    • The TCR triggering puzzle
    • van der Merwe PA. The TCR triggering puzzle. Immunity 2001;14:665-668.
    • (2001) Immunity , vol.14 , pp. 665-668
    • Van Der Merwe, P.A.1
  • 62
    • 0037318863 scopus 로고    scopus 로고
    • CD45 ectodomain controls interaction with GEMs and Lck activity for optimal TCR signaling
    • Irles C, Symons A, Michel F, Bakker TR, van der Merwe PA, Acuto O. CD45 ectodomain controls interaction with GEMs and Lck activity for optimal TCR signaling. Nat Immunol 2003;4:189-197.
    • (2003) Nat Immunol , vol.4 , pp. 189-197
    • Irles, C.1    Symons, A.2    Michel, F.3    Bakker, T.R.4    Van Der Merwe, P.A.5    Acuto, O.6
  • 63
    • 0036839104 scopus 로고    scopus 로고
    • Dynamic association of CD45 with detergent-insoluble microdomains in T lymphocytes
    • Edmonds SD, Ostergaard HL. 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
  • 64
    • 2142710163 scopus 로고    scopus 로고
    • Altered lipid raft-associated signaling and ganglioside expression in T lymphocytes from patients with systemic lupus erythema tosus
    • Jury EC, Kabouridis PS, Flores-Borja F, Mageed RA, Isenberg DA. Altered lipid raft-associated signaling and ganglioside expression in T lymphocytes from patients with systemic lupus erythema tosus. J Clin Invest 2004;113:1176-1187.
    • (2004) J Clin Invest , vol.113 , pp. 1176-1187
    • Jury, E.C.1    Kabouridis, P.S.2    Flores-Borja, F.3    Mageed, R.A.4    Isenberg, D.A.5
  • 65
    • 2942586874 scopus 로고    scopus 로고
    • Alterations in lipid raft composition and dynamics contribute to abnormal T cell responses in systemic lupus erythematosus
    • Krishnan S, Nambiar MP, Warke VG, Fisher CU, Mitchell J, Delaney N, Tsokos GC. Alterations in lipid raft composition and dynamics contribute to abnormal T cell responses in systemic lupus erythematosus. J Immunol 2004;172:7821-7831.
    • (2004) J Immunol , vol.172 , pp. 7821-7831
    • Krishnan, S.1    Nambiar, M.P.2    Warke, V.G.3    Fisher, C.U.4    Mitchell, J.5    Delaney, N.6    Tsokos, G.C.7
  • 66
    • 3142706505 scopus 로고    scopus 로고
    • T lymphocyte signalling in systemic lupus erythematosus: A lipid raft perspective
    • Jury EC, Kabouridis PS. T lymphocyte signalling in systemic lupus erythematosus: A lipid raft perspective. Lupus 2004;13:413-422.
    • (2004) Lupus , vol.13 , pp. 413-422
    • Jury, E.C.1    Kabouridis, P.S.2
  • 67
    • 0032727709 scopus 로고    scopus 로고
    • Aggregation of lipid rafts accompanies signaling via the T cell antigen receptor
    • Janes PW, Ley SC, Magee AI. Aggregation of lipid rafts accompanies signaling via the T cell antigen receptor. J Cell Biol 1999;147:447-461.
    • (1999) J Cell Biol , vol.147 , pp. 447-461
    • Janes, P.W.1    Ley, S.C.2    Magee, A.I.3
  • 70
    • 0037438349 scopus 로고    scopus 로고
    • Lipid raft distribution of CD4 depends on its palmitoylation and association with Lck, and evidence for CD4-induced lipid raft aggregation as an additional mechanism to enhance CD3 signaling
    • Fragoso R, Ren D, Zhang X, Su MW, Burakoff SJ, Jin YJ. Lipid raft distribution of CD4 depends on its palmitoylation and association with Lck, and evidence for CD4-induced lipid raft aggregation as an additional mechanism to enhance CD3 signaling. J Immunol 2003;170:913-921.
    • (2003) J Immunol , vol.170 , pp. 913-921
    • Fragoso, R.1    Ren, D.2    Zhang, X.3    Su, M.W.4    Burakoff, S.J.5    Jin, Y.J.6
  • 71
    • 2442494090 scopus 로고    scopus 로고
    • CD4 raft association and signaling regulate molecular clustering at the immunological synapse site
    • Balamuth F, Brogdon JL, Bottomly K. CD4 raft association and signaling regulate molecular clustering at the immunological synapse site. J Immunol 2004;172:5887-5892.
    • (2004) J Immunol , vol.172 , pp. 5887-5892
    • Balamuth, F.1    Brogdon, J.L.2    Bottomly, K.3
  • 73
    • 0344458247 scopus 로고
    • T-cell receptor-CD4 physical association in a murine T-cell hybridoma: Induction by antigen receptor ligation
    • USA
    • Mittler RS, Goldman SJ, Spitalny GL, Burakoff SJ. T-cell receptor-CD4 physical association in a murine T-cell hybridoma: induction by antigen receptor ligation. Proc Natl Acad Sci USA 1989;86:8531-8535.
    • (1989) Proc Natl Acad Sci , vol.86 , pp. 8531-8535
    • Mittler, R.S.1    Goldman, S.J.2    Spitalny, G.L.3    Burakoff, S.J.4
  • 74
    • 0036195934 scopus 로고    scopus 로고
    • Regulation of Lck activity by CD4 and CD28 in the immunological synapse
    • Holdorf AD, Lee KH, Burack WR, Allen PM, Shaw AS. Regulation of Lck activity by CD4 and CD28 in the immunological synapse. Nat Immunol 2002;3:259-264.
    • (2002) Nat Immunol , vol.3 , pp. 259-264
    • Holdorf, A.D.1    Lee, K.H.2    Burack, W.R.3    Allen, P.M.4    Shaw, A.S.5
  • 75
    • 0032986671 scopus 로고    scopus 로고
    • Membrane compartmentation and the response to antigen
    • Xavier R, Seed B. Membrane compartmentation and the response to antigen. Curr Opin Immunol 1999;11:265-269.
    • (1999) Curr Opin Immunol , vol.11 , pp. 265-269
    • Xavier, R.1    Seed, B.2
  • 76
    • 0034924486 scopus 로고    scopus 로고
    • The amplification of TCR signaling by dynamic membrane microdomains
    • Viola A. The amplification of TCR signaling by dynamic membrane microdomains. Trends Immunol 2001;22:322-327.
    • (2001) Trends Immunol , vol.22 , pp. 322-327
    • Viola, A.1
  • 78
    • 0034596827 scopus 로고    scopus 로고
    • Recruitment of SLP-76 to the membrane and glycolipid-enriched membrane microdomains replaces the requirement for linker for activation of T cells in T cell receptor signaling
    • Boerth NJ, Sadler JJ, Bauer DE, Clements JL, Gheith SM, Koretzky GA. Recruitment of SLP-76 to the membrane and glycolipid-enriched membrane microdomains replaces the requirement for linker for activation of T cells in T cell receptor signaling. J Exp Med 2000;192:1047-1058.
    • (2000) J Exp Med , vol.192 , pp. 1047-1058
    • Boerth, N.J.1    Sadler, J.J.2    Bauer, D.E.3    Clements, J.L.4    Gheith, S.M.5    Koretzky, G.A.6
  • 79
    • 0032212728 scopus 로고    scopus 로고
    • LAT is required for TCR-mediated activation of PLCγ1 and the Ras pathway
    • Finco TS, Kadlecek T, Zhang W, Samelson LE, Weiss A. LAT is required for TCR-mediated activation of PLCγ1 and the Ras pathway. Immunity 1998;9:617-626.
    • (1998) Immunity , vol.9 , pp. 617-626
    • Finco, T.S.1    Kadlecek, T.2    Zhang, W.3    Samelson, L.E.4    Weiss, A.5
  • 81
    • 1542399850 scopus 로고    scopus 로고
    • Lipid raft proteins have a random distribution during localized activation of the T-cell receptor
    • Glebov OO, Nichols BJ. Lipid raft proteins have a random distribution during localized activation of the T-cell receptor. Nat Cell Biol 2004;6:238-243.
    • (2004) Nat Cell Biol , vol.6 , pp. 238-243
    • Glebov, O.O.1    Nichols, B.J.2
  • 82
    • 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 AD, Vale RD. 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.