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Volumn 369, Issue 2, 2003, Pages 301-309

Extensive temporally regulated reorganization of the lipid raft proteome following T-cell antigen receptor triggering

Author keywords

Membrane microdomain; Protein segregation; Proteomics; Signal transduction; T lymphocyte

Indexed keywords

ANTIGENS; COMPOSITION; IMMUNOLOGY; MEMBRANES; PROTEINS;

EID: 0347298692     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20020503     Document Type: Article
Times cited : (128)

References (50)
  • 1
    • 0034093737 scopus 로고    scopus 로고
    • Signal transduction by the TCR for antigen
    • Kane, L. P., Lin, J. and Weiss, A. (2000) Signal transduction by the TCR for antigen. Curr. Opin. Immunol. 12, 242-249
    • (2000) Curr. Opin. Immunol. , vol.12 , pp. 242-249
    • Kane, L.P.1    Lin, J.2    Weiss, A.3
  • 2
    • 0034046180 scopus 로고    scopus 로고
    • T cell activation and the cytoskeleton
    • Acuto, O. and Cantrell, D. (2000) T cell activation and the cytoskeleton. Annu. Rev. Immunol. 18, 165-184
    • (2000) Annu. Rev. Immunol. , vol.18 , pp. 165-184
    • Acuto, O.1    Cantrell, D.2
  • 3
    • 0033735397 scopus 로고    scopus 로고
    • Internalization and intracellular fate of TCR-CD3 complexes
    • Alcover, A. and Alarcon, B. (2000) Internalization and intracellular fate of TCR-CD3 complexes. Crit. Rev. Immunol. 20, 325-346
    • (2000) Crit. Rev. Immunol. , vol.20 , pp. 325-346
    • Alcover, A.1    Alarcon, B.2
  • 4
    • 0034327809 scopus 로고    scopus 로고
    • Regulation of cell surface expression of CTLA-4 by secretion of CTLA-4-containing lysosomes upon activation of CD4 + T cells
    • Iida, T., Ohno, H., Nakaseko, C., Sakuma, M., Takeda-Ezaki, M., Arase, H., Kominami, E., Fujisawa, T. and Saito, T. (2000) Regulation of cell surface expression of CTLA-4 by secretion of CTLA-4-containing lysosomes upon activation of CD4 + T cells. J. Immunol. 165, 5062-5068
    • (2000) J. Immunol. , vol.165 , pp. 5062-5068
    • Iida, T.1    Ohno, H.2    Nakaseko, C.3    Sakuma, M.4    Takeda-Ezaki, M.5    Arase, H.6    Kominami, E.7    Fujisawa, T.8    Saito, T.9
  • 5
    • 0034051162 scopus 로고    scopus 로고
    • Membrane rafts and signaling by the multichain immune recognition receptors
    • Langlet, C., Bernard, A. M., Drevot, P. and He, H. T. (2000) Membrane rafts and signaling by the multichain immune recognition receptors. Curr. Opin. Immunol 12, 250-255
    • (2000) Curr. Opin. Immunol. , vol.12 , pp. 250-255
    • Langlet, C.1    Bernard, A.M.2    Drevot, P.3    He, H.T.4
  • 6
    • 0034625373 scopus 로고    scopus 로고
    • Structure and function of sphingolipid- and cholesterol-rich membrane rafts
    • Brown, D. A. and London, E. (2000) Structure and function of sphingolipid- and cholesterol-rich membrane rafts. J. Biol. Chem. 275, 17221-17224
    • (2000) J. Biol. Chem. , vol.275 , pp. 17221-17224
    • Brown, D.A.1    London, E.2
  • 7
    • 0031965054 scopus 로고    scopus 로고
    • Sphingolipid organization in biomembranes: What physical studies of model membranes reveal
    • Brown, R. E. (1998) Sphingolipid organization in biomembranes: what physical studies of model membranes reveal. J. Cell Sci. 111, 1-9
    • (1998) J. Cell Sci. , vol.111 , pp. 1-9
    • Brown, R.E.1
  • 8
    • 0035423556 scopus 로고    scopus 로고
    • Roles of lipid rafts in membrane transport
    • Ikonen, E. (2001) Roles of lipid rafts in membrane transport. Curr. Opin. Cell Biol. 13, 470-477
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 470-477
    • Ikonen, E.1
  • 9
    • 0030949124 scopus 로고    scopus 로고
    • Functional rafts in cell membranes
    • Simons, K. and Ikonen, E. (1997) Functional rafts in cell membranes. Nature (London) 387, 589-572
    • (1997) Nature (London) , vol.387 , pp. 589-572
    • Simons, K.1    Ikonen, E.2
  • 11
    • 0032101348 scopus 로고    scopus 로고
    • Membrane compartmentation is required for efficient T cell activation
    • Xavier, R., Brennan, T., Li, Q., McCormack, C. and Seed, B. (1998) Membrane compartmentation is required for efficient T cell activation. Immunity 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
  • 12
    • 0032438178 scopus 로고    scopus 로고
    • Engagement of GPI-linked CD48 contributes to TCR signals and cytoskeletal reorganization: A role for lipid rafts in T cell activation
    • Moran, M. and Miceli, M. C. (1998) Engagement of GPI-linked CD48 contributes to TCR signals and cytoskeletal reorganization: a role for lipid rafts in T cell activation. Immunity 9, 787-796
    • (1998) Immunity , vol.9 , pp. 787-796
    • Moran, M.1    Miceli, M.C.2
  • 13
    • 0034665044 scopus 로고    scopus 로고
    • EMBO Workshop Report: Lymphocyte antigen receptor and coreceptor signaling, Siena, Italy, November 6-10, 1999
    • Baldari, C. T., Telford, J. L. and Acuto, O. (2000) EMBO Workshop Report: lymphocyte antigen receptor and coreceptor signaling, Siena, Italy, November 6-10, 1999. EMBO J. 19, 4857-4865
    • (2000) EMBO J. , vol.19 , pp. 4857-4865
    • Baldari, C.T.1    Telford, J.L.2    Acuto, O.3
  • 14
    • 0029768926 scopus 로고    scopus 로고
    • The aminoterminal phosphotyrosine binding domain of Shc associates with ZAP-70 and mediates TCR dependent gene activation
    • Milia, E., Di Somma, M. M., Baldoni, F., Chiari, R., Lanfrancone, L., Pelicci, P. G., Telford, J. L. and Baldari, C. T. (1996) The aminoterminal phosphotyrosine binding domain of Shc associates with ZAP-70 and mediates TCR dependent gene activation. Oncogene 13, 767-775
    • (1996) Oncogene , vol.13 , pp. 767-775
    • Milia, E.1    Di Somma, M.M.2    Baldoni, F.3    Chiari, R.4    Lanfrancone, L.5    Pelicci, P.G.6    Telford, J.L.7    Baldari, C.T.8
  • 15
    • 0032493626 scopus 로고    scopus 로고
    • Tyrosine 474 of ZAP-70 is required for association with the Shc adaptor and for T-cell antigen receptor-dependent gene activation
    • Pacini, S., Ulivieri, C., Di Somma, M. M., Isacchi, A., Lanfrancone, L., Pelicci, P. G., Telford, J. L. and Baldari, C. T. (1998) Tyrosine 474 of ZAP-70 is required for association with the Shc adaptor and for T-cell antigen receptor-dependent gene activation. J. Biol. Chem. 273, 20487-20493
    • (1998) J. Biol. Chem. , vol.273 , pp. 20487-20493
    • Pacini, S.1    Ulivieri, C.2    Di Somma, M.M.3    Isacchi, A.4    Lanfrancone, L.5    Pelicci, P.G.6    Telford, J.L.7    Baldari, C.T.8
  • 16
    • 0034673718 scopus 로고    scopus 로고
    • Constitutive activation of the Ras/MAP kinase pathway and enhanced TCR signaling by targeting the Shc adaptor to membrane rafts
    • Plyte, S., Majolini, M. B., Pacini, S., Scarpini, F., Bianchini, C., Lantrancone, L., Pelicci, P. and Baldari, C. T. (2000) Constitutive activation of the Ras/MAP kinase pathway and enhanced TCR signaling by targeting the Shc adaptor to membrane rafts. Oncogene 10, 1529-1537
    • (2000) Oncogene , vol.10 , pp. 1529-1537
    • Plyte, S.1    Majolini, M.B.2    Pacini, S.3    Scarpini, F.4    Bianchini, C.5    Lantrancone, L.6    Pelicci, P.7    Baldari, C.T.8
  • 17
    • 0027763435 scopus 로고
    • A nonlinear wide-range immobilized pH gradient for two-dimensional electrophoresis and its definition in a relevant pH scale
    • Bjellqvist, B., Pasquali, C., Ravier, F., Sanchez, J.-C. and Hochstrasser, D. F. (1993) A nonlinear wide-range immobilized pH gradient for two-dimensional electrophoresis and its definition in a relevant pH scale. Electrophoresis 14, 1357-1365
    • (1993) Electrophoresis , vol.14 , pp. 1357-1365
    • Bjellqvist, B.1    Pasquali, C.2    Ravier, F.3    Sanchez, J.-C.4    Hochstrasser, D.F.5
  • 19
    • 0039846981 scopus 로고    scopus 로고
    • Functional proteomics analysis of signal transduction pathways of the platelet-derived growth factor beta receptor
    • Soskic, V., Gorlach, M., Poznanovic, S., Boehmer, F. D. and Godovac-Zimmermann, J. (1999) Functional proteomics analysis of signal transduction pathways of the platelet-derived growth factor beta receptor. Biochemistry 38, 1757-1764
    • (1999) Biochemistry , vol.38 , pp. 1757-1764
    • Soskic, V.1    Gorlach, M.2    Poznanovic, S.3    Boehmer, F.D.4    Godovac-Zimmermann, J.5
  • 20
    • 0034714421 scopus 로고    scopus 로고
    • Gene expression data analysis
    • Brazma, A. and Vilo, J. (2000) Gene expression data analysis. FEBS Lett. 480, 17-24
    • (2000) FEBS Lett. , vol.480 , pp. 17-24
    • Brazma, A.1    Vilo, J.2
  • 21
    • 0034069892 scopus 로고    scopus 로고
    • Interactions between FcεRl and lipid raft components are regulated by the actin cytoskeleton
    • Holowka, D., Sheets, E. D. and Baird, B. (2000) Interactions between FcεRl and lipid raft components are regulated by the actin cytoskeleton. J. Cell Sci. 113, 1009-1019
    • (2000) J. Cell Sci. , vol.113 , pp. 1009-1019
    • Holowka, D.1    Sheets, E.D.2    Baird, B.3
  • 22
    • 0033997322 scopus 로고    scopus 로고
    • The role of membrane-associated adaptors in T cell receptor signalling
    • Zhang, W. and Samelson, L. E. (2001) The role of membrane-associated adaptors in T cell receptor signalling. Semin. Immunol. 12, 35-41
    • (2001) Semin. Immunol. , vol.12 , pp. 35-41
    • Zhang, W.1    Samelson, L.E.2
  • 23
    • 0032212728 scopus 로고    scopus 로고
    • LAT is required for TCR-mediated activation of PLCγ1 and the Ras pathway
    • Finco, T. S., Kadlecek, T., Zhang, W., Samelson, L. E. and Weiss, A. (1998) LAT is required for TCR-mediated activation of PLCγ1 and the Ras pathway. Immunity 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
  • 24
    • 0033830057 scopus 로고    scopus 로고
    • Temporally regulated assembly of a dynamic signaling complex associated with the activated TCR
    • Pacini, S., Valensin, S., Telford, J. L., Ladbury, J. and Baldari, C. T. (2000) Temporally regulated assembly of a dynamic signaling complex associated with the activated TCR. Eur. J. Immunol. 30, 2620-2631
    • (2000) Eur. J. Immunol. , vol.30 , pp. 2620-2631
    • Pacini, S.1    Valensin, S.2    Telford, J.L.3    Ladbury, J.4    Baldari, C.T.5
  • 25
    • 0030804183 scopus 로고    scopus 로고
    • Interaction of influenza virus haemagglutinin with sphingolipid-cholesterol membrane domains via its transmembrane domain
    • Scheiffele, P., Roth, M. G. and Simons, K. (1997) Interaction of influenza virus haemagglutinin with sphingolipid-cholesterol membrane domains via its transmembrane domain. EMBO J. 16, 5501-5508
    • (1997) EMBO J. , vol.16 , pp. 5501-5508
    • Scheiffele, P.1    Roth, M.G.2    Simons, K.3
  • 27
    • 0033033321 scopus 로고    scopus 로고
    • Clusters of glycolipid and glycosylphosphatidylinositol-anchored proteins in lymphoid cells: Accumulation of actin regulated by local tyrosine phosphorylation
    • Harder, T. and Simons, K. (1999) Clusters of glycolipid and glycosylphosphatidylinositol-anchored proteins in lymphoid cells: accumulation of actin regulated by local tyrosine phosphorylation. Eur. J. Immunol. 29, 556-562
    • (1999) Eur. J. Immunol. , vol.29 , pp. 556-562
    • Harder, T.1    Simons, K.2
  • 29
    • 0035865744 scopus 로고    scopus 로고
    • Stomatin, flotillin-1, and flotillin-2 are major integral proteins of erythrocyte lipid rafts
    • Salzer, U. and Prohaska, R. (2001) Stomatin, flotillin-1, and flotillin-2 are major integral proteins of erythrocyte lipid rafts. Blood 97, 1141-1143
    • (2001) Blood , vol.97 , pp. 1141-1143
    • Salzer, U.1    Prohaska, R.2
  • 30
    • 0032076636 scopus 로고    scopus 로고
    • TIP47: A cargo selection device for mannose 6-phosphate receptor trafficking
    • Diaz, E. and Pfeffer, S. R. (1998) TIP47: a cargo selection device for mannose 6-phosphate receptor trafficking. Cell 93, 433-443
    • (1998) Cell , vol.93 , pp. 433-443
    • Diaz, E.1    Pfeffer, S.R.2
  • 31
    • 85047669331 scopus 로고    scopus 로고
    • Post-translational protein translocation: Not all hsc70s are created equal
    • Brodsky, J. L. (1996) Post-translational protein translocation: not all hsc70s are created equal. Trends Biochem. Sci. 21, 122-126
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 122-126
    • Brodsky, J.L.1
  • 32
    • 0035423875 scopus 로고    scopus 로고
    • The glucose-regulated proteins: Stress induction and clinical applications
    • Lee, A. S. (2001) The glucose-regulated proteins: stress induction and clinical applications. Trends Biochem. Sci. 26, 504-510
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 504-510
    • Lee, A.S.1
  • 33
    • 0029040549 scopus 로고
    • Subcellular localization of human voltage-dependent anion channel isoforms
    • Yu, W. H., Wolfgang, W. and Forte, M. (1995) Subcellular localization of human voltage-dependent anion channel isoforms. J. Biol. Chem. 270, 13998-14006
    • (1995) J. Biol. Chem. , vol.270 , pp. 13998-14006
    • Yu, W.H.1    Wolfgang, W.2    Forte, M.3
  • 34
    • 0031741738 scopus 로고    scopus 로고
    • Preprotein translocase of the outer mitochondrial membrane: Molecular dissection and assembly of the general import pore complex
    • Dekker, P. J., Ryan, M. T., Brix, J., Muller, H., Honlinger, A. and Pfanner, N. (1998) Preprotein translocase of the outer mitochondrial membrane: molecular dissection and assembly of the general import pore complex. Mol. Cell. Biol. 18, 6515-6524
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 6515-6524
    • Dekker, P.J.1    Ryan, M.T.2    Brix, J.3    Muller, H.4    Honlinger, A.5    Pfanner, N.6
  • 35
    • 0033606811 scopus 로고    scopus 로고
    • Biogenesis of Tom40, core component of the TOM complex of mitochondria
    • Rapaport, D. and Neupert, W. (1999) Biogenesis of Tom40, core component of the TOM complex of mitochondria. J. Cell Biol. 146, 321-331
    • (1999) J. Cell Biol. , vol.146 , pp. 321-331
    • Rapaport, D.1    Neupert, W.2
  • 36
    • 0033525924 scopus 로고    scopus 로고
    • Oxidative phosphorylation at the fin de siecle
    • Saraste, M. (1999) Oxidative phosphorylation at the fin de siecle. Science 283, 1488-1493
    • (1999) Science , vol.283 , pp. 1488-1493
    • Saraste, M.1
  • 38
    • 0029815971 scopus 로고    scopus 로고
    • Molecular characterization of mitofilin (HMP), a mitochondria-associated protein with predicted coiled coil and intermembrane space targeting domains
    • Odgren, P. R., Toukatly, G., Bangs, P. L., Gilmore, R. and Fey, E. G. (1996) Molecular characterization of mitofilin (HMP), a mitochondria-associated protein with predicted coiled coil and intermembrane space targeting domains. J. Cell Sci. 109, 2253-2264
    • (1996) J. Cell Sci. , vol.109 , pp. 2253-2264
    • Odgren, P.R.1    Toukatly, G.2    Bangs, P.L.3    Gilmore, R.4    Fey, E.G.5
  • 39
    • 0031149813 scopus 로고    scopus 로고
    • Mitofilin is a transmembrane protein of the inner mitochondrial membrane expressed as two isoforms
    • Gieffers, C., Korioth, F., Heimann, P., Ungermann, C. and Frey, J. (1997) Mitofilin is a transmembrane protein of the inner mitochondrial membrane expressed as two isoforms. Exp. Cell Res. 232, 395-399
    • (1997) Exp. Cell Res. , vol.232 , pp. 395-399
    • Gieffers, C.1    Korioth, F.2    Heimann, P.3    Ungermann, C.4    Frey, J.5
  • 40
    • 0025181995 scopus 로고
    • Membrane topography of the subunits of ubiquinol-cytochrome-c oxidoreductase of Saccharomyces cerevisiae. The 14-kDa and the 11-kDa subunits face opposite sides of the mitochondrial inner membrane
    • Hemrika, W. and Berden, J. A. (1990) Membrane topography of the subunits of ubiquinol-cytochrome-c oxidoreductase of Saccharomyces cerevisiae. The 14-kDa and the 11-kDa subunits face opposite sides of the mitochondrial inner membrane. Eur. J. Biochem. 192, 761-765
    • (1990) Eur. J. Biochem. , vol.192 , pp. 761-765
    • Hemrika, W.1    Berden, J.A.2
  • 41
    • 0035433580 scopus 로고    scopus 로고
    • Mass spectrometric characterization of proteins extracted from Jurkat T cell detergent-resistant membrane domains
    • von Haller, P. D., Donohoe, S., Goodlett, D. R., Aebersold, R. and Watts, J. D. (2001) Mass spectrometric characterization of proteins extracted from Jurkat T cell detergent-resistant membrane domains. Proteomics 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
  • 43
    • 0028000374 scopus 로고
    • The IgM antigen receptor of B lymphocytes is associated with prohibitin and a prohibitin-related protein
    • Terashima, M., Kim, K. M., Adachi, T., Nielsen, P. J., Reth, M., Kohler, G. and Lamers, M. C. (1994) The IgM antigen receptor of B lymphocytes is associated with prohibitin and a prohibitin-related protein. EMBO J. 13, 3782-3792
    • (1994) EMBO J. , vol.13 , pp. 3782-3792
    • Terashima, M.1    Kim, K.M.2    Adachi, T.3    Nielsen, P.J.4    Reth, M.5    Kohler, G.6    Lamers, M.C.7
  • 44
    • 0027456914 scopus 로고
    • Variable subcellular localization of glycosphingolipids
    • Gillard, B. K., Thurmon, L. T. and Marcus, D. M. (1993) Variable subcellular localization of glycosphingolipids. Glycobiology 3, 57-67
    • (1993) Glycobiology , vol.3 , pp. 57-67
    • Gillard, B.K.1    Thurmon, L.T.2    Marcus, D.M.3
  • 46
    • 0037090529 scopus 로고    scopus 로고
    • TCR signal initiation machinery is pre-assembled and activated in a subset of membrane rafts
    • Drevot, P., Langlet, C., Guo, X. J., Bernard, A. M., Colard, O., Chauvin, J. P., Lasserre, R. and He, H. T. (2002) TCR signal initiation machinery is pre-assembled and activated in a subset of membrane rafts. EMBO J. 21, 1899-1908
    • (2002) EMBO J. , vol.21 , pp. 1899-1908
    • Drevot, P.1    Langlet, C.2    Guo, X.J.3    Bernard, A.M.4    Colard, O.5    Chauvin, J.P.6    Lasserre, R.7    He, H.T.8
  • 47
    • 0033613826 scopus 로고    scopus 로고
    • T lymphocyte costimulation mediated by reorganization of membrane microdomains
    • Viola, A., Schroeder, S., Sakakibara, Y. and Lanzavecchia, A. (1999) T lymphocyte costimulation mediated by reorganization of membrane microdomains. Science 283, 680-682
    • (1999) Science , vol.283 , pp. 680-682
    • Viola, A.1    Schroeder, S.2    Sakakibara, Y.3    Lanzavecchia, A.4
  • 48
    • 0033065731 scopus 로고    scopus 로고
    • Structural features of heterotrimeric G-protein-coupled receptors and their modulatory proteins
    • LeVine 3rd, H. (1999) Structural features of heterotrimeric G-protein-coupled receptors and their modulatory proteins. Mol. Neurobiol. 19, 111-149
    • (1999) Mol. Neurobiol. , vol.19 , pp. 111-149
    • LeVine H. III1
  • 49
    • 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. and Morrow, J. S. (2000) Identification and characterization of human SLP-2, a novel homologue of stomatin (band 7.2b) present in erythrocytes and other tissues. J. Biol. Chem. 275, 8062-8071
    • (2000) J. Biol. Chem. , vol.275 , pp. 8062-8071
    • Wang, Y.1    Morrow, J.S.2
  • 50
    • 0033565557 scopus 로고    scopus 로고
    • The mitochondrial permeability transition pore and its role in cell death
    • Crompton, M. (1999) The mitochondrial permeability transition pore and its role in cell death. Biochem. J. 341, 233-249
    • (1999) Biochem. J. , vol.341 , pp. 233-249
    • Crompton, M.1


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