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Volumn 182, Issue 12, 2009, Pages 7672-7680

Sequential cooperation of CD2 and CD48 in the buildup of the early TCR signalosome

Author keywords

[No Author keywords available]

Indexed keywords

CD2 ANTIGEN; CD3 ANTIGEN; CD48 ANTIGEN; CD59 ANTIGEN; GLYCOSYLPHOSPHATIDYLINOSITOL; INTERLEUKIN 2; PROTEIN KINASE LCK; T LYMPHOCYTE RECEPTOR; LEUKOCYTE ANTIGEN; LYMPHOCYTE ANTIGEN RECEPTOR;

EID: 67649226596     PISSN: 00221767     EISSN: 15506606     Source Type: Journal    
DOI: 10.4049/jimmunol.0800691     Document Type: Article
Times cited : (38)

References (38)
  • 1
    • 0028014460 scopus 로고
    • Signal transduction by lymphocyte antigen receptors
    • Weiss, A., and D. R. Littman. 1994. Signal transduction by lymphocyte antigen receptors. Cell 76: 263-274.
    • (1994) Cell , vol.76 , pp. 263-274
    • Weiss, A.1    Littman, D.R.2
  • 2
    • 0037306143 scopus 로고    scopus 로고
    • Transmembrane adapters: Attractants for cytoplasmic effectors
    • Lindquist, J. A., L. Simeoni, and B. Schraven. 2003. Transmembrane adapters: attractants for cytoplasmic effectors. Immunol. Rev. 191: 165-182.
    • (2003) Immunol. Rev. , vol.191 , pp. 165-182
    • Lindquist, J.A.1    Simeoni, L.2    Schraven, B.3
  • 4
    • 0032992072 scopus 로고    scopus 로고
    • Functional analysis of LAT in TCR-mediated signaling pathways using a LATdeficient Jurkat cell line
    • Zhang, W., B. J. Irvin, R. P. Trible, R. T. Abraham, and L. E. Samelson. 1999. Functional analysis of LAT in TCR-mediated signaling pathways using a LATdeficient Jurkat cell line. Int. Immunol. 11: 943-950.
    • (1999) Int. Immunol. , vol.11 , pp. 943-950
    • Zhang, W.1    Irvin, B.J.2    Trible, R.P.3    Abraham, R.T.4    Samelson, L.E.5
  • 5
    • 0032480279 scopus 로고    scopus 로고
    • Three dimensional segregation of supramolecular activation clusters in T cells
    • Monks, C. R., B. A. Freiberg, H. Kupfer, N. Sciaky, and A. Kupfer. 1998. Three dimensional segregation of supramolecular activation clusters in T cells. Nature 395: 82-86.
    • (1998) Nature , vol.395 , pp. 82-86
    • Monks, C.R.1    Freiberg, B.A.2    Kupfer, H.3    Sciaky, N.4    Kupfer, A.5
  • 7
    • 33646137152 scopus 로고    scopus 로고
    • Immunological synapse and microclusters: The site for recognition and activation of T cells
    • Saito, T., and T. Yokosuka. 2006. Immunological synapse and microclusters: the site for recognition and activation of T cells. Curr. Opin. Immunol. 18: 305-313.
    • (2006) Curr. Opin. Immunol. , vol.18 , pp. 305-313
    • Saito, T.1    Yokosuka, T.2
  • 9
    • 0037306407 scopus 로고    scopus 로고
    • The roles of membrane microdomains (rafts) in T cell activation
    • Horejsi, V. 2003. The roles of membrane microdomains (rafts) in T cell activation. Immunol. Rev. 191: 148-164.
    • (2003) Immunol. Rev. , vol.191 , pp. 148-164
    • Horejsi, V.1
  • 10
    • 0026352248 scopus 로고
    • GPI-anchored cell-surface molecules complexed to protein tyrosine kinases
    • Stefanova, I., V. Horejsi, I. J. Ansotegui, W. Knapp, and H. Stockinger. 1991. GPI-anchored cell-surface molecules complexed to protein tyrosine kinases. Science 254: 1016-1019. (Pubitemid 21917433)
    • (1991) Science , vol.254 , Issue.5034 , pp. 1016-1019
    • Stefanova, I.1    Horejsi, V.2    Ansotegui, I.J.3    Knapp, W.4    Stockinger, H.5
  • 11
    • 0036582493 scopus 로고    scopus 로고
    • The role of glycosyl phosphatidyl inositol (GPI)-anchored cell surface proteins in T-cell activation
    • Loertscher, R., and P. Lavery. 2002. The role of glycosyl phosphatidyl inositol (GPI)-anchored cell surface proteins in T-cell activation. Transplant. Immunol. 9: 93-96.
    • (2002) Transplant. Immunol. , vol.9 , pp. 93-96
    • Loertscher, R.1    Lavery, P.2
  • 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 M. C. Miceli. 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
  • 15
    • 0036498797 scopus 로고    scopus 로고
    • Lipid raft heterogeneity in human peripheral blood T lymphoblasts: A mechanism for regulating the initiation of TCR signal transduction
    • Schade, A. E., and A. D. Levine. 2002. Lipid raft heterogeneity in human peripheral blood T lymphoblasts: a mechanism for regulating the initiation of TCR signal transduction. J. Immunol. 168: 2233-2239.
    • (2002) J. Immunol. , vol.168 , pp. 2233-2239
    • Schade, A.E.1    Levine, A.D.2
  • 16
    • 1542379962 scopus 로고    scopus 로고
    • The membrane domains occupied by glycosylphosphatidylinositol-anchored prion protein and Thy-1 differ in lipid composition
    • Brugger, B., C. Graham, I. Leibrecht, E. Mombelli, A. Jen, F. Wieland, and R. Morris. 2004. The membrane domains occupied by glycosylphosphatidylinositol-anchored prion protein and Thy-1 differ in lipid composition. J. Biol. Chem. 279: 7530-7536.
    • (2004) J. Biol. Chem. , vol.279 , pp. 7530-7536
    • Brugger, B.1    Graham, C.2    Leibrecht, I.3    Mombelli, E.4    Jen, A.5    Wieland, F.6    Morris, R.7
  • 17
    • 21244442348 scopus 로고    scopus 로고
    • Spatial and functional heterogeneity of sphingolipid-rich membrane domains
    • Kiyokawa, E., T. Baba, N. Otsuka, A. Makino, S. Ohno, and T. Kobayashi. 2005. Spatial and functional heterogeneity of sphingolipid-rich membrane domains. J. Biol. Chem. 280: 24072-24084.
    • (2005) J. Biol. Chem. , vol.280 , pp. 24072-24084
    • Kiyokawa, E.1    Baba, T.2    Otsuka, N.3    Makino, A.4    Ohno, S.5    Kobayashi, T.6
  • 19
    • 0027433268 scopus 로고
    • Production and characterization of soluble and transmembrane murine CD2: Demonstration that CD48 is a ligand for CD2 and that CD48 adhesion is regulated by CD2
    • Kaplan, A. J., K. D. Chavin, H. Yagita, M. S. Sandrin, L. H. Qin, J. Lin, G. Lindenmayer, and J. S. Bromberg. 1993. Production and characterization of soluble and transmembrane murine CD2: demonstration that CD48 is a ligand for CD2 and that CD48 adhesion is regulated by CD2. J. Immunol. 151: 4022-4032.
    • (1993) J. Immunol. , vol.151 , pp. 4022-4032
    • Kaplan, A.J.1    Chavin, K.D.2    Yagita, H.3    Sandrin, M.S.4    Qin, L.H.5    Lin, J.6    Lindenmayer, G.7    Bromberg, J.S.8
  • 20
    • 0037044326 scopus 로고    scopus 로고
    • Direct measurements of heterotypic adhesion between the cell surface proteins CD2 and CD48
    • Zhu, B., E. A. Davies, P. A. van der Merwe, T. Calvert, and D. E. Leckband. 2002. Direct measurements of heterotypic adhesion between the cell surface proteins CD2 and CD48. Biochemistry 41: 12163-12170.
    • (2002) Biochemistry , vol.41 , pp. 12163-12170
    • Zhu, B.1    Davies, E.A.2    Van Der Merwe, P.A.3    Calvert, T.4    Leckband, D.E.5
  • 21
    • 0027405371 scopus 로고
    • A soluble multimeric recombinant CD2 protein identifies CD48 as a low affinity ligand for human CD2: Divergence of CD2 ligands during the evolution of humans and mice
    • Arulanandam, A. R., P. Moingeon, M. F. Concino, M. A. Recny, K. Kato, H. Yagita, S. Koyasu, and E. L. Reinherz. 1993. A soluble multimeric recombinant CD2 protein identifies CD48 as a low affinity ligand for human CD2: divergence of CD2 ligands during the evolution of humans and mice. J. Exp. Med. 177: 1439-1450.
    • (1993) J. Exp. Med. , vol.177 , pp. 1439-1450
    • Arulanandam, A.R.1    Moingeon, P.2    Concino, M.F.3    Recny, M.A.4    Kato, K.5    Yagita, H.6    Koyasu, S.7    Reinherz, E.L.8
  • 22
    • 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., and R. D. Vale. 2005. Single-molecule microscopy reveals plasma membrane microdomains created by protein-protein networks that exclude or trap signaling molecules in T cells. Cell 121: 937-950.
    • (2005) Cell , vol.121 , pp. 937-950
    • Douglass, A.D.1    Vale, R.D.2
  • 23
    • 0026704425 scopus 로고
    • Overlapping but nonidentical binding sites on CD2 for CD58 and a second ligand CD59
    • Hahn, W. C., E. Menu, A. L. Bothwell, P. J. Sims, and B. E. Bierer. 1992. Overlapping but nonidentical binding sites on CD2 for CD58 and a second ligand CD59. Science 256: 1805-1807.
    • (1992) Science , vol.256 , pp. 1805-1807
    • Hahn, W.C.1    Menu, E.2    Bothwell, A.L.3    Sims, P.J.4    Bierer, B.E.5
  • 25
    • 0027932728 scopus 로고
    • Human cell-adhesion molecule CD2 binds CD58 (LFA-3) with a very low affinity and an extremely fast dissociation rate but does not bind CD48 or CD59
    • van der Merwe, P. A., A. N. Barclay, D. W. Mason, E. A. Davies, B. P. Morgan, M. Tone, A. K. Krishnam, C. Ianelli, and S. J. Davis. 1994. Human cell-adhesion molecule CD2 binds CD58 (LFA-3) with a very low affinity and an extremely fast dissociation rate but does not bind CD48 or CD59. Biochemistry 33: 10149-10160.
    • (1994) Biochemistry , vol.33 , pp. 10149-10160
    • Van Der Merwe, P.A.1    Barclay, A.N.2    Mason, D.W.3    Davies, E.A.4    Morgan, B.P.5    Tone, M.6    Krishnam, A.K.7    Ianelli, C.8    Davis, S.J.9
  • 28
    • 0035957138 scopus 로고    scopus 로고
    • Immunoisolation of TCR signaling complexes from Jurkat T leukemic cells
    • Harder, T., and M. Kuhn. 2001. Immunoisolation of TCR signaling complexes from Jurkat T leukemic cells. Sci. STKE 2001: PL1.
    • (2001) Sci. STKE , vol.2001
    • Harder, T.1    Kuhn, M.2
  • 29
    • 0037370491 scopus 로고    scopus 로고
    • Phosphorylation-dependent regulation of T-cell activation by PAG/Cbp, a lipid raft-associated transmembrane adaptor
    • Davidson, D., M. Bakinowski, M. L. Thomas, V. Horejsi, and A. Veillette. 2003. Phosphorylation-dependent regulation of T-cell activation by PAG/Cbp, a lipid raft-associated transmembrane adaptor. Mol. Cell Biol. 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
  • 30
    • 0033993454 scopus 로고    scopus 로고
    • Cholesterol depletion disrupts lipid rafts and modulates the activity of multiple signaling pathways in T lymphocytes
    • Kabouridis, P. S., J. Janzen, A. L. Magee, and S. C. Ley. 2000. Cholesterol depletion disrupts lipid rafts and modulates the activity of multiple signaling pathways in T lymphocytes. Eur. J. Immunol. 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
  • 32
    • 0029060404 scopus 로고
    • The glycosylphosphatidylinositol-anchored CD59 protein stimulates both T cell receptor ζ/ZAP-70-dependent and -independent signaling pathways in T cells
    • Deckert, M., M. Ticchioni, B. Mari, D. Mary, and A. Bernard. 1995. The glycosylphosphatidylinositol-anchored CD59 protein stimulates both T cell receptor ζ/ZAP-70-dependent and -independent signaling pathways in T cells. Eur. J. Immunol. 25: 1815-1822.
    • (1995) Eur. J. Immunol. , vol.25 , pp. 1815-1822
    • Deckert, M.1    Ticchioni, M.2    Mari, B.3    Mary, D.4    Bernard, A.5
  • 33
    • 0026079656 scopus 로고
    • CD59 functions as a signaltransducing molecule for human T cell activation
    • Korty, P. E., C. Brando, and E. M. Shevach. 1991. CD59 functions as a signaltransducing molecule for human T cell activation. J. Immunol. 146: 4092-4098.
    • (1991) J. Immunol. , vol.146 , pp. 4092-4098
    • Korty, P.E.1    Brando, C.2    Shevach, E.M.3
  • 35
    • 0035039037 scopus 로고    scopus 로고
    • Co-stimulation and counter-stimulation: Lipid raft clustering controls TCR signaling and functional outcomes
    • Miceli, M. C., M. Moran, C. D. Chung, V. P. Patel, T. Low, and W. Zinnanti. 2001. Co-stimulation and counter-stimulation: lipid raft clustering controls TCR signaling and functional outcomes. Semin. Immunol. 13: 115-128.
    • (2001) Semin. Immunol. , vol.13 , pp. 115-128
    • Miceli, M.C.1    Moran, M.2    Chung, C.D.3    Patel, V.P.4    Low, T.5    Zinnanti, W.6


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