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Volumn 3, Issue JUN, 2012, Pages

Lck, membrane microdomains, and TCR triggering machinery: Defining the new rules of engagement

Author keywords

Compartmentalization; Fyn; Heavy and light drms; Lck; Membrane microdomains; Spatio temporal regulation; TCR triggering

Indexed keywords


EID: 84873088843     PISSN: None     EISSN: 16643224     Source Type: Journal    
DOI: 10.3389/fimmu.2012.00155     Document Type: Review
Times cited : (38)

References (160)
  • 1
    • 0026080883 scopus 로고
    • Enhancement of T-cell responsiveness by the lymphocyte-specific tyrosine protein kinase p56lck
    • Abraham, N., Miceli, M. C., Parnes, J. R., and Veillette,A. (1991). Enhancement of T-cell responsiveness by the lymphocyte-specific tyrosine protein kinase p56lck. Nature 350, 62-66.
    • (1991) Nature , vol.350 , pp. 62-66
    • Abraham, N.1    Miceli, M.C.2    Parnes, J.R.3    Veillette, A.4
  • 2
    • 50249105938 scopus 로고    scopus 로고
    • Tailoring T-cell receptor signals by proximal negative feedback mechanisms
    • Acuto, O., di Bartolo, V., and Micheli, F. (2008). Tailoring T-cell receptor signals by proximal negative feedback mechanisms. Nat. Rev. Immunol. 8, 699-712.
    • (2008) Nat. Rev. Immunol. , vol.8 , pp. 699-712
    • Acuto, O.1    di Bartolo, V.2    Micheli, F.3
  • 4
    • 0033199461 scopus 로고    scopus 로고
    • CD45 and Src-family kinases: and now for something completely different
    • Ashwell, J. D., and D'Oro, U. (1999). CD45 and Src-family kinases: and now for something completely different. Immunol. Today 20, 412-416.
    • (1999) Immunol. Today , vol.20 , pp. 412-416
    • Ashwell, J.D.1    D'Oro, U.2
  • 5
    • 84857192210 scopus 로고    scopus 로고
    • A specific type of membrane microdomains is involved in the maintenance and translocation of kinase active Lck to lipid rafts
    • doi:10.1016/j.imlet.2012.01.001
    • Ballek, O., Brouckova, A., Manning, J., and Filipp, D. (2012). A specific type of membrane microdomains is involved in the maintenance and translocation of kinase active Lck to lipid rafts. Immunol. Lett. doi:10.1016/j.imlet.2012.01.001
    • (2012) Immunol. Lett
    • Ballek, O.1    Brouckova, A.2    Manning, J.3    Filipp, D.4
  • 6
    • 79251485975 scopus 로고    scopus 로고
    • The role of L(u)ck in Tcelltriggering
    • Berry, R. (2011). The role of L(u)ck in Tcelltriggering.Sci. Signal. 4, jc2.
    • (2011) Sci. Signal. , vol.4
    • Berry, R.1
  • 7
    • 0028347409 scopus 로고
    • The CD45 tyrosine phosphatase regulates specific pools of antigen receptor-associated p59fyn and CD4-associated p56lck tyrosine in human T-cells
    • Biffen, M., McMichael-Phillips, D., Larson, T., Venkitaraman, A., and Alexander, D. (1994). The CD45 tyrosine phosphatase regulates specific pools of antigen receptor-associated p59fyn and CD4-associated p56lck tyrosine in human T-cells. EMBO J. 13, 1920-1929.
    • (1994) EMBO J , vol.13 , pp. 1920-1929
    • Biffen, M.1    McMichael-Phillips, D.2    Larson, T.3    Venkitaraman, A.4    Alexander, D.5
  • 8
    • 33846626054 scopus 로고    scopus 로고
    • Regulation of T-cell activation by the cytoskeleton
    • Billadeau, D. D., Nolz, J. C., and Gomez, T. S. (2007). Regulation of T-cell activation by the cytoskeleton. Nat. Rev. Immunol. 7, 131-143.
    • (2007) Nat. Rev. Immunol. , vol.7 , pp. 131-143
    • Billadeau, D.D.1    Nolz, J.C.2    Gomez, T.S.3
  • 9
    • 7944223078 scopus 로고    scopus 로고
    • Structure and regulation of Src family kinases
    • Boggon, T. J., and Eck, M. J. (2004). Structure and regulation of Src family kinases. Oncogene 23, 7918-7927.
    • (2004) Oncogene , vol.23 , pp. 7918-7927
    • Boggon, T.J.1    Eck, M.J.2
  • 10
    • 0031561767 scopus 로고    scopus 로고
    • Physical association of CD4 and CD45 in primary, resting CD4+ T cells
    • Bonnard, M., Maroun, C. R., and Julius, M. (1997). Physical association of CD4 and CD45 in primary, resting CD4+ T cells. Cell. Immunol. 175, 1-11.
    • (1997) Cell. Immunol. , vol.175 , pp. 1-11
    • Bonnard, M.1    Maroun, C.R.2    Julius, M.3
  • 11
    • 0342313755 scopus 로고    scopus 로고
    • Angelisova, P., Scherer, J., Shevchenko, A., Hilgert, I., Cerny, J., Drbal, K., Kuramitsu, Y., Kornacker, B., Horejsi, V., and Schraven, B
    • Brdicka, T., Pavlistova, D., Leo, A., Bruyns, E., Korinek, V., Angelisova, P., Scherer, J., Shevchenko, A., Hilgert, I., Cerny, J., Drbal, K., Kuramitsu, Y., Kornacker, B., Horejsi, V., and Schraven, B. (2000). Phosphoprotein associated with glycosphingolipid-enriched microdomains (PAG), a novel ubiquitously expressed transmembrane adaptor protein, binds the protein tyrosine kinase csk and is involved in regulation of T cell activation. J. Exp. Med. 191, 1591-1604.
    • (2000) J. Exp. Med. , vol.191 , pp. 1591-1604
    • Brdicka, T.1    Pavlistova, D.2    Leo, A.3    Bruyns, E.4    Korinek, V.5
  • 13
    • 33845309656 scopus 로고    scopus 로고
    • Lipid rafts, detergent-resistant membranes, and raft targeting signals
    • Brown, D. A. (2006). Lipid rafts, detergent-resistant membranes, and raft targeting signals. Physiology (Bethesda) 21, 430-439.
    • (2006) Physiology (Bethesda) , vol.21 , pp. 430-439
    • Brown, D.A.1
  • 14
    • 38949171464 scopus 로고    scopus 로고
    • Analysis of raft affinity of membrane proteins by detergent-insolubility
    • Brown, D. A. (2007). Analysis of raft affinity of membrane proteins by detergent-insolubility. Methods Mol. Biol. 398, 9-20.
    • (2007) Methods Mol. Biol. , vol.398 , pp. 9-20
    • Brown, D.A.1
  • 15
    • 0026512314 scopus 로고
    • Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface
    • Brown, D. A., and Rose, J. K. (1992). Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface. Cell 68, 533-544.
    • (1992) Cell , vol.68 , pp. 533-544
    • Brown, D.A.1    Rose, J.K.2
  • 16
    • 1542379962 scopus 로고    scopus 로고
    • The membrane domains occupied by glycosylphosphatidylinositolanchored prion protein and Thy-1 differ in lipid composition
    • Brugger, B., Graham, C., Leibrecht, I., Mombelli, E., Jen, A., Wieland, F., and Morris, R. (2004). The membrane domains occupied by glycosylphosphatidylinositolanchored 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
  • 18
    • 80052314133 scopus 로고    scopus 로고
    • Boltzmann energy-based image analysis demonstrates that extracellular domain size differences explain protein segregation at immune synapses
    • doi:10.1371/jour-nal.pcbi.1002076
    • Burroughs, N. J., Kohler, K., Miloserdov, V., Dustin, M. L., van der Merwe, P. A., and Davis, D. M. (2011). Boltzmann energy-based image analysis demonstrates that extracellular domain size differences explain protein segregation at immune synapses. PLoS Comput. Biol. 7, e1002076. doi:10.1371/journal.pcbi.1002076
    • (2011) PLoS Comput. Biol. , vol.7
    • Burroughs, N.J.1    Kohler, K.2    Miloserdov, V.3    Dustin, M.L.4    van der Merwe, P.A.5    Davis, D.M.6
  • 19
    • 77951217914 scopus 로고    scopus 로고
    • Dynamic regulation of CD45 lateral mobility by the spectrin-ankyrin cytoskeleton of T cells
    • Cairo, C. W., Das, R., Albohy, A., Baca, Q. J., Pradhan, D., Morrow, J. S., Coombs,D.,and Golan,D. E. (2010). Dynamic regulation of CD45 lateral mobility by the spectrin-ankyrin cytoskeleton of T cells. J. Biol. Chem. 285, 11392-11401.
    • (2010) J. Biol. Chem. , vol.285 , pp. 11392-11401
    • Cairo, C.W.1    Das, R.2    Albohy, A.3    Baca, Q.J.4    Pradhan, D.5    Morrow, J.S.6    Coombs, D.7    Golan, D.E.8
  • 20
    • 0037184955 scopus 로고    scopus 로고
    • The organizing principle in the formation of the T cell receptor-CD3 complex
    • Call, M. E., Pyrdol, J., Wiedmann, M., and Wucherpfennig, K. W. (2002). The organizing principle in the formation of the T cell receptor-CD3 complex. Cell 111, 967-979.
    • (2002) Cell , vol.111 , pp. 967-979
    • Call, M.E.1    Pyrdol, J.2    Wiedmann, M.3    Wucherpfennig, K.W.4
  • 21
    • 72949108077 scopus 로고    scopus 로고
    • Pairing computation with experimentation: a powerful coupling for understanding T cell signalling
    • Chakraborty, A. K., and Das, J. (2010). Pairing computation with experimentation: a powerful coupling for understanding T cell signalling. Nat. Rev. Immunol. 10, 59-71.
    • (2010) Nat. Rev. Immunol. , vol.10 , pp. 59-71
    • Chakraborty, A.K.1    Das, J.2
  • 22
    • 0000110483 scopus 로고    scopus 로고
    • Dissociation of intracellular signaling pathways in response to partial agonist ligands of theTcellreceptor
    • Chau, L. A., Bluestone, J. A., and Madrenas, J. (1998). Dissociation of intracellular signaling pathways in response to partial agonist ligands of theTcellreceptor.J. Exp. Med. 187, 1699-1709.
    • (1998) J. Exp. Med. , vol.187 , pp. 1699-1709
    • Chau, L.A.1    Bluestone, J.A.2    Madrenas, J.3
  • 23
    • 0033566749 scopus 로고    scopus 로고
    • Phospho-LAT-independent activation of the ras-mitogenactivated protein kinase pathway: a differential recruitment model of TCR partial agonist signaling
    • Chau, L. A., and Madrenas, J. (1999). Phospho-LAT-independent activation of the ras-mitogenactivated protein kinase pathway: a differential recruitment model of TCR partial agonist signaling. J. Immunol. 163, 1853-1858.
    • (1999) J. Immunol. , vol.163 , pp. 1853-1858
    • Chau, L.A.1    Madrenas, J.2
  • 24
    • 58249092344 scopus 로고    scopus 로고
    • Isolation at physiological temperature of detergentresistant membranes with properties expected of lipid rafts: the influence of buffer composition
    • Chen, X., Jen, A., Warley, A., Lawrence, M. J., Quinn, P. J., and Morris, R. J. (2009). Isolation at physiological temperature of detergentresistant membranes with properties expected of lipid rafts: the influence of buffer composition. Biochem. J. 417, 525-533.
    • (2009) Biochem. J. , vol.417 , pp. 525-533
    • Chen, X.1    Jen, A.2    Warley, A.3    Lawrence, M.J.4    Quinn, P.J.5    Morris, R.J.6
  • 25
    • 33846491349 scopus 로고    scopus 로고
    • The isolation and structure of membrane lipid rafts from rat brain
    • Chen, X., Morris, R., Lawrence, M. J., and Quinn, P. J. (2007). The isolation and structure of membrane lipid rafts from rat brain. Biochimie 89, 192-196.
    • (2007) Biochimie , vol.89 , pp. 192-196
    • Chen, X.1    Morris, R.2    Lawrence, M.J.3    Quinn, P.J.4
  • 26
    • 0035933771 scopus 로고    scopus 로고
    • Specific dephosphorylation of the Lck tyrosine protein kinase at Tyr394 by the SHP-1 protein-tyrosine phosphatase
    • Chiang, G. G., and Sefton, B. M. (2001). Specific dephosphorylation of the Lck tyrosine protein kinase at Tyr394 by the SHP-1 protein-tyrosine phosphatase. J. Biol. Chem. 276, 23173-23178.
    • (2001) J. Biol. Chem. , vol.276 , pp. 23173-23178
    • Chiang, G.G.1    Sefton, B.M.2
  • 27
    • 77951991606 scopus 로고    scopus 로고
    • T cell signal regulation by the actin cytoskeleton
    • Chichili, G. R., Westmuckett, A. D., and Rodgers, W. (2010). T cell signal regulation by the actin cytoskeleton. J. Biol. Chem. 285, 14737-14746.
    • (2010) J. Biol. Chem. , vol.285 , pp. 14737-14746
    • Chichili, G.R.1    Westmuckett, A.D.2    Rodgers, W.3
  • 28
    • 34447286463 scopus 로고    scopus 로고
    • Molecular mechanisms involved in T cell receptor triggering
    • Choudhuri, K., and van der Merwe, P. A. (2007). Molecular mechanisms involved in T cell receptor triggering. Semin. Immunol. 19, 255-261.
    • (2007) Semin. Immunol. , vol.19 , pp. 255-261
    • Choudhuri, K.1    van der Merwe, P.A.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., Bakinowski, M., Thomas, M. L., Horejsi, V., and Veillette, A. (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
    • 33847208485 scopus 로고    scopus 로고
    • PAG-associated FynT regulates calcium signaling and promotes anergy in T lymphocytes
    • Davidson, D., Schraven, B., andVeillette, A. (2007). PAG-associated FynT regulates calcium signaling and promotes anergy in T lymphocytes. Mol. Cell. Biol. 27, 1960-1973.
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 1960-1973
    • Davidson, D.1    Schraven, B.2    Veillette, A.3
  • 31
    • 68849090313 scopus 로고    scopus 로고
    • Mechanisms and functions for the duration of intercellular contacts made by lymphocytes
    • Davis, D. M. (2009). Mechanisms and functions for the duration of intercellular contacts made by lymphocytes. Nat. Rev. Immunol. 9,543-555.
    • (2009) Nat. Rev. Immunol. , vol.9 , pp. 543-555
    • Davis, D.M.1
  • 32
    • 2342566929 scopus 로고    scopus 로고
    • What is the importance of the immunological synapse
    • Davis, D. M., and Dustin, M. L. (2004). What is the importance of the immunological synapse Trends Immunol. 25, 323-327
    • (2004) Trends Immunol , vol.25 , pp. 323-327
    • Davis, D.M.1    Dustin, M.L.2
  • 33
    • 33746114879 scopus 로고    scopus 로고
    • The kinetic-segregation model: TCR triggering and beyond
    • Davis, S. J., and van der Merwe, P. A. (2006). The kinetic-segregation model: TCR triggering and beyond. Nat. Immunol. 7, 803-809.
    • (2006) Nat. Immunol. , vol.7 , pp. 803-809
    • Davis, S.J.1    van der Merwe, P.A.2
  • 34
    • 78650719213 scopus 로고    scopus 로고
    • Lck and the nature of the T cell receptor trigger
    • Davis, S. J., and van der Merwe, P. A. (2011). Lck and the nature of the T cell receptor trigger. Trends Immunol. 32, 1-5.
    • (2011) Trends Immunol , vol.32 , pp. 1-5
    • Davis, S.J.1    van der Merwe, P.A.2
  • 35
    • 0033965050 scopus 로고    scopus 로고
    • Differential T-cell antigen receptor signaling mediated by the Src family kinases Lck and Fyn
    • Denny, M. F., Patai, B., and Straus, D. B. (2000). Differential T-cell antigen receptor signaling mediated by the Src family kinases Lck and Fyn. Mol. Cell. Biol. 20, 1426-1435.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 1426-1435
    • Denny, M.F.1    Patai, B.2    Straus, D.B.3
  • 36
    • 27944447718 scopus 로고    scopus 로고
    • The ubiquitously expressed Csk adaptor protein Cbp is dispensable for embryogenesis and Tcell development and function
    • Dobenecker, M. W., Schmedt, C., Okada, M., and Tarakhovsky, A. (2005). The ubiquitously expressed Csk adaptor protein Cbp is dispensable for embryogenesis and Tcell development and function. Mol. Cell. Biol. 25, 10533-10542.
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 10533-10542
    • Dobenecker, M.W.1    Schmedt, C.2    Okada, M.3    Tarakhovsky, A.4
  • 37
    • 0033558102 scopus 로고    scopus 로고
    • Cutting edge: the CD45 tyrosine phosphatase is an inhibitor of Lck activity in thymocytes
    • D'Oro, U., and Ashwell, J. D. (1999). Cutting edge: the CD45 tyrosine phosphatase is an inhibitor of Lck activity in thymocytes. J. Immunol. 162, 1879-1883.
    • (1999) J. Immunol. , vol.162 , pp. 1879-1883
    • D'Oro, U.1    Ashwell, J.D.2
  • 38
    • 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
  • 40
    • 0037959071 scopus 로고    scopus 로고
    • The state of lipid rafts: from model membranes to cells
    • Edidin, M. (2003). The state of lipid rafts: from model membranes to cells. Annu. Rev. Biophys. Biomol. Struct. 32, 257-283.
    • (2003) Annu. Rev. Biophys. Biomol. Struct. , vol.32 , pp. 257-283
    • Edidin, M.1
  • 41
    • 0036839104 scopus 로고    scopus 로고
    • Dynamic association of CD45 with detergent-insoluble microdomains in T lymphocytes
    • Edmonds, S. D., and Ostergaard, H. L. (2002). Dynamic association of CD45 with detergent-insoluble microdomains in T lymphocytes. J. Immunol. 169, 5036-5042.
    • (2002) J. Immunol. , vol.169 , pp. 5036-5042
    • Edmonds, S.D.1    Ostergaard, H.L.2
  • 43
    • 3042609934 scopus 로고    scopus 로고
    • Lipid rafts: resolution of the "fyn problem" Mol
    • Filipp, D., and Julius, M. (2004). Lipid rafts: resolution of the "fyn problem" Mol. Immunol. 41, 645-656.
    • (2004) Immunol , vol.41 , pp. 645-656
    • Filipp, D.1    Julius, M.2
  • 44
    • 1642282774 scopus 로고    scopus 로고
    • Enrichment of lck in lipid rafts regulates colocalized fyn activation and the initiation of proximal signals through TCR alpha beta
    • Filipp, D., Leung, B. L., Zhang, J., Veillette, A., and Julius, M. (2004). Enrichment of lck in lipid rafts regulates colocalized fyn activation and the initiation of proximal signals through TCR alpha beta. J. Immunol. 172, 4266-4274.
    • (2004) J. Immunol. , vol.172 , pp. 4266-4274
    • Filipp, D.1    Leung, B.L.2    Zhang, J.3    Veillette, A.4    Julius, M.5
  • 47
    • 21844440052 scopus 로고    scopus 로고
    • Tuning immune responses: diversity and adaptation of the immunological synapse
    • Friedl, P., den Boer, A. T., and Gunzer, M. (2005). Tuning immune responses: diversity and adaptation of the immunological synapse. Nat. Rev. Immunol. 5, 532-545.
    • (2005) Nat. Rev. Immunol. , vol.5 , pp. 532-545
    • Friedl, P.1    den Boer, A.T.2    Gunzer, M.3
  • 48
  • 49
    • 38949168914 scopus 로고    scopus 로고
    • Visualization of detergent solubilization of membranes: implications for the isolation of rafts
    • Garner, A. E., Smith, D. A., and Hooper, N. M. (2008). Visualization of detergent solubilization of membranes: implications for the isolation of rafts. Biophys. J. 94, 1326-1340.
    • (2008) Biophys. J. , vol.94 , pp. 1326-1340
    • Garner, A.E.1    Smith, D.A.2    Hooper, N.M.3
  • 52
    • 0034737616 scopus 로고    scopus 로고
    • Cross-linking of CD4 induces cytoskeletal association of CD4 and p56lck
    • Ha-Lee, Y. M., Lee, Y., Kim, Y. K., and Sohn, J. (2000). Cross-linking of CD4 induces cytoskeletal association of CD4 and p56lck. Exp. Mol. Med. 32, 18-22.
    • (2000) Exp. Mol. Med. , vol.32 , pp. 18-22
    • Ha-Lee, Y.M.1    Lee, Y.2    Kim, Y.K.3    Sohn, J.4
  • 53
    • 0030761189 scopus 로고    scopus 로고
    • The activated form of the Lck tyrosine protein kinase in cells exposed to hydrogen peroxide is phosphorylated at both Tyr-394 and Tyr-505
    • Hardwick,J. S.,and Sefton,B. M. (1997). The activated form of the Lck tyrosine protein kinase in cells exposed to hydrogen peroxide is phosphorylated at both Tyr-394 and Tyr-505. J. Biol. Chem. 272, 25429-25432.
    • (1997) J. Biol. Chem. , vol.272 , pp. 25429-25432
    • Hardwick, J.S.1    Sefton, B.M.2
  • 54
    • 84863860582 scopus 로고    scopus 로고
    • The cytoskeleton coordinates the early events of B-cell activation
    • Harwood, N. E., and Batista, F. D. (2011). The cytoskeleton coordinates the early events of B-cell activation. Cold Spring Harb. Perspect. Biol. 3, a002360.
    • (2011) Cold Spring Harb. Perspect. Biol. , vol.3
    • Harwood, N.E.1    Batista, F.D.2
  • 55
    • 0030998039 scopus 로고    scopus 로고
    • Physical modulation of intracellular signaling processes by locational regulation
    • Haugh, J. M., and Lauffenburger, D. A. (1997). Physical modulation of intracellular signaling processes by locational regulation. Biophys. J. 72, 2014-2031.
    • (1997) Biophys. J. , vol.72 , pp. 2014-2031
    • Haugh, J.M.1    Lauffenburger, D.A.2
  • 56
    • 0026647524 scopus 로고
    • Association of tyrosine kinase p56lck with CD4 inhibits the induction of growth through the alpha beta T-cell receptor
    • Haughn, L., Gratton, S., Caron, L., Sekaly, R. P., Veillette, A., and Julius, M. (1992). Association of tyrosine kinase p56lck with CD4 inhibits the induction of growth through the alpha beta T-cell receptor. Nature 358, 328-331.
    • (1992) Nature , vol.358 , pp. 328-331
    • Haughn, L.1    Gratton, S.2    Caron, L.3    Sekaly, R.P.4    Veillette, A.5    Julius, M.6
  • 57
    • 0032476736 scopus 로고    scopus 로고
    • Interleukin 2mediated uncoupling of T cell receptor alpha/beta from CD3 signaling
    • Haughn, L., Leung, B., Boise, L., Veillette, A., Thompson, C., and Julius, M. (1998). Interleukin 2mediated uncoupling of T cell receptor alpha/beta from CD3 signaling. J. Exp. Med. 188, 1575-1586.
    • (1998) J. Exp. Med. , vol.188 , pp. 1575-1586
    • Haughn, L.1    Leung, B.2    Boise, L.3    Veillette, A.4    Thompson, C.5    Julius, M.6
  • 58
    • 0345222470 scopus 로고    scopus 로고
    • Contribution of kinases and the CD45 phosphatase to the generation of tyrosine phosphorylation patterns in the T-cell receptor complex zeta chain
    • Hegedus, Z., Chitu, V., Toth, G. K., Finta, C., Varadi, G., Ando, I., and Monostori, E. (1999). Contribution of kinases and the CD45 phosphatase to the generation of tyrosine phosphorylation patterns in the T-cell receptor complex zeta chain. Immunol. Lett. 67, 31-39.
    • (1999) Immunol. Lett. , vol.67 , pp. 31-39
    • Hegedus, Z.1    Chitu, V.2    Toth, G.K.3    Finta, C.4    Varadi, G.5    Ando, I.6    Monostori, E.7
  • 59
    • 0038815306 scopus 로고    scopus 로고
    • CD45: a critical regulator of signaling thresholds in immune cells
    • Hermiston, M. L., Xu, Z., and Weiss, A. (2003). CD45: a critical regulator of signaling thresholds in immune cells. Annu. Rev. Immunol. 21, 107-137.
    • (2003) Annu. Rev. Immunol. , vol.21 , pp. 107-137
    • Hermiston, M.L.1    Xu, Z.2    Weiss, A.3
  • 60
    • 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
  • 62
    • 0027410485 scopus 로고
    • Differential effects of expression of the CD45 tyrosine protein phosphatase on the tyrosine phosphorylation of the lck, fyn, and c-src tyrosine protein kinases
    • Hurley, T. R., Hyman, R., and Sefton, B. M. (1993). Differential effects of expression of the CD45 tyrosine protein phosphatase on the tyrosine phosphorylation of the lck, fyn, and c-src tyrosine protein kinases. Mol. Cell. Biol. 13, 1651-1656.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 1651-1656
    • Hurley, T.R.1    Hyman, R.2    Sefton, B.M.3
  • 63
    • 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, T. R., van der Merwe, P. A., and Acuto, O. (2003). CD45 ectodomain controls interaction with GEMs and Lck activity for optimal TCR signaling. Nat. Immunol. 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
  • 64
    • 0037167816 scopus 로고    scopus 로고
    • Direct observation of ligand recognition by T cells
    • Irvine, D. J., Purbhoo, M. A., Krogsgaard, M., and Davis, M. M. (2002). Direct observation of ligand recognition by T cells. Nature 419, 845-849.
    • (2002) Nature , vol.419 , pp. 845-849
    • Irvine, D.J.1    Purbhoo, M.A.2    Krogsgaard, M.3    Davis, M.M.4
  • 66
    • 33645295218 scopus 로고    scopus 로고
    • Lipid rafts in T cell receptor signalling
    • Kabouridis, P. S. (2006). Lipid rafts in T cell receptor signalling. Mol. Membr. Biol. 23, 49-57.
    • (2006) Mol. Membr. Biol. , vol.23 , pp. 49-57
    • Kabouridis, P.S.1
  • 67
    • 0030746106 scopus 로고    scopus 로고
    • S-acylation of LCK protein tyrosine kinase is essential for its signalling function in T lymphocytes
    • Kabouridis, P. S., Magee, A. I., and Ley, S. C. (1997). S-acylation of LCK protein tyrosine kinase is essential for its signalling function in T lymphocytes. EMBO J. 16, 4983-4998.
    • (1997) EMBO J , vol.16 , pp. 4983-4998
    • Kabouridis, P.S.1    Magee, A.I.2    Ley, S.C.3
  • 69
    • 84869428183 scopus 로고    scopus 로고
    • Analysis of detergent-free lipid rafts isolated from a CD4+ T cell line: Interaction with antigen presenting cells promotes coalescing of lipid rafts
    • Kennedy, C., Nelson, M. D., and Bamezai, A. K. (2011). Analysis of detergent-free lipid rafts isolated from a CD4+ T cell line: Interaction with antigen presenting cells promotes coalescing of lipid rafts. Cell Commun. Signal. 9, 31.
    • (2011) Cell Commun. Signal. , vol.9 , pp. 31
    • Kennedy, C.1    Nelson, M.D.2    Bamezai, A.K.3
  • 70
    • 0032563231 scopus 로고    scopus 로고
    • Fidelity of T cell activation through multistep T cell receptor zeta phosphorylation
    • Kersh, E. N., Shaw,A. S., and Allen, P. M. (1998). Fidelity of T cell activation through multistep T cell receptor zeta phosphorylation. Science 281, 572-575.
    • (1998) Science , vol.281 , pp. 572-575
    • Kersh, E.N.1    Shaw, A.S.2    Allen, P.M.3
  • 71
    • 67649922863 scopus 로고    scopus 로고
    • Endocytosis of MHC molecules by distinct membrane rafts
    • Knorr, R., Karacsonyi, C., and Lindner, R. (2009). Endocytosis of MHC molecules by distinct membrane rafts. J. Cell. Sci. 122, 1584-1594.
    • (2009) J. Cell. Sci. , vol.122 , pp. 1584-1594
    • Knorr, R.1    Karacsonyi, C.2    Lindner, R.3
  • 72
    • 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., and Hamaoka, T. (2001). Involvement of SHP-1 tyrosine phosphatase in TCR-mediated signaling pathways in lipid rafts. Immunity 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
  • 73
    • 11144267107 scopus 로고    scopus 로고
    • Comparative lipid analysis and structure of detergent-resistant membrane raft fractions isolated from human and ruminant erythrocytes
    • Koumanov, K. S., Tessier, C., Momchilova, A. B., Rainteau, D., Wolf, C., and Quinn, P. J. (2005). Comparative lipid analysis and structure of detergent-resistant membrane raft fractions isolated from human and ruminant erythrocytes. Arch. Biochem. Biophys. 434, 150-158.
    • (2005) Arch. Biochem. Biophys. , vol.434 , pp. 150-158
    • Koumanov, K.S.1    Tessier, C.2    Momchilova, A.B.3    Rainteau, D.4    Wolf, C.5    Quinn, P.J.6
  • 75
    • 55449093482 scopus 로고    scopus 로고
    • The safety on the TCR trigger
    • Kuhns, M. S., and Davis, M. M. (2008). The safety on the TCR trigger. Cell 135, 594-596.
    • (2008) Cell , vol.135 , pp. 594-596
    • Kuhns, M.S.1    Davis, M.M.2
  • 76
    • 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., and Fujiwara, T. (2005). Single-molecule tracking of membrane molecules: plasma membrane compartmentalization and dynamic assembly of raft-philic signaling molecules. Semin. Immunol. 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
  • 78
    • 0035367576 scopus 로고    scopus 로고
    • Proximal protein tyrosine kinases in immunoreceptor signaling
    • Latour, S., and Veillette, A. (2001). Proximal protein tyrosine kinases in immunoreceptor signaling. Curr. Opin. Immunol. 13, 299-306.
    • (2001) Curr. Opin. Immunol. , vol.13 , pp. 299-306
    • Latour, S.1    Veillette, A.2
  • 80
    • 22744437388 scopus 로고    scopus 로고
    • Detergent-resistant membranes should not be identified with membrane rafts
    • Lichtenberg, D., Goni, F. M., and Heerklotz, H. (2005). Detergent-resistant membranes should not be identified with membrane rafts. Trends Biochem. Sci. 30, 430-436.
    • (2005) Trends Biochem. Sci. , vol.30 , pp. 430-436
    • Lichtenberg, D.1    Goni, F.M.2    Heerklotz, H.3
  • 81
    • 77951282449 scopus 로고    scopus 로고
    • Rafting trips into the cell
    • Lindner, R., and Knorr, R. (2009). Rafting trips into the cell. Commun. Integr. Biol. 2, 420-421.
    • (2009) Commun. Integr. Biol. , vol.2 , pp. 420-421
    • Lindner, R.1    Knorr, R.2
  • 82
    • 70349469585 scopus 로고    scopus 로고
    • Domains in biological membranes
    • Lindner, R., and Naim, H. Y. (2009). Domains in biological membranes. Exp. Cell Res. 315, 2871-2878.
    • (2009) Exp. Cell Res. , vol.315 , pp. 2871-2878
    • Lindner, R.1    Naim, H.Y.2
  • 83
    • 38449114971 scopus 로고    scopus 로고
    • Detergent resistance as a tool in membrane research
    • Lingwood, D., and Simons, K. (2007). Detergent resistance as a tool in membrane research. Nat. Protoc. 2, 2159-2165.
    • (2007) Nat. Protoc. , vol.2 , pp. 2159-2165
    • Lingwood, D.1    Simons, K.2
  • 84
    • 74849118341 scopus 로고    scopus 로고
    • Lipid rafts as a membraneorganizing principle
    • Lingwood, D., and Simons, K. (2010). Lipid rafts as a membraneorganizing principle. Science 327, 46-50.
    • (2010) Science , vol.327 , pp. 46-50
    • Lingwood, D.1    Simons, K.2
  • 85
    • 0024166623 scopus 로고
    • p56lck protein-tyrosine kinase is cytoskeletal and does not bind to polyomavirus middle T antigen
    • Louie, R. R., King, C. S., MacAuley, A., Marth, J. D., Perlmutter, R. M., Eckhart, W., and Cooper, J. A. (1988). p56lck protein-tyrosine kinase is cytoskeletal and does not bind to polyomavirus middle T antigen. J. Virol. 62, 4673-4679.
    • (1988) J. Virol. , vol.62 , pp. 4673-4679
    • Louie, R.R.1    King, C.S.2    MacAuley, A.3    Marth, J.D.4    Perlmutter, R.M.5    Eckhart, W.6    Cooper, J.A.7
  • 86
    • 0025194043 scopus 로고
    • Analysis of the sites in p56lck whose phosphorylation is induced by tetradecanoyl phorbol acetate
    • Luo, K. X., and Sefton, B. M. (1990). Analysis of the sites in p56lck whose phosphorylation is induced by tetradecanoyl phorbol acetate. Oncogene 5, 803-808.
    • (1990) Oncogene , vol.5 , pp. 803-808
    • Luo, K.X.1    Sefton, B.M.2
  • 87
    • 0033573083 scopus 로고    scopus 로고
    • Functionally different GPI proteins are organized in different domains on the neuronal surface
    • Madore, N., Smith, K. L., Graham, C. H., Jen, A., Brady, K., Hall, S., and Morris, R. (1999). Functionally different GPI proteins are organized in different domains on the neuronal surface. EMBO J. 18, 6917-6926.
    • (1999) EMBO J , vol.18 , pp. 6917-6926
    • Madore, N.1    Smith, K.L.2    Graham, C.H.3    Jen, A.4    Brady, K.5    Hall, S.6    Morris, R.7
  • 88
    • 29144480861 scopus 로고    scopus 로고
    • Protein tyrosine phosphatase alpha regulates Fyn activity and Cbp/PAG phosphorylation in thymocyte lipid rafts
    • Maksumova, L., Le, H. T., Muratkhodjaev, F., Davidson, D., Veillette, A., and Pallen,C. J. (2005). Protein tyrosine phosphatase alpha regulates Fyn activity and Cbp/PAG phosphorylation in thymocyte lipid rafts. J. Immunol. 175, 7947-7956.
    • (2005) J. Immunol. , vol.175 , pp. 7947-7956
    • Maksumova, L.1    Le, H.T.2    Muratkhodjaev, F.3    Davidson, D.4    Veillette, A.5    Pallen, C.J.6
  • 89
    • 33645288264 scopus 로고    scopus 로고
    • Lipid rafts in lymphocyte activation and migration
    • Manes, S., and Viola, A. (2006). Lipid rafts in lymphocyte activation and migration. Mol. Membr. Biol. 23, 59-69.
    • (2006) Mol. Membr. Biol. , vol.23 , pp. 59-69
    • Manes, S.1    Viola, A.2
  • 90
    • 0035469893 scopus 로고    scopus 로고
    • Role for lipid rafts in regulating interleukin-2 receptor signaling
    • Marmor, M. D., and Julius, M. (2001). Role for lipid rafts in regulating interleukin-2 receptor signaling. Blood 98, 1489-1497.
    • (2001) Blood , vol.98 , pp. 1489-1497
    • Marmor, M.D.1    Julius, M.2
  • 91
    • 0028281225 scopus 로고
    • Distinct roles for CD4 and CD8 as co-receptors in T cell receptor signalling
    • Maroun, C. R., and Julius, M. (1994). Distinct roles for CD4 and CD8 as co-receptors in T cell receptor signalling. Eur. J. Immunol. 24, 959-966.
    • (1994) Eur. J. Immunol. , vol.24 , pp. 959-966
    • Maroun, C.R.1    Julius, M.2
  • 92
    • 33645384693 scopus 로고    scopus 로고
    • Essential role of the T cellspecific adapter protein in the activation of LCK in peripheral T cells
    • Marti, F., Garcia, G. G., Lapinski, P. E., MacGregor, J. N., and King, P. D. (2006). Essential role of the T cellspecific adapter protein in the activation of LCK in peripheral T cells. J. Exp. Med. 203, 281-287.
    • (2006) J. Exp. Med. , vol.203 , pp. 281-287
    • Marti, F.1    Garcia, G.G.2    Lapinski, P.E.3    MacGregor, J.N.4    King, P.D.5
  • 93
    • 0031149691 scopus 로고    scopus 로고
    • Signal transduction: clamping down on Src activity
    • Mayer, B. J. (1997). Signal transduction: clamping down on Src activity. Curr. Biol. 7, R295-R298.
    • (1997) Curr. Biol. , vol.7
    • Mayer, B.J.1
  • 95
    • 4444336426 scopus 로고    scopus 로고
    • In silico activation of Src tyrosine kinase reveals the molecular basis for intramolecular autophosphorylation
    • Mendieta, J., and Gago, F. (2004). In silico activation of Src tyrosine kinase reveals the molecular basis for intramolecular autophosphorylation. J. Mol. Graph. Model. 23, 189-198.
    • (2004) J. Mol. Graph. Model. , vol.23 , pp. 189-198
    • Mendieta, J.1    Gago, F.2
  • 96
    • 34548809782 scopus 로고    scopus 로고
    • Hypophosphorylated TCR/CD3zeta signals through a Grb2-SOS1-Ras pathway in Lck knockdown cells
    • Methi, T., Ngai, J., Vang, T., Torgersen, K. M., and Tasken, K. (2007). Hypophosphorylated TCR/CD3zeta signals through a Grb2-SOS1-Ras pathway in Lck knockdown cells. Eur. J. Immunol. 37, 2539-2548.
    • (2007) Eur. J. Immunol. , vol.37 , pp. 2539-2548
    • Methi, T.1    Ngai, J.2    Vang, T.3    Torgersen, K.M.4    Tasken, K.5
  • 97
    • 0000484021 scopus 로고
    • Clonal analysis of human cytotoxic T lymphocytes: T4+ and T8+ effector T cells recognize products of different major histocompatibility complex regions
    • Meuer, S. C., Schlossman, S. F., and Reinherz, E. L. (1982). Clonal analysis of human cytotoxic T lymphocytes: T4+ and T8+ effector T cells recognize products of different major histocompatibility complex regions. Proc. Natl. Acad. Sci. U.S.A. 79, 4395-4399.
    • (1982) Proc. Natl. Acad. Sci. U. S. A. , vol.79 , pp. 4395-4399
    • Meuer, S.C.1    Schlossman, S.F.2    Reinherz, E.L.3
  • 98
    • 33846224785 scopus 로고    scopus 로고
    • Full activation of the T cell receptor requires both clustering and conformational changes at CD3
    • Minguet, S., Swamy, M., Alarcon, B., Luescher, I. F., and Schamel, W. W. (2007). Full activation of the T cell receptor requires both clustering and conformational changes at CD3. Immunity 26, 43-54.
    • (2007) Immunity , vol.26 , pp. 43-54
    • Minguet, S.1    Swamy, M.2    Alarcon, B.3    Luescher, I.F.4    Schamel, W.W.5
  • 101
    • 0000072679 scopus 로고
    • Rapid activation of the T-cell tyrosine protein kinase pp56lck by the CD45 phosphotyrosine phosphatase
    • Mustelin, T., Coggeshall, K. M., and Altman, A. (1989). Rapid activation of the T-cell tyrosine protein kinase pp56lck by the CD45 phosphotyrosine phosphatase. Proc. Natl. Acad. Sci. U.S.A. 86, 6302-6306.
    • (1989) Proc. Natl. Acad. Sci. U. S. A. , vol.86 , pp. 6302-6306
    • Mustelin, T.1    Coggeshall, K.M.2    Altman, A.3
  • 103
    • 0037392883 scopus 로고    scopus 로고
    • Positive and negative regulation of T-cell activation through kinases and phosphatases
    • Mustelin, T., and Tasken, K. (2003). Positive and negative regulation of T-cell activation through kinases and phosphatases. Biochem. J. 371, 15-27.
    • (2003) Biochem. J. , vol.371 , pp. 15-27
    • Mustelin, T.1    Tasken, K.2
  • 105
    • 13644253773 scopus 로고    scopus 로고
    • Structural basis for the function and regulation of the receptor protein tyrosine phosphatase CD45
    • Nam, H. J., Poy, F., Saito, H., and Frederick, C. A. (2005). Structural basis for the function and regulation of the receptor protein tyrosine phosphatase CD45. J. Exp. Med. 201, 441-452.
    • (2005) J. Exp. Med. , vol.201 , pp. 441-452
    • Nam, H.J.1    Poy, F.2    Saito, H.3    Frederick, C.A.4
  • 106
    • 0036247432 scopus 로고    scopus 로고
    • T-cell activation through the antigen receptor Part 1 signaling components, signaling pathways, and signal integration at the T-cell antigen receptor synapse
    • Nel, A. E. (2002). T-cell activation through the antigen receptor. Part 1: signaling components, signaling pathways, and signal integration at the T-cell antigen receptor synapse. J. Allergy Clin. Immunol. 109, 758-770.
    • (2002) J. Allergy Clin. Immunol. , vol.109 , pp. 758-770
    • Nel, A.E.1
  • 108
    • 37249068430 scopus 로고    scopus 로고
    • A weak Lck tail bite is necessary for Lck function in T cell antigen receptor signaling
    • Nika, K., Tautz, L., Arimura, Y., Vang, T., Williams, S., and Mustelin, T. (2007). A weak Lck tail bite is necessary for Lck function in T cell antigen receptor signaling. J. Biol. Chem. 282, 36000-36009.
    • (2007) J. Biol. Chem. , vol.282 , pp. 36000-36009
    • Nika, K.1    Tautz, L.2    Arimura, Y.3    Vang, T.4    Williams, S.5    Mustelin, T.6
  • 110
    • 77951643625 scopus 로고    scopus 로고
    • A new type of membrane raft-like microdomains and their possible involvement in TCR signaling
    • Otahal, P., Angelisova, P., Hrdinka, M., Brdicka, T., Novak, P., Drbal, K., and Horejsi, V. (2010). A new type of membrane raft-like microdomains and their possible involvement in TCR signaling. J. Immunol. 184, 3689-3696.
    • (2010) J. Immunol. , vol.184 , pp. 3689-3696
    • Otahal, P.1    Angelisova, P.2    Hrdinka, M.3    Brdicka, T.4    Novak, P.5    Drbal, K.6    Horejsi, V.7
  • 112
    • 7944231534 scopus 로고    scopus 로고
    • Function of the Src-family kinases, Lck and Fyn, in T-cell development and activation
    • Palacios, E. H., and Weiss, A. (2004). Function of the Src-family kinases, Lck and Fyn, in T-cell development and activation. Oncogene 23, 7990-8000.
    • (2004) Oncogene , vol.23 , pp. 7990-8000
    • Palacios, E.H.1    Weiss, A.2
  • 113
    • 61449170053 scopus 로고    scopus 로고
    • Genetically encoded Forster resonance energy transfer sensors for the conformation of the Src family kinase Lck
    • Paster, W., Paar, C., Eckerstorfer, P., Jakober, A., Drbal, K., Schutz, G. J., Sonnleitner, A., and Stockinger, H. (2009). Genetically encoded Forster resonance energy transfer sensors for the conformation of the Src family kinase Lck. J. Immunol. 182, 2160-2167.
    • (2009) J. Immunol. , vol.182 , pp. 2160-2167
    • Paster, W.1    Paar, C.2    Eckerstorfer, P.3    Jakober, A.4    Drbal, K.5    Schutz, G.J.6    Sonnleitner, A.7    Stockinger, H.8
  • 115
    • 77956394811 scopus 로고    scopus 로고
    • A lipid matrix model of membrane raft structure
    • Quinn,P. J. (2010). A lipid matrix model of membrane raft structure. Prog. Lipid Res. 49, 390-406.
    • (2010) Prog. Lipid Res. , vol.49 , pp. 390-406
    • Quinn, P.J.1
  • 116
    • 2642586455 scopus 로고    scopus 로고
    • Isolation and characterization of lipid rafts with different properties from RBL-2H3 (rat basophilic leukaemia) cells
    • Radeva, G., and Sharom, F. J. (2004). Isolation and characterization of lipid rafts with different properties from RBL-2H3 (rat basophilic leukaemia) cells. Biochem. J. 380, 219-230.
    • (2004) Biochem. J. , vol.380 , pp. 219-230
    • Radeva, G.1    Sharom, F.J.2
  • 117
    • 34247590130 scopus 로고    scopus 로고
    • Palmitoylation of ligands, receptors, and intracellular signaling molecules
    • Resh, M. D. (2006). Palmitoylation of ligands, receptors, and intracellular signaling molecules. Sci. STKE 2006, re14.
    • (2006) Sci. STKE , vol.2006
    • Resh, M.D.1
  • 118
    • 12744262695 scopus 로고    scopus 로고
    • Merging complexes: properties of membrane raft assembly during lymphocyte signaling
    • Rodgers, W., Farris, D., and Mishra, S. (2005). Merging complexes: properties of membrane raft assembly during lymphocyte signaling. Trends Immunol. 26, 97-103.
    • (2005) Trends Immunol , vol.26 , pp. 97-103
    • Rodgers, W.1    Farris, D.2    Mishra, S.3
  • 119
    • 4344663113 scopus 로고    scopus 로고
    • Recruitment of the cross-linked opsonic receptor CD32A (FcgammaRIIA) to high-density detergent-resistant membrane domains in human neutrophils
    • Rollet-Labelle, E., Marois, S., Barbeau, K., Malawista, S. E., and Naccache, P. H. (2004). Recruitment of the cross-linked opsonic receptor CD32A (FcgammaRIIA) to high-density detergent-resistant membrane domains in human neutrophils. Biochem. J. 381, 919-928.
    • (2004) Biochem. J. , vol.381 , pp. 919-928
    • Rollet-Labelle, E.1    Marois, S.2    Barbeau, K.3    Malawista, S.E.4    Naccache, P.H.5
  • 120
    • 0032532949 scopus 로고    scopus 로고
    • pp56Lck mediates TCR zetachain binding to the microfilament cytoskeleton
    • Rozdzial, M. M., Pleiman, C. M., Cambier, J. C., and Finkel, T. H. (1998). pp56Lck mediates TCR zetachain binding to the microfilament cytoskeleton. J. Immunol. 161, 5491-5499.
    • (1998) J. Immunol. , vol.161 , pp. 5491-5499
    • Rozdzial, M.M.1    Pleiman, C.M.2    Cambier, J.C.3    Finkel, T.H.4
  • 121
    • 33750362016 scopus 로고    scopus 로고
    • Lck SH3 domain function is required for T-cell receptor signals regulating thymocyte development
    • Rudd, M. L., Tua-Smith, A., and Straus, D. B. (2006). Lck SH3 domain function is required for T-cell receptor signals regulating thymocyte development. Mol. Cell. Biol. 26, 7892-7900.
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 7892-7900
    • Rudd, M.L.1    Tua-Smith, A.2    Straus, D.B.3
  • 122
    • 78650992400 scopus 로고    scopus 로고
    • Mislocalization of Lck impairs thymocyte differentiation and can promote development of thymomas
    • Salmond, R. J., Filby, A., Pirinen, N., Magee, A. I., and Zamoyska, R. (2011). Mislocalization of Lck impairs thymocyte differentiation and can promote development of thymomas. Blood 117, 108-117.
    • (2011) Blood , vol.117 , pp. 108-117
    • Salmond, R.J.1    Filby, A.2    Pirinen, N.3    Magee, A.I.4    Zamoyska, R.5
  • 123
    • 61849128182 scopus 로고    scopus 로고
    • T-cell receptor proximal signaling via the Src-family kinases, Lck and Fyn, influences T-cell activation, differentiation, and tolerance
    • Salmond, R. J., Filby, A., Qureshi, I., Caserta, S., and Zamoyska, R. (2009). T-cell receptor proximal signaling via the Src-family kinases, Lck and Fyn, influences T-cell activation, differentiation, and tolerance. Immunol. Rev. 228, 9-22.
    • (2009) Immunol. Rev. , vol.228 , pp. 9-22
    • Salmond, R.J.1    Filby, A.2    Qureshi, I.3    Caserta, S.4    Zamoyska, R.5
  • 125
    • 80052946904 scopus 로고    scopus 로고
    • Feedback circuits monitor and adjust basal Lck-dependent events in T cell receptor signaling
    • Schoenborn, J. R., Tan, Y. X., Zhang, C., Shokat, K. M., and Weiss, A. (2011). Feedback circuits monitor and adjust basal Lck-dependent events in T cell receptor signaling. Sci. Signal. 4, ra59.
    • (2011) Sci. Signal. , vol.4
    • Schoenborn, J.R.1    Tan, Y.X.2    Zhang, C.3    Shokat, K.M.4    Weiss, A.5
  • 127
    • 0033049188 scopus 로고    scopus 로고
    • Expression of the p56(Lck) Y505F mutation in CD45-deficient mice rescues thymocyte development
    • Seavitt, J. R., White, L. S., Murphy, K. M., Loh, D. Y., Perlmutter, R. M., and Thomas, M. L. (1999). Expression of the p56(Lck) Y505F mutation in CD45-deficient mice rescues thymocyte development. Mol. Cell. Biol. 19, 4200-4208.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 4200-4208
    • Seavitt, J.R.1    White, L.S.2    Murphy, K.M.3    Loh, D.Y.4    Perlmutter, R.M.5    Thomas, M.L.6
  • 128
    • 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., Rao, M., and Mayor, S. (2004). Nanoscale organization of multiple GPI-anchored proteins in living cell membranes. Cell 116, 577-589.
    • (2004) Cell , vol.116 , pp. 577-589
    • Sharma, P.1    Varma, R.2    Sarasij, R.C.3    Ira, G.K.4    Krishnamoorthy, G.5    Rao, M.6    Mayor, S.7
  • 129
    • 33750130964 scopus 로고    scopus 로고
    • Lipid rafts: now you see them, now you don't
    • Shaw, A. S. (2006). Lipid rafts: now you see them, now you don't. Nat. Immunol. 7, 1139-1142.
    • (2006) Nat. Immunol. , vol.7 , pp. 1139-1142
    • Shaw, A.S.1
  • 131
    • 0031034930 scopus 로고    scopus 로고
    • Crystal structure of the Src family tyrosine kinase Hck
    • Sicheri, F., Moarefi, I., and Kuriyan, J. (1997). Crystal structure of the Src family tyrosine kinase Hck. Nature 385, 602-609.
    • (1997) Nature , vol.385 , pp. 602-609
    • Sicheri, F.1    Moarefi, I.2    Kuriyan, J.3
  • 133
    • 0030949124 scopus 로고    scopus 로고
    • Functional rafts in cell membranes
    • Simons, K., and Ikonen, E. (1997). Functional rafts in cell membranes. Nature 387, 569-572.
    • (1997) Nature , vol.387 , pp. 569-572
    • Simons, K.1    Ikonen, E.2
  • 135
  • 136
    • 34547116642 scopus 로고    scopus 로고
    • A novel negative regulatory function of the phosphoprotein associated with glycosphingolipidenriched microdomains: blocking Ras activation
    • Smida, M., Posevitz-Fejfar, A., Horejsi, V., Schraven, B., and Lindquist, J. A. (2007). A novel negative regulatory function of the phosphoprotein associated with glycosphingolipidenriched microdomains: blocking Ras activation. Blood 110, 596-615.
    • (2007) Blood , vol.110 , pp. 596-615
    • Smida, M.1    Posevitz-Fejfar, A.2    Horejsi, V.3    Schraven, B.4    Lindquist, J.A.5
  • 138
    • 0031570545 scopus 로고    scopus 로고
    • Aberrant TCR-mediated signaling in CD45null thymocytes involves dysfunctional regulation of Lck, Fyn, TCRzeta, and ZAP-70
    • Stone, J. D., Conroy, L. A., Byth, K. F., Hederer, R. A., Howlett, S., Takemoto, Y., Holmes, N., and Alexander, D. R. (1997). Aberrant TCR-mediated signaling in CD45null thymocytes involves dysfunctional regulation of Lck, Fyn, TCRzeta, and ZAP-70. J. Immunol. 158, 5773-5782.
    • (1997) J. Immunol. , vol.158 , pp. 5773-5782
    • Stone, J.D.1    Conroy, L.A.2    Byth, K.F.3    Hederer, R.A.4    Howlett, S.5    Takemoto, Y.6    Holmes, N.7    Alexander, D.R.8
  • 139
    • 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., and Weiss, A. (1992). Genetic evidence for the involvement of the lck tyrosine kinase in signal transduction through the T cell antigen receptor. Cell 70, 585-593.
    • (1992) Cell , vol.70 , pp. 585-593
    • Straus, D.B.1    Weiss, A.2
  • 140
    • 6944241415 scopus 로고    scopus 로고
    • Activation of naive CD4 T cells by anti-CD3 reveals an important role for Fyn in Lckmediated signaling
    • Sugie, K., Jeon, M. S., and Grey, H. M. (2004). Activation of naive CD4 T cells by anti-CD3 reveals an important role for Fyn in Lckmediated signaling. Proc. Natl. Acad. Sci. U.S.A. 101, 14859-14864.
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 14859-14864
    • Sugie, K.1    Jeon, M.S.2    Grey, H.M.3
  • 142
    • 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., and Viola, A. (2006). CD28 interaction with filamin-A controls lipid raft accumulation at the T-cell immunological synapse. Nat. Cell Biol. 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    Viola, A.7
  • 143
    • 6344241298 scopus 로고    scopus 로고
    • CD28 and lipid rafts coordinate recruitment of Lck to the immunological synapse of human T lymphocytes
    • Tavano, R., Gri, G., Molon, B., Marinari, B., Rudd, C. E., Tuosto, L., and Viola, A. (2004). CD28 and lipid rafts coordinate recruitment of Lck to the immunological synapse of human T lymphocytes. J. Immunol. 173, 5392-5397.
    • (2004) J. Immunol. , vol.173 , pp. 5392-5397
    • Tavano, R.1    Gri, G.2    Molon, B.3    Marinari, B.4    Rudd, C.E.5    Tuosto, L.6    Viola, A.7
  • 145
    • 0028346560 scopus 로고
    • CD45: an emerging role as a protein tyrosine phosphatase required for lymphocyte activation and development
    • Trowbridge, I. S., and Thomas, M. L. (1994). CD45: an emerging role as a protein tyrosine phosphatase required for lymphocyte activation and development. Annu. Rev. Immunol. 12, 85-116.
    • (1994) Annu. Rev. Immunol. , vol.12 , pp. 85-116
    • Trowbridge, I.S.1    Thomas, M.L.2
  • 146
    • 58149089103 scopus 로고    scopus 로고
    • Activation of c-Src and Fyn kinases by protein-tyrosine phosphatase RPTPalpha is substratespecific and compatible with lipid raft localization
    • Vacaresse, N., Moller, B., Danielsen, E. M., Okada, M., and Sap, J. (2008). Activation of c-Src and Fyn kinases by protein-tyrosine phosphatase RPTPalpha is substratespecific and compatible with lipid raft localization. J. Biol. Chem. 283, 35815-35824.
    • (2008) J. Biol. Chem. , vol.283 , pp. 35815-35824
    • Vacaresse, N.1    Moller, B.2    Danielsen, E.M.3    Okada, M.4    Sap, J.5
  • 148
    • 0029866039 scopus 로고    scopus 로고
    • Lck regulates the tyrosine phosphorylation of the T cell receptor subunits and ZAP-70 in murine thymocytes
    • van Oers, N. S., Killeen, N., and Weiss, A. (1996). Lck regulates the tyrosine phosphorylation of the T cell receptor subunits and ZAP-70 in murine thymocytes. J. Exp. Med. 183, 1053-1062.
    • (1996) J. Exp. Med. , vol.183 , pp. 1053-1062
    • van Oers, N.S.1    Killeen, N.2    Weiss, A.3
  • 149
    • 0036219193 scopus 로고    scopus 로고
    • Negative regulation of immunoreceptor signaling
    • Veillette, A., Latour, S., and Davidson, D. (2002). Negative regulation of immunoreceptor signaling. Annu. Rev. Immunol. 20, 669-707.
    • (2002) Annu. Rev. Immunol. , vol.20 , pp. 669-707
    • Veillette, A.1    Latour, S.2    Davidson, D.3
  • 150
    • 35548942611 scopus 로고    scopus 로고
    • Tether and trap: regulation of membraneraft dynamics by actin-binding proteins
    • Viola, A., and Gupta, N. (2007). Tether and trap: regulation of membraneraft dynamics by actin-binding proteins. Nat. Rev. Immunol. 7,889-896.
    • (2007) Nat. Rev. Immunol. , vol.7 , pp. 889-896
    • Viola, A.1    Gupta, N.2
  • 151
    • 0036604916 scopus 로고    scopus 로고
    • The T-cell receptor signalosome: a dynamic structure with expanding complexity
    • Werlen, G., and Palmer, E. (2002). The T-cell receptor signalosome: a dynamic structure with expanding complexity. Curr. Opin. Immunol. 14, 299-305.
    • (2002) Curr. Opin. Immunol. , vol.14 , pp. 299-305
    • Werlen, G.1    Palmer, E.2
  • 152
  • 153
    • 77956076669 scopus 로고    scopus 로고
    • Structural biology of the T-cell receptor: insights into receptor assembly,ligand recognition,and initiation of signaling
    • Wucherpfennig, K. W., Gagnon, E., Call, M. J., Huseby, E. S., and Call, M. E. (2010). Structural biology of the T-cell receptor: insights into receptor assembly,ligand recognition,and initiation of signaling. Cold Spring Harb. Perspect. Biol. 2, a005140.
    • (2010) Cold Spring Harb. Perspect. Biol. , vol.2
    • Wucherpfennig, K.W.1    Gagnon, E.2    Call, M.J.3    Huseby, E.S.4    Call, M.E.5
  • 154
    • 55449138409 scopus 로고    scopus 로고
    • Regulation of T cell receptor activation by dynamic membrane binding of the CD3epsilon cytoplasmic tyrosinebased motif
    • Xu, C., Gagnon, E., Call, M. E., Schnell, J. R., Schwieters, C. D., Carman, C. V., Chou, J. J., and Wucherpfennig, K. W. (2008). Regulation of T cell receptor activation by dynamic membrane binding of the CD3epsilon cytoplasmic tyrosinebased motif. Cell 135, 702-713.
    • (2008) Cell , vol.135 , pp. 702-713
    • Xu, C.1    Gagnon, E.2    Call, M.E.3    Schnell, J.R.4    Schwieters, C.D.5    Carman, C.V.6    Chou, J.J.7    Wucherpfennig, K.W.8
  • 155
    • 0031025991 scopus 로고    scopus 로고
    • Three-dimensional structure of the tyrosine kinase c-Src
    • Xu, W., Harrison, S. C., and Eck, M. J. (1997). Three-dimensional structure of the tyrosine kinase c-Src. Nature 385, 595-602.
    • (1997) Nature , vol.385 , pp. 595-602
    • Xu, W.1    Harrison, S.C.2    Eck, M.J.3
  • 156
    • 16144364951 scopus 로고    scopus 로고
    • Structural basis for activation of human lymphocyte kinase Lck upon tyrosine phosphorylation
    • Yamaguchi, H., and Hendrickson, W. A. (1996). Structural basis for activation of human lymphocyte kinase Lck upon tyrosine phosphorylation. Nature 384, 484-489.
    • (1996) Nature , vol.384 , pp. 484-489
    • Yamaguchi, H.1    Hendrickson, W.A.2
  • 158
    • 0037307095 scopus 로고    scopus 로고
    • The influence of the srcfamily kinases,Lck and Fyn, on T cell differentiation, survival and activation
    • Zamoyska, R., Basson, A., Filby, A., Legname, G., Lovatt, M., and Seddon, B. (2003). The influence of the srcfamily kinases,Lck and Fyn, on T cell differentiation, survival and activation. Immunol. Rev. 191, 107-118.
    • (2003) Immunol. Rev. , vol.191 , pp. 107-118
    • Zamoyska, R.1    Basson, A.2    Filby, A.3    Legname, G.4    Lovatt, M.5    Seddon, B.6


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