메뉴 건너뛰기




Volumn 277, Issue 21, 2010, Pages 4383-4397

LAT - An important raft-associated transmembrane adaptor protein: Delivered on 6 July 2009 at the 34th FEBS Congress in Prague, Czech Republic

Author keywords

Immunoreceptor signalling; LAT; Raft; Transmembrane adaptor protein; Tyrosine phosphorylation

Indexed keywords

FC RECEPTOR; LAT PROTEIN; NATURAL KILLER CELL RECEPTOR; T LYMPHOCYTE RECEPTOR; THROMBOCYTE RECEPTOR; CELL SURFACE RECEPTOR; LAT PROTEIN, HUMAN; LYMPHOCYTE ANTIGEN RECEPTOR; MEMBRANE PROTEIN; SIGNAL TRANSDUCING ADAPTOR PROTEIN;

EID: 79952114745     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2010.07831.x     Document Type: Conference Paper
Times cited : (7)

References (154)
  • 2
    • 34548319444 scopus 로고    scopus 로고
    • Role of the extracellular and transmembrane domain of Ig-α/β in assembly of the B cell antigen receptor (BCR)
    • DOI 10.1016/j.imlet.2007.06.005, PII S0165247807001435
    • Dylke J, Lopes J, Dang-Lawson M, Machtaler S & Matsuuchi L (2007) Role of the extracellular and transmembrane domain of Ig-α/β in assembly of the B cell antigen receptor (BCR). Immunol Lett 112, 47-57. (Pubitemid 47336979)
    • (2007) Immunology Letters , vol.112 , Issue.1 , pp. 47-57
    • Dylke, J.1    Lopes, J.2    Dang-Lawson, M.3    Machtaler, S.4    Matsuuchi, L.5
  • 3
    • 28544438330 scopus 로고    scopus 로고
    • Role of ITAM-containing adapter proteins and their receptors in the immune system and bone
    • Humphrey MB, Lanier LL & Nakamura MC (2005) Role of ITAM-containing adapter proteins and their receptors in the immune system and bone. Immunol Rev 208, 50-65. (Pubitemid 41746384)
    • (2005) Immunological Reviews , vol.208 , pp. 50-65
    • Humphrey, M.B.1    Lanier, L.L.2    Nakamura, M.C.3
  • 4
    • 70350414455 scopus 로고    scopus 로고
    • The expanding roles of ITAM adapters FcRγ and DAP12 in myeloid cells
    • Hamerman JA, Ni M, Killebrew JR, Chu CL & Lowell CA (2009) The expanding roles of ITAM adapters FcRγ and DAP12 in myeloid cells. Immunol Rev 232, 42-58.
    • (2009) Immunol Rev , vol.232 , pp. 42-58
    • Hamerman, J.A.1    Ni, M.2    Killebrew, J.R.3    Chu, C.L.4    Lowell, C.A.5
  • 5
    • 58049200736 scopus 로고    scopus 로고
    • DAP10- and DAP12-associated receptors in innate immunity
    • Lanier LL (2009) DAP10- and DAP12-associated receptors in innate immunity. Immunol Rev 227, 150-160.
    • (2009) Immunol Rev , vol.227 , pp. 150-160
    • Lanier, L.L.1
  • 6
    • 1842814045 scopus 로고    scopus 로고
    • Transmembrane adaptor proteins in membrane microdomains: Important regulators of immunoreceptor signaling
    • Horejsi V (2004) Transmembrane adaptor proteins in membrane microdomains: important regulators of immunoreceptor signaling. Immunol Lett 92, 43-49.
    • (2004) Immunol Lett , vol.92 , pp. 43-49
    • Horejsi, V.1
  • 7
    • 50849124153 scopus 로고    scopus 로고
    • Identification of a new transmembrane adaptor protein that constitutively binds Grb2 in B cells
    • Liu Y & Zhang W (2008) Identification of a new transmembrane adaptor protein that constitutively binds Grb2 in B cells. J Leukoc Biol 84, 842-851.
    • (2008) J Leukoc Biol , vol.84 , pp. 842-851
    • Liu, Y.1    Zhang, W.2
  • 8
    • 3543071011 scopus 로고    scopus 로고
    • Transmembrane adaptor proteins: Organizers of immunoreceptor signalling
    • Horejsi V, Zhang W & Schraven B (2004) Transmembrane adaptor proteins: organizers of immunoreceptor signalling. Nat Rev Immunol 4, 603-616. (Pubitemid 39025046)
    • (2004) Nature Reviews Immunology , vol.4 , Issue.8 , pp. 603-616
    • Horejsi, V.1    Zhang, W.2    Schraven, B.3
  • 9
    • 4544309074 scopus 로고    scopus 로고
    • TCR ζ-chain downregulation: Curtailing an excessive inflammatory immune response
    • Baniyash M (2004) TCR ζ-chain downregulation: curtailing an excessive inflammatory immune response. Nat Rev Immunol 4, 675-687.
    • (2004) Nat Rev Immunol , vol.4 , pp. 675-687
    • Baniyash, M.1
  • 10
    • 14644403593 scopus 로고    scopus 로고
    • NTAL/LAB and LAT: A balancing act in mast-cell activation and function
    • Rivera J (2005) NTAL/LAB and LAT: a balancing act in mast-cell activation and function. Trends Immunol 26, 119-122.
    • (2005) Trends Immunol , vol.26 , pp. 119-122
    • Rivera, J.1
  • 11
    • 9644266657 scopus 로고    scopus 로고
    • Right time, right place: The organization of membrane proximal signaling
    • DOI 10.1016/j.smim.2004.09.002, PII S1044532304000570, Spacial Organization in Immune Cell Signaling
    • Simeoni L, Smida M, Posevitz V, Schraven B & Lindquist JA (2005) Right time, right place: the organization of membrane proximal signaling. Semin Immunol 17, 35-49. (Pubitemid 39575980)
    • (2005) Seminars in Immunology , vol.17 , Issue.1 , pp. 35-49
    • Simeoni, L.1    Smida, M.2    Posevitz, V.3    Schraven, B.4    Lindquist, J.A.5
  • 13
    • 34247871586 scopus 로고    scopus 로고
    • The expanding role for ITAM-based signaling pathways in immune cells
    • Abram CL & Lowell CA (2007) The expanding role for ITAM-based signaling pathways in immune cells. Sci STKE 2007, re2.
    • (2007) Sci STKE , vol.2007
    • Abram, C.L.1    Lowell, C.A.2
  • 14
    • 33846562134 scopus 로고    scopus 로고
    • Activating and inhibitory functions of DAP12
    • DOI 10.1038/nri2014, PII NRI2014
    • Turnbull IR & Colonna M (2007) Activating and inhibitory functions of DAP12. Nat Rev Immunol 7, 155-161. (Pubitemid 46174861)
    • (2007) Nature Reviews Immunology , vol.7 , Issue.2 , pp. 155-161
    • Turnbull, I.R.1    Colonna, M.2
  • 15
    • 70350376377 scopus 로고    scopus 로고
    • Regulation of lymphocyte development and activation by the LAT family of adapter proteins
    • Fuller DM & Zhang W (2009) Regulation of lymphocyte development and activation by the LAT family of adapter proteins. Immunol Rev 232, 72-83.
    • (2009) Immunol Rev , vol.232 , pp. 72-83
    • Fuller, D.M.1    Zhang, W.2
  • 16
    • 79952231423 scopus 로고    scopus 로고
    • Transmembrane adaptor proteins positively regulating the activation of lymphocytes
    • Park I & Yun Y (2009) Transmembrane adaptor proteins positively regulating the activation of lymphocytes. Immune Netw 9, 53-57.
    • (2009) Immune Netw , vol.9 , pp. 53-57
    • Park, I.1    Yun, Y.2
  • 17
    • 33746085241 scopus 로고    scopus 로고
    • Rafts defined: A report on the Keystone Symposium on Lipid Rafts and Cell Function
    • Pike LJ (2006) Rafts defined: a report on the Keystone Symposium on Lipid Rafts and Cell Function. J Lipid Res 47, 1597-1598.
    • (2006) J Lipid Res , vol.47 , pp. 1597-1598
    • Pike, L.J.1
  • 18
    • 0343151924 scopus 로고    scopus 로고
    • Signal transduction in leucocytes via GPI-anchored proteins: An experimental artefact or an aspect of immunoreceptor function?
    • Horejsi V, Cebecauer M, Cerny J, Brdicka T, Angelisova P & Drbal K (1998) Signal transduction in leucocytes via GPI-anchored proteins: an experimental artefact or an aspect of immunoreceptor function? Immunol Lett 63, 63-73.
    • (1998) Immunol Lett , vol.63 , pp. 63-73
    • Horejsi, V.1    Cebecauer, M.2    Cerny, J.3    Brdicka, T.4    Angelisova, P.5    Drbal, K.6
  • 19
    • 46849102138 scopus 로고    scopus 로고
    • The glycosylphosphatidylinositol anchor: A complex membrane-anchoring structure for proteins
    • DOI 10.1021/bi8006324
    • Paulick MG & Bertozzi CR (2008) The glycosylphosphatidylinositol anchor: a complex membrane-anchoring structure for proteins. Biochemistry 47, 6991-7000. (Pubitemid 351956348)
    • (2008) Biochemistry , vol.47 , Issue.27 , pp. 6991-7000
    • Paulick, M.G.1    Bertozzi, C.R.2
  • 20
    • 54249110423 scopus 로고    scopus 로고
    • Dual acylation and lipid raft association of Src-family protein tyrosine kinases are required for SDF-1/CXCL12-mediated chemotaxis in the Jurkat human T cell lymphoma cell line
    • Zaman SN, Resek ME & Robbins SM (2008) Dual acylation and lipid raft association of Src-family protein tyrosine kinases are required for SDF-1/CXCL12-mediated chemotaxis in the Jurkat human T cell lymphoma cell line. J Leukoc Biol 84, 1082-1091.
    • (2008) J Leukoc Biol , vol.84 , pp. 1082-1091
    • Zaman, S.N.1    Resek, M.E.2    Robbins, S.M.3
  • 21
    • 23044449837 scopus 로고    scopus 로고
    • Lipids, lipid rafts and caveolae: Their importance for GPCR signaling and their centrality to the endocannabinoid system
    • DOI 10.1016/j.lfs.2005.05.040, PII S0024320505004868, Yargeted Lipidomics: Endocannabinoids and other Endolipid Modulators
    • Barnett-Norris J, Lynch D & Reggio PH (2005) Lipids, lipid rafts and caveolae: their importance for GPCR signaling and their centrality to the endocannabinoid system. Life Sci 77, 1625-1639. (Pubitemid 41073657)
    • (2005) Life Sciences , vol.77 , Issue.14 , pp. 1625-1639
    • Barnett-Norris, J.1    Lynch, D.2    Reggio, P.H.3
  • 22
    • 0035028838 scopus 로고    scopus 로고
    • Raft membrane domains: From a liquid-ordered membrane phase to a site of pathogen attack
    • van der Goot FG & Harder T (2001) Raft membrane domains: from a liquid-ordered membrane phase to a site of pathogen attack. Semin Immunol 13, 89-97.
    • (2001) Semin Immunol , vol.13 , pp. 89-97
    • Van Der Goot, F.G.1    Harder, T.2
  • 23
    • 15244348270 scopus 로고    scopus 로고
    • Lipid rafts and their roles in T-cell activation
    • Horejsi V (2005) Lipid rafts and their roles in T-cell activation. Microbes Infect 7, 310-316.
    • (2005) Microbes Infect , vol.7 , pp. 310-316
    • Horejsi, V.1
  • 24
    • 2442713628 scopus 로고    scopus 로고
    • Lipid rafts in lymphocyte activation
    • DOI 10.1016/j.micinf.2004.02.017, PII S1286457904000954
    • Pizzo P & Viola A (2004) Lipid rafts in lymphocyte activation. Microbes Infect 6, 686-692. (Pubitemid 38670550)
    • (2004) Microbes and Infection , vol.6 , Issue.7 , pp. 686-692
    • Pizzo, P.1    Viola, A.2
  • 25
    • 74849118341 scopus 로고    scopus 로고
    • Lipid rafts as a membrane-organizing principle
    • Lingwood D & Simons K (2010) Lipid rafts as a membrane-organizing principle. Science 327, 46-50.
    • (2010) Science , vol.327 , pp. 46-50
    • Lingwood, D.1    Simons, K.2
  • 26
    • 70349469585 scopus 로고    scopus 로고
    • Domains in biological membranes
    • Lindner R & Naim HY (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
  • 27
    • 65649122726 scopus 로고    scopus 로고
    • Lattices, rafts, and scaffolds: Domain regulation of receptor signaling at the plasma membrane
    • Lajoie P, Goetz JG, Dennis JW & Nabi IR (2009) Lattices, rafts, and scaffolds: domain regulation of receptor signaling at the plasma membrane. J Cell Biol 185, 381-385.
    • (2009) J Cell Biol , vol.185 , pp. 381-385
    • Lajoie, P.1    Goetz, J.G.2    Dennis, J.W.3    Nabi, I.R.4
  • 28
    • 33845901815 scopus 로고    scopus 로고
    • Lipid rafts: At a crossroad between cell biology and physics
    • DOI 10.1038/ncb0107-7, PII NCB0107-7
    • Jacobson K, Mouritsen OG & Anderson RG (2007) Lipid rafts: at a crossroad between cell biology and physics. Nat Cell Biol 9, 7-14. (Pubitemid 46024188)
    • (2007) Nature Cell Biology , vol.9 , Issue.1 , pp. 7-14
    • Jacobson, K.1    Mouritsen, O.G.2    Anderson, R.G.W.3
  • 32
    • 77950860471 scopus 로고    scopus 로고
    • Exploring the caves: Cavins, caveolins and caveolae
    • Hansen CG & Nichols BJ (2010) Exploring the caves: cavins, caveolins and caveolae. Trends Cell Biol 20, 177-186.
    • (2010) Trends Cell Biol , vol.20 , pp. 177-186
    • Hansen, C.G.1    Nichols, B.J.2
  • 34
    • 77949888199 scopus 로고    scopus 로고
    • Plasma membrane rafts engaged in T cell signalling: New developments in an old concept
    • Harder T & Sangani D (2009) Plasma membrane rafts engaged in T cell signalling: new developments in an old concept. Cell Commun Signal 7, 21.
    • (2009) Cell Commun Signal , vol.7 , pp. 21
    • Harder, T.1    Sangani, D.2
  • 35
    • 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
  • 36
    • 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 & 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
  • 37
    • 0037090529 scopus 로고    scopus 로고
    • TCR signal initiation machinery is pre-assembled and activated in a subset of membrane rafts
    • DOI 10.1093/emboj/21.8.1899
    • Drevot P, Langlet C, Guo XJ, Bernard AM, Colard O, Chauvin JP, Lasserre R & He HT (2002) TCR signal initiation machinery is pre-assembled and activated in a subset of membrane rafts. EMBO J 21, 1899-1908. (Pubitemid 34437187)
    • (2002) EMBO Journal , vol.21 , Issue.8 , 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
  • 38
    • 67649922863 scopus 로고    scopus 로고
    • Endocytosis of MHC molecules by distinct membrane rafts
    • Knorr R, Karacsonyi C & 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
  • 39
    • 0029081182 scopus 로고
    • T cell activation-dependent association between the p85 subunit of the phosphatidylinositol 3-kinase and Grb2/phospholipase C-γ 1-binding phosphotyrosyl protein pp36/38
    • Fukazawa T, Reedquist KA, Panchamoorthy G, Soltoff S, Trub T, Druker B, Cantley L, Shoelson SE & Band H (1995) T cell activation-dependent association between the p85 subunit of the phosphatidylinositol 3-kinase and Grb2/phospholipase C-γ 1-binding phosphotyrosyl protein pp36/38. J Biol Chem 270, 20177-20182.
    • (1995) J Biol Chem , vol.270 , pp. 20177-20182
    • Fukazawa, T.1    Reedquist, K.A.2    Panchamoorthy, G.3    Soltoff, S.4    Trub, T.5    Druker, B.6    Cantley, L.7    Shoelson, S.E.8    Band, H.9
  • 40
    • 0032498231 scopus 로고    scopus 로고
    • LAT: The ZAP-70 tyrosine kinase substrate that links T cell receptor to cellular activation
    • DOI 10.1016/S0092-8674(00)80901-0
    • Zhang W, Sloan-Lancaster J, Kitchen J, Trible RP & Samelson LE (1998) LAT: the ZAP-70 tyrosine kinase substrate that links T cell receptor to cellular activation. Cell 92, 83-92. (Pubitemid 28053300)
    • (1998) Cell , vol.92 , Issue.1 , pp. 83-92
    • Zhang, W.1    Sloan-Lancaster, J.2    Kitchen, J.3    Trible, R.P.4    Samelson, L.E.5
  • 42
    • 0038127081 scopus 로고    scopus 로고
    • Appearance of the LAT protein at an early stage of B-cell development and its possible role
    • DOI 10.1046/j.1365-2567.2003.01671.x
    • Oya K, Wang J, Watanabe Y, Koga R & Watanabe T (2003) Appearance of the LAT protein at an early stage of B-cell development and its possible role. Immunology 109, 351-359. (Pubitemid 36783260)
    • (2003) Immunology , vol.109 , Issue.3 , pp. 351-359
    • Oya, K.1    Wang, J.2    Watanabe, Y.3    Koga, R.4    Watanabe, T.5
  • 43
    • 0041429608 scopus 로고    scopus 로고
    • LAT links the pre-BCR to calcium signaling
    • Su YW & Jumaa H (2003) LAT links the pre-BCR to calcium signaling. Immunity 19, 295-305.
    • (2003) Immunity , vol.19 , pp. 295-305
    • Su, Y.W.1    Jumaa, H.2
  • 45
    • 0032545307 scopus 로고    scopus 로고
    • The p85 subunit of phosphatidylinositol 3-kinase associates with the Fc receptor gamma-chain and linker for activitor of T cells (LAT) in platelets stimulated by collagen and convulxin
    • DOI 10.1074/jbc.273.51.34437
    • Gibbins JM, Briddon S, Shutes A, van Vugt MJ, van de Winkel JG, Saito T & Watson SP (1998) The p85 subunit of phosphatidylinositol 3-kinase associates with the Fc receptor γ-chain and linker for activitor of T cells (LAT) in platelets stimulated by collagen and convulxin. J Biol Chem 273, 34437-34443. (Pubitemid 29008923)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.51 , pp. 34437-34443
    • Gibbins, J.M.1    Briddon, S.2    Shutes, A.3    Van, V.M.J.4    Van De, W.J.G.J.5    Saito, T.6    Watson, S.P.7
  • 46
    • 0032921873 scopus 로고    scopus 로고
    • Linker for activation of T cells (LAT), a novel immunohistochemical marker for T cells, NK cells, mast cells, and megakaryocytes. Evaluation in normal and pathological conditions
    • Facchetti F, Chan JK, Zhang W, Tironi A, Chilosi M, Parolini S, Notarangelo LD & Samelson LE (1999) Linker for activation of T cells (LAT), a novel immunohistochemical marker for T cells, NK cells, mast cells, and megakaryocytes: evaluation in normal and pathological conditions. Am J Pathol 154, 1037-1046. (Pubitemid 29169738)
    • (1999) American Journal of Pathology , vol.154 , Issue.4 , pp. 1037-1046
    • Facchetti, F.1    Chan, J.K.C.2    Zhang, W.3    Tironi, A.4    Chilosi, M.5    Parolini, S.6    Notarangelo, L.D.7    Samelson, L.E.8
  • 47
    • 68149166401 scopus 로고    scopus 로고
    • Palmitoylation-dependent plasma membrane transport but lipid raft-independent signaling by linker for activation of T cells
    • Hundt M, Harada Y, De Giorgio L, Tanimura N, Zhang W & Altman A (2009) Palmitoylation-dependent plasma membrane transport but lipid raft-independent signaling by linker for activation of T cells. J Immunol 183, 1685-1694.
    • (2009) J Immunol , vol.183 , pp. 1685-1694
    • Hundt, M.1    Harada, Y.2    De Giorgio, L.3    Tanimura, N.4    Zhang, W.5    Altman, A.6
  • 48
    • 0037385274 scopus 로고    scopus 로고
    • + T cells in the presence of anti-CD4 monoclonal antibodies: Evidence for reduced phosphorylation of Zap-70 and LAT
    • DOI 10.1046/j.1365-3083.2003.01241.x
    • Pullar CE, Morris PJ & Wood KJ (2003) Altered proximal T-cell receptor signalling events in mouse CD4+ T cells in the presence of anti-CD4 monoclonal antibodies: evidence for reduced phosphorylation of Zap-70 and LAT. Scand J Immunol 57, 333-341. (Pubitemid 36408204)
    • (2003) Scandinavian Journal of Immunology , vol.57 , Issue.4 , pp. 333-341
    • Pullar, C.E.1    Morris, P.J.2    Wood, K.J.3
  • 49
    • 33846693328 scopus 로고    scopus 로고
    • Evidence of LAT as a dual substrate for Lck and Syk in T lymphocytes
    • DOI 10.1016/j.leukres.2006.07.010, PII S0145212606002748
    • Jiang Y & Cheng H (2007) Evidence of LAT as a dual substrate for Lck and Syk in T lymphocytes. Leuk Res 31, 541-545. (Pubitemid 46198937)
    • (2007) Leukemia Research , vol.31 , Issue.4 , pp. 541-545
    • Jiang, Y.1    Cheng, H.2
  • 50
    • 0034725625 scopus 로고    scopus 로고
    • Association of Grb2, Gads, and phospholipase C-γ1 with phosphorylated LAT tyrosine residues: Effect of LAT tyrosine mutations on T cell antigen receptor-mediated signaling
    • DOI 10.1074/jbc.M000404200
    • Zhang W, Trible RP, Zhu M, Liu SK, McGlade CJ & Samelson LE (2000) Association of Grb2, Gads, and phospholipase C-γ 1 with phosphorylated LAT tyrosine residues. Effect of LAT tyrosine mutations on T cell antigen receptor-mediated signaling. J Biol Chem 275, 23355-23361. (Pubitemid 30646238)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.30 , pp. 23355-23361
    • Zhang, W.1    Trible, R.P.2    Zhu, M.3    Liu, S.K.4    McGlade, C.J.5    Samelson, L.E.6
  • 51
    • 0035800805 scopus 로고    scopus 로고
    • Identification of the Minimal Tyrosine Residues Required for Linker for Activation of T Cell Function
    • DOI 10.1074/jbc.M102221200
    • Lin J & Weiss A (2001) Identification of the minimal tyrosine residues required for linker for activation of T cell function. J Biol Chem 276, 29588-29595. (Pubitemid 37452058)
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.31 , pp. 29588-29595
    • Lin, J.1    Weiss, A.2
  • 52
    • 0035365877 scopus 로고    scopus 로고
    • Mapping the Zap-70 phosphorylation sites on LAT (linker for activation of T cells) required for recruitment and activation of signalling proteins in T cells
    • DOI 10.1042/0264-6021:3560461
    • Paz PE, Wang S, Clarke H, Lu X, Stokoe D & Abo A (2001) Mapping the Zap-70 phosphorylation sites on LAT (linker for activation of T cells) required for recruitment and activation of signalling proteins in T cells. Biochem J 356, 461-471. (Pubitemid 32532357)
    • (2001) Biochemical Journal , vol.356 , Issue.2 , pp. 461-471
    • Paz, P.E.1    Wang, S.2    Clarke, H.3    Lu, X.4    Stokoe, D.5    Abo, A.6
  • 53
    • 0343181431 scopus 로고    scopus 로고
    • The hematopoietic-specific adaptor protein Gads functions in T-cell signaling via interactions with the SLP-76 and LAT adaptors
    • DOI 10.1016/S0960-9822(99)80017-7
    • Liu SK, Fang N, Koretzky GA & McGlade CJ (1999) The hematopoietic-specific adaptor protein Gads functions in T-cell signaling via interactions with the SLP-76 and LAT adaptors. Curr Biol 9, 67-75. (Pubitemid 29083530)
    • (1999) Current Biology , vol.9 , Issue.2 , pp. 67-75
    • Liu, S.K.1    Fang, N.2    Koretzky, G.A.3    McGlade, C.J.4
  • 54
    • 61349122046 scopus 로고    scopus 로고
    • Phosphotyrosine- dependent in vitro reconstitution of recombinant LAT-nucleated multiprotein signalling complexes on liposomes
    • Sangani D, Venien-Bryan C & Harder T (2009) Phosphotyrosine- dependent in vitro reconstitution of recombinant LAT-nucleated multiprotein signalling complexes on liposomes. Mol Membr Biol 26, 159-170.
    • (2009) Mol Membr Biol , vol.26 , pp. 159-170
    • Sangani, D.1    Venien-Bryan, C.2    Harder, T.3
  • 55
    • 2342558054 scopus 로고    scopus 로고
    • Structural basis for differential recognition of tyrosine-phosphorylated sites in the linker for activation of T cells (LAT) by the adaptor Gads
    • DOI 10.1038/sj.emboj.7600168
    • Cho S, Velikovsky CA, Swaminathan CP, Houtman JC, Samelson LE & Mariuzza RA (2004) Structural basis for differential recognition of tyrosine-phosphorylated sites in the linker for activation of T cells (LAT) by the adaptor Gads. EMBO J 23, 1441-1451. (Pubitemid 38579505)
    • (2004) EMBO Journal , vol.23 , Issue.7 , pp. 1441-1451
    • Cho, S.1    Velikovsky, C.A.2    Swaminathan, C.P.3    Houtman, J.C.D.4    Samelson, L.E.5    Mariuzza, R.A.6
  • 56
    • 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 (2003) 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 371, 907-915.
    • (2003) Biochem J , vol.371 , pp. 907-915
    • Kabouridis, P.S.1
  • 58
    • 67650351935 scopus 로고    scopus 로고
    • Cytoskeletal protein 4.1R negatively regulates T-cell activation by inhibiting the phosphorylation of LAT
    • Kang Q, Yu Y, Pei X, Hughes R, Heck S, Zhang X, Guo X, Halverson G, Mohandas N & An X (2009) Cytoskeletal protein 4.1R negatively regulates T-cell activation by inhibiting the phosphorylation of LAT. Blood 113, 6128-6137.
    • (2009) Blood , vol.113 , pp. 6128-6137
    • Kang, Q.1    Yu, Y.2    Pei, X.3    Hughes, R.4    Heck, S.5    Zhang, X.6    Guo, X.7    Halverson, G.8    Mohandas, N.9    An, X.10
  • 59
    • 22744444805 scopus 로고    scopus 로고
    • Receptor-stimulated oxidation of SHP-2 promotes T-cell adhesion through SLP-76-ADAP
    • DOI 10.1038/sj.emboj.7600706
    • Kwon J, Qu CK, Maeng JS, Falahati R, Lee C & Williams MS (2005) Receptor-stimulated oxidation of SHP-2 promotes T-cell adhesion through SLP-76-ADAP. EMBO J 24, 2331-2341. (Pubitemid 41032585)
    • (2005) EMBO Journal , vol.24 , Issue.13 , pp. 2331-2341
    • Kwon, J.1    Qu, C.-K.2    Maeng, J.-S.3    Falahati, R.4    Lee, C.5    Williams, M.S.6
  • 60
    • 85047682727 scopus 로고    scopus 로고
    • FcγRIIB-mediated inhibition of T-cell receptor signal transduction involves the phosphorylation of SH2-containing inositol 5-phosphatase (SHIP), dephosphorylation of the linker of activated T-cells (LAT) and inhibition of calcium mobilization
    • DOI 10.1042/0300-5127:0290840
    • Jensen WA, Marschner S, Ott VL & Cambier JC (2001) FcγRIIB-mediated inhibition of T-cell receptor signal transduction involves the phosphorylation of SH2-containing inositol 5-phosphatase (SHIP), dephosphorylation of the linker of activated T-cells (LAT) and inhibition of calcium mobilization. Biochem Soc Trans 29, 840-846. (Pubitemid 33131791)
    • (2001) Biochemical Society Transactions , vol.29 , Issue.6 , pp. 840-846
    • Jensen, W.A.1    Marschner, S.2    Ott, V.L.3    Cambier, J.C.4
  • 62
    • 13644264764 scopus 로고    scopus 로고
    • The adaptor molecules LAT and SLP-76 are specifically targeted by Yersinia to inhibit T cell activation
    • DOI 10.1084/jem.20041120
    • Gerke C, Falkow S & Chien YH (2005) The adaptor molecules LAT and SLP-76 are specifically targeted by Yersinia to inhibit T cell activation. J Exp Med 201, 361-371. (Pubitemid 40229411)
    • (2005) Journal of Experimental Medicine , vol.201 , Issue.3 , pp. 361-371
    • Gerke, C.1    Falkow, S.2    Chien, Y.-H.3
  • 63
    • 34548012864 scopus 로고    scopus 로고
    • Plasma membrane segregation during T cell activation: Probing the order of domains
    • DOI 10.1016/j.coi.2007.05.002, PII S0952791507000970
    • Harder T, Rentero C, Zech T & Gaus K (2007) Plasma membrane segregation during T cell activation: probing the order of domains. Curr Opin Immunol 19, 470-475. (Pubitemid 47284850)
    • (2007) Current Opinion in Immunology , vol.19 , Issue.4 , pp. 470-475
    • Harder, T.1    Rentero, C.2    Zech, T.3    Gaus, K.4
  • 64
    • 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 AE & Levine AD (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. (Pubitemid 34171823)
    • (2002) Journal of Immunology , vol.168 , Issue.5 , pp. 2233-2239
    • Schade, A.E.1    Levine, A.D.2
  • 66
    • 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
    • DOI 10.1016/j.cell.2005.04.009, PII S0092867405003521
    • Douglass AD & Vale RD (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. (Pubitemid 40806424)
    • (2005) Cell , vol.121 , Issue.6 , pp. 937-950
    • Douglass, A.D.1    Vale, R.D.2
  • 67
  • 69
    • 27644439861 scopus 로고    scopus 로고
    • Examining multiprotein signaling complexes from all angles
    • Houtman JC, Barda-Saad M & Samelson LE (2005) Examining multiprotein signaling complexes from all angles. FEBS J 272, 5426-5435.
    • (2005) FEBS J , vol.272 , pp. 5426-5435
    • Houtman, J.C.1    Barda-Saad, M.2    Samelson, L.E.3
  • 71
    • 77649255627 scopus 로고    scopus 로고
    • Subcellular dynamics of T cell immunological synapses and kinases in lymph nodes
    • Azar GA, Lemaitre F, Robey EA & Bousso P (2010) Subcellular dynamics of T cell immunological synapses and kinases in lymph nodes. Proc Natl Acad Sci USA 107, 3675-3680.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 3675-3680
    • Azar, G.A.1    Lemaitre, F.2    Robey, E.A.3    Bousso, P.4
  • 74
    • 77954380512 scopus 로고    scopus 로고
    • T-cell receptor microclusters critical for T-cell activation are formed independently of lipid raft clustering
    • Hashimoto-Tane A, Yokosuka T, Ishihara C, Sakuma M, Kobayashi W & Saito T (2010) T-cell receptor microclusters critical for T-cell activation are formed independently of lipid raft clustering. Mol Cell Biol 30, 3421-3429.
    • (2010) Mol Cell Biol , vol.30 , pp. 3421-3429
    • Hashimoto-Tane, A.1    Yokosuka, T.2    Ishihara, C.3    Sakuma, M.4    Kobayashi, W.5    Saito, T.6
  • 75
    • 0342713043 scopus 로고    scopus 로고
    • T cell receptor signalling results in rapid tyrosine phosphorylation of the linker protein LAT present in detergent-resistant membrane microdomains
    • DOI 10.1006/bbrc.1998.8857
    • Brdicka T, Cerny J & Horejsi V (1998) T cell receptor signalling results in rapid tyrosine phosphorylation of the linker protein LAT present in detergent-resistant membrane microdomains. Biochem Biophys Res Commun 248, 356-360. (Pubitemid 28386426)
    • (1998) Biochemical and Biophysical Research Communications , vol.248 , Issue.2 , pp. 356-360
    • Brdicka, T.1    Cerny, J.2    Horejsi, V.3
  • 76
    • 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 (1998) LAT palmitoylation: its essential role in membrane microdomain targeting and tyrosine phosphorylation during T cell activation. Immunity 9, 239-246. (Pubitemid 28400037)
    • (1998) Immunity , vol.9 , Issue.2 , pp. 239-246
    • Zhang, W.1    Trible, R.P.2    Samelson, L.E.3
  • 77
    • 0032856990 scopus 로고    scopus 로고
    • Localization of LAT in glycolipid-enriched microdomains is required for T cell activation
    • Lin J, Weiss A & Finco TS (1999) Localization of LAT in glycolipid-enriched microdomains is required for T cell activation. J Biol Chem 274, 28861-28864.
    • (1999) J Biol Chem , vol.274 , pp. 28861-28864
    • Lin, J.1    Weiss, A.2    Finco, T.S.3
  • 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 (2000) 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 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
    • 0037047336 scopus 로고    scopus 로고
    • LAT displacement from lipid rafts as a molecular mechanism for the inhibition of T cell signaling by polyunsaturated fatty acids
    • DOI 10.1074/jbc.M203343200
    • Zeyda M, Staffler G, Horejsi V, Waldhausl W & Stulnig TM (2002) LAT displacement from lipid rafts as a molecular mechanism for the inhibition of T cell signaling by polyunsaturated fatty acids. J Biol Chem 277, 28418-28423. (Pubitemid 41079265)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.32 , pp. 28418-28423
    • Zeyda, M.1    Staffler, G.2    Horejsi, V.3    Waldhausl, W.4    Stulnig, T.M.5
  • 80
    • 33646568738 scopus 로고    scopus 로고
    • Impaired Activation and Localization of LAT in Anergic T Cells as a Consequence of a Selective Palmitoylation Defect
    • DOI 10.1016/j.immuni.2006.03.011, PII S1074761306002093
    • Hundt M, Tabata H, Jeon MS, Hayashi K, Tanaka Y, Krishna R, De Giorgio L, Liu YC, Fukata M & Altman A (2006) Impaired activation and localization of LAT in anergic T cells as a consequence of a selective palmitoylation defect. Immunity 24, 513-522. (Pubitemid 43728146)
    • (2006) Immunity , vol.24 , Issue.5 , pp. 513-522
    • Hundt, M.1    Tabata, H.2    Jeon, M.-S.3    Hayashi, K.4    Tanaka, Y.5    Krishna, R.6    De, G.L.7    Liu, Y.-C.8    Fukata, M.9    Altman, A.10
  • 81
    • 0035083283 scopus 로고    scopus 로고
    • A soluble LAT deletion mutant inhibits T-cell activation: Reduced recruitment of signalling molecules to glycolipid-enriched microdomains
    • DOI 10.1016/S0898-6568(01)00131-0, PII S0898656801001310
    • Torgersen KM, Vaage JT, Rolstad B & Tasken K (2001) A soluble LAT deletion mutant inhibits T-cell activation: reduced recruitment of signalling molecules to glycolipid-enriched microdomains. Cell Signal 13, 213-220. (Pubitemid 32244406)
    • (2001) Cellular Signalling , vol.13 , Issue.3 , pp. 213-220
    • Torgersen, K.M.1    Vaage, J.T.2    Rolstad, B.3    Tasken, K.4
  • 84
    • 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 (2005) Cutting edge: localization of linker for activation of T cells to lipid rafts is not essential in T cell activation and development. J Immunol 174, 31-35. (Pubitemid 40007388)
    • (2005) Journal of Immunology , vol.174 , Issue.1 , pp. 31-35
    • Zhu, M.1    Shen, S.2    Liu, Y.3    Granillo, O.4    Zhang, W.5
  • 86
    • 0033571795 scopus 로고    scopus 로고
    • Association of the adaptor molecule LAT with CD4 and CD8 coreceptors identifies a new coreceptor function in T cell receptor signal transduction
    • Bosselut R, Zhang W, Ashe JM, Kopacz JL, Samelson LE & Singer A (1999) Association of the adaptor molecule LAT with CD4 and CD8 coreceptors identifies a new coreceptor function in T cell receptor signal transduction. J Exp Med 190, 1517-1526.
    • (1999) J Exp Med , vol.190 , pp. 1517-1526
    • Bosselut, R.1    Zhang, W.2    Ashe, J.M.3    Kopacz, J.L.4    Samelson, L.E.5    Singer, A.6
  • 87
    • 65649098764 scopus 로고    scopus 로고
    • The coreceptor CD2 uses plasma membrane microdomains to transduce signals in T cells
    • Kaizuka Y, Douglass AD, Vardhana S, Dustin ML & Vale RD (2009) The coreceptor CD2 uses plasma membrane microdomains to transduce signals in T cells. J Cell Biol 185, 521-534.
    • (2009) J Cell Biol , vol.185 , pp. 521-534
    • Kaizuka, Y.1    Douglass, A.D.2    Vardhana, S.3    Dustin, M.L.4    Vale, R.D.5
  • 88
    • 0034665654 scopus 로고    scopus 로고
    • Signaling via LAT (linker for T-cell activation) and Syk? ZAP70 is required for ERK activation and NFAT transcriptional activation following CD2 stimulation
    • Martelli MP, Lin H, Zhang W, Samelson LE & Bierer BE (2000) Signaling via LAT (linker for T-cell activation) and Syk ? ZAP70 is required for ERK activation and NFAT transcriptional activation following CD2 stimulation. Blood 96, 2181-2190.
    • (2000) Blood , vol.96 , pp. 2181-2190
    • Martelli, M.P.1    Lin, H.2    Zhang, W.3    Samelson, L.E.4    Bierer, B.E.5
  • 90
    • 11244321555 scopus 로고    scopus 로고
    • EphrinB1 is essential in T-cell-T-cell co-operation during T-cell activation
    • DOI 10.1074/jbc.M410814200
    • Yu G, Luo H, Wu Y & Wu J (2004) EphrinB1 is essential in T-cell-T-cell co-operation during T-cell activation. J Biol Chem 279, 55531-55539. (Pubitemid 40066555)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.53 , pp. 55531-55539
    • Yu, G.1    Luo, H.2    Wu, Y.3    Wu, J.4
  • 91
    • 67649559489 scopus 로고    scopus 로고
    • A new function for LAT and CD8 during CD8-mediated apoptosis that is independent of TCR signal transduction
    • Clarke RL, Thiemann S, Refaeli Y, Werlen G & Potter TA (2009) A new function for LAT and CD8 during CD8-mediated apoptosis that is independent of TCR signal transduction. Eur J Immunol 39, 1619-1631.
    • (2009) Eur J Immunol , vol.39 , pp. 1619-1631
    • Clarke, R.L.1    Thiemann, S.2    Refaeli, Y.3    Werlen, G.4    Potter, T.A.5
  • 92
    • 33847624931 scopus 로고    scopus 로고
    • CXCR3-mediated T-cell chemotaxis involves ZAP-70 and is regulated by signalling through the T-cell receptor
    • DOI 10.1111/j.1365-2567.2006.02534.x
    • Dar WA & Knechtle SJ (2007) CXCR3-mediated T-cell chemotaxis involves ZAP-70 and is regulated by signalling through the T-cell receptor. Immunology 120, 467-485. (Pubitemid 46365016)
    • (2007) Immunology , vol.120 , Issue.4 , pp. 467-485
    • Dar, W.A.1    Knechtle, S.J.2
  • 93
    • 0032933558 scopus 로고    scopus 로고
    • TCR activation inhibits chemotaxis toward stromal cell-derived factor- 1: Evidence for reciprocal regulation between CXCR4 and the TCR
    • Peacock JW & Jirik FR (1999) TCR activation inhibits chemotaxis toward stromal cell-derived factor-1: evidence for reciprocal regulation between CXCR4 and the TCR. J Immunol 162, 215-223. (Pubitemid 29018923)
    • (1999) Journal of Immunology , vol.162 , Issue.1 , pp. 215-223
    • Peacock, J.W.1    Jirik, F.R.2
  • 94
    • 0242720665 scopus 로고    scopus 로고
    • Rapamycin antagonizes cyclosporin A- And tacrolimus (FK506)-mediated augmentation of linker for activation of T cell expression in T cells
    • DOI 10.1093/intimm/dxg138
    • Cho CS, Chang Z, Elkahwaji J, Scheunemann TL, Manthei ER, Colburn M, Knechtle SJ & Hamawy MM (2003) Rapamycin antagonizes cyclosporin A- and tacrolimus (FK506)-mediated augmentation of linker for activation of T cell expression in T cells. Int Immunol 15, 1369-1378. (Pubitemid 37369330)
    • (2003) International Immunology , vol.15 , Issue.11 , pp. 1369-1378
    • Cho, C.S.1    Chang, Z.2    Elkahwaji, J.3    Scheunemann, T.L.4    Manthei, E.R.5    Colburn, M.6    Knechtle, S.J.7    Hamawy, M.M.8
  • 96
    • 33846231873 scopus 로고    scopus 로고
    • Negative Regulation of T Cell Activation and Autoimmunity by the Transmembrane Adaptor Protein LAB
    • DOI 10.1016/j.immuni.2006.08.025, PII S1074761306004699
    • Zhu M, Koonpaew S, Liu Y, Shen S, Denning T, Dzhagalov I, Rhee I & Zhang W(2006) Negative regulation of T cell activation and autoimmunity by the transmembrane adaptor protein LAB. Immunity 25, 757-768. (Pubitemid 46107283)
    • (2006) Immunity , vol.25 , Issue.5 , pp. 757-768
    • Zhu, M.1    Koonpaew, S.2    Liu, Y.3    Shen, S.4    Denning, T.5    Dzhagalov, I.6    Rhee, I.7    Zhang, W.8
  • 98
    • 0033564933 scopus 로고    scopus 로고
    • Perturbed regulation of ZAP-70 and sustained tyrosine phosphorylation of LAT and SLP-76 in c-CBL-deficient thymocytes
    • Thien CB, Bowtell DD & Langdon WY (1999) Perturbed regulation of ZAP-70 and sustained tyrosine phosphorylation of LAT and SLP-76 in c-Cbl-deficient thymocytes. J Immunol 162, 7133-7139. (Pubitemid 29277683)
    • (1999) Journal of Immunology , vol.162 , Issue.12 , pp. 7133-7139
    • Thien, C.B.F.1    Bowtell, D.D.L.2    Langdon, W.Y.3
  • 100
    • 0032212728 scopus 로고    scopus 로고
    • LAT is required for TCR-mediated activation of PLCgamma1 and the Ras pathway
    • Finco TS, Kadlecek T, Zhang W, Samelson LE & Weiss A (1998) LAT is required for TCR-mediated activation of PLCgamma1 and the Ras pathway. Immunity 9, 617-626. (Pubitemid 28557590)
    • (1998) Immunity , vol.9 , Issue.5 , pp. 617-626
    • Finco, T.S.1    Kadlecek, T.2    Zhang, W.3    Samelson, L.E.4    Weiss, A.5
  • 101
    • 0032992072 scopus 로고    scopus 로고
    • Functional analysis of LAT in TCR-mediated signaling pathways using a LAT-deficient Jurkat cell line
    • DOI 10.1093/intimm/11.6.943
    • Zhang W, Irvin BJ, Trible RP, Abraham RT & Samelson LE (1999) Functional analysis of LAT in TCR-mediated signaling pathways using a LAT-deficient Jurkat cell line. Int Immunol 11, 943-950. (Pubitemid 29276606)
    • (1999) International Immunology , vol.11 , Issue.6 , pp. 943-950
    • Zhang, W.1    Irvin, B.J.2    Trible, R.P.3    Abraham, R.T.4    Samelson, L.E.5
  • 102
    • 0035898379 scopus 로고    scopus 로고
    • Knock-in mutation of the distal four tyrosines of linker for activation of T cells blocks murine T cell development
    • DOI 10.1084/jem.194.2.135
    • Sommers CL, Menon RK, Grinberg A, Zhang W, Samelson LE & Love PE (2001) Knock-in mutation of the distal four tyrosines of linker for activation of T cells blocks murine T cell development. J Exp Med 194, 135-142. (Pubitemid 32673346)
    • (2001) Journal of Experimental Medicine , vol.194 , Issue.2 , pp. 135-142
    • Sommers, C.L.1    Menon, R.K.2    Grinberg, A.3    Zhang, W.4    Samelson, L.E.5    Love, P.E.6
  • 110
    • 77951902637 scopus 로고    scopus 로고
    • The role of the LAT-PLC-γ1 interaction in T regulatory cell function
    • Chuck MI, Zhu M, Shen S & Zhang W (2010) The role of the LAT-PLC-γ1 interaction in T regulatory cell function. J Immunol 184, 2476-2486.
    • (2010) J Immunol , vol.184 , pp. 2476-2486
    • Chuck, M.I.1    Zhu, M.2    Shen, S.3    Zhang, W.4
  • 111
  • 113
    • 33750530393 scopus 로고    scopus 로고
    • T cell receptor for antigen induces linker for activation of T cell-dependent activation of a negative signaling complex involving Dok-2, SHIP-1, and Grb-2
    • DOI 10.1084/jem.20060650
    • Dong S, Corre B, Foulon E, Dufour E, Veillette A, Acuto O & Michel F (2006) T cell receptor for antigen induces linker for activation of T cell-dependent activation of a negative signaling complex involving Dok-2, SHIP-1, and Grb-2. J Exp Med 203, 2509-2518. (Pubitemid 44664620)
    • (2006) Journal of Experimental Medicine , vol.203 , Issue.11 , pp. 2509-2518
    • Dong, S.1    Corre, B.2    Foulon, E.3    Dufour, E.4    Veillette, A.5    Acuto, O.6    Michel, F.7
  • 114
    • 0034948374 scopus 로고    scopus 로고
    • Involvement of SHP-1 tyrosine phosphatase in TCR-Mediated signaling pathways in lipid rafts
    • DOI 10.1016/S1074-7613(01)00146-7
    • Kosugi A, Sakakura J, Yasuda K, Ogata M & Hamaoka T (2001) Involvement of SHP-1 tyrosine phosphatase in TCR-mediated signaling pathways in lipid rafts. Immunity 14, 669-680. (Pubitemid 32592415)
    • (2001) Immunity , vol.14 , Issue.6 , pp. 669-680
    • Kosugi, A.1    Sakakura, J.2    Yasuda, K.3    Ogata, M.4    Hamaoka, T.5
  • 115
    • 3342912122 scopus 로고    scopus 로고
    • Negative feedback loop in T-cell activation through MAPK-catalyzed threonine phosphorylation of LAT
    • DOI 10.1038/sj.emboj.7600268
    • Matsuda S, Miwa Y, Hirata Y, Minowa A, Tanaka J, Nishida E & Koyasu S (2004) Negative feedback loop in T-cell activation through MAPK-catalyzed threonine phosphorylation of LAT. EMBO J 23, 2577-2585. (Pubitemid 38988229)
    • (2004) EMBO Journal , vol.23 , Issue.13 , pp. 2577-2585
    • Matsuda, S.1    Miwa, Y.2    Hirata, Y.3    Minowa, A.4    Tanaka, J.5    Nishida, E.6    Koyasu, S.7
  • 116
    • 0035976967 scopus 로고    scopus 로고
    • Docking protein Gab2 is phosphorylated by ZAP-70 and negatively regulates T cell receptor signaling by recruitment of inhibitory molecules
    • Yamasaki S, Nishida K, Hibi M, Sakuma M, Shiina R, Takeuchi A, Ohnishi H, Hirano T & Saito T (2001) Docking protein Gab2 is phosphorylated by ZAP-70 and negatively regulates T cell receptor signaling by recruitment of inhibitory molecules. J Biol Chem 276, 45175-45183.
    • (2001) J Biol Chem , vol.276 , pp. 45175-45183
    • Yamasaki, S.1    Nishida, K.2    Hibi, M.3    Sakuma, M.4    Shiina, R.5    Takeuchi, A.6    Ohnishi, H.7    Hirano, T.8    Saito, T.9
  • 117
    • 0037379218 scopus 로고    scopus 로고
    • Gads/Grb2-mediated association with LAT is critical for the inhibitory function of Gab2 in T cells
    • DOI 10.1128/MCB.23.7.2515-2529.2003
    • Yamasaki S, Nishida K, Sakuma M, Berry D, McGlade CJ, Hirano T & Saito T (2003) Gads/Grb2-mediated association with LAT is critical for the inhibitory function of Gab2 in T cells. Mol Cell Biol 23, 2515-2529. (Pubitemid 36351031)
    • (2003) Molecular and Cellular Biology , vol.23 , Issue.7 , pp. 2515-2529
    • Yamasaki, S.1    Nishida, K.2    Sakuma, M.3    Berry, D.4    McGlade, C.J.5    Hirano, T.6    Saito, T.7
  • 119
    • 0000633068 scopus 로고    scopus 로고
    • Evidence that phospholipase C-γ2 interacts with SLP-76, Syk, Lyn, LAT and the Fc receptor gamma-chain after stimulation of the collagen receptor glycoprotein VI in human platelets
    • DOI 10.1046/j.1432-1327.1999.00560.x
    • Gross BS, Melford SK & Watson SP (1999) Evidence that phospholipase C-γ2 interacts with SLP-76, Syk, Lyn, LAT and the Fc receptor gamma-chain after stimulation of the collagen receptor glycoprotein VI in human platelets. Eur J Biochem 263, 612-623. (Pubitemid 29361933)
    • (1999) European Journal of Biochemistry , vol.263 , Issue.3 , pp. 612-623
    • Gross, B.S.1    Melford, S.K.2    Watson, S.P.3
  • 120
    • 0034721865 scopus 로고    scopus 로고
    • Interaction of linker for activation of T cells with multiple adapter proteins in platelets activated by the glycoprotein VI-selective ligand, convulxin
    • Asazuma N, Wilde JI, Berlanga O, Leduc M, Leo A, Schweighoffer E, Tybulewicz V, Bon C, Liu SK, McGlade CJ et al. (2000) Interaction of linker for activation of T cells with multiple adapter proteins in platelets activated by the glycoprotein VI-selective ligand, convulxin. J Biol Chem 275, 33427-33434.
    • (2000) J Biol Chem , vol.275 , pp. 33427-33434
    • Asazuma, N.1    Wilde, J.I.2    Berlanga, O.3    Leduc, M.4    Leo, A.5    Schweighoffer, E.6    Tybulewicz, V.7    Bon, C.8    Liu, S.K.9    McGlade, C.J.10
  • 123
  • 124
    • 34948891046 scopus 로고    scopus 로고
    • Roles of the C-terminal tyrosine residues of LAT in GPVI-induced platelet activation: Insights into the mechanism of PLCγ2 activation
    • DOI 10.1182/blood-2007-02-075432
    • Ragab A, Severin S, Gratacap MP, Aguado E, Malissen M, Jandrot-Perrus M, Malissen B, Ragab-Thomas J & Payrastre B (2007) Roles of the C-terminal tyrosine residues of LAT in GPVI-induced platelet activation: insights into the mechanism of PLC γ 2 activation. Blood 110, 2466-2474. (Pubitemid 47523168)
    • (2007) Blood , vol.110 , Issue.7 , pp. 2466-2474
    • Ragab, A.1    Severin, S.2    Gratacap, M.-P.3    Aguado, E.4    Malissen, M.5    Jandrot-Perrus, M.6    Malissen, B.7    Ragab-Thomas, J.8    Payrastre, B.9
  • 125
    • 34547134973 scopus 로고    scopus 로고
    • Diverging signaling events control the pathway of GPVI down-regulation in vivo
    • DOI 10.1182/blood-2006-11-058107
    • Rabie T, Varga-Szabo D, Bender M, Pozgaj R, Lanza F, Saito T, Watson SP & Nieswandt B (2007) Diverging signaling events control the pathway of GPVI down-regulation in vivo. Blood 110, 529-535. (Pubitemid 47105390)
    • (2007) Blood , vol.110 , Issue.2 , pp. 529-535
    • Rabie, T.1    Varga-Szabo, D.2    Bender, M.3    Pozgaj, R.4    Lanza, F.5    Saito, T.6    Watson, S.P.7    Nieswandt, B.8
  • 126
    • 0037323803 scopus 로고    scopus 로고
    • A critical role of lipid rafts in the organization of a key FcγRIIa-mediated signaling pathway in human platelets
    • Bodin S, Viala C, Ragab A & Payrastre B (2003) A critical role of lipid rafts in the organization of a key FcγRIIa-mediated signaling pathway in human platelets. Thromb Haemost 89, 318-330. (Pubitemid 36230872)
    • (2003) Thrombosis and Haemostasis , vol.89 , Issue.2 , pp. 318-330
    • Bodin, S.1    Viala, C.2    Ragab, A.3    Payrastre, B.4
  • 127
    • 18844444812 scopus 로고    scopus 로고
    • 3
    • DOI 10.1160/TH04-08-0482
    • Pampolina C & McNicol A (2005) Streptococcus sanguis- induced platelet activation involves two waves of tyrosine phosphorylation mediated by FcγRIIA and αIIβ3. Thromb Haemost 93, 932-939. (Pubitemid 40691553)
    • (2005) Thrombosis and Haemostasis , vol.93 , Issue.5 , pp. 932-939
    • Pampolina, C.1    McNicol, A.2
  • 129
    • 1542284643 scopus 로고    scopus 로고
    • The heptapeptide LSARLAF mediates platelet activation through phospholipase Cγ2 independently of glycoprotein IIb-IIIa
    • DOI 10.1042/BJ20031298
    • Pearce AC, Wonerow P, Marshall SJ, Frampton J, Gartner TK & Watson SP (2004) The heptapeptide LSARLAF mediates platelet activation through phospholipase Cγ2 independently of glycoprotein IIb-IIIa. Biochem J 378, 193-199. (Pubitemid 38299557)
    • (2004) Biochemical Journal , vol.378 , Issue.1 , pp. 193-199
    • Pearce, A.C.1    Wonerow, P.2    Marshall, S.J.3    Frampton, J.4    Gartner, T.K.5    Watson, S.P.6
  • 130
    • 0032426644 scopus 로고    scopus 로고
    • Tyrosine phosphorylation and translocation of LAT in platelets
    • Sarkar S (1998) Tyrosine phosphorylation and translocation of LAT in platelets. FEBS Lett 441, 357-360.
    • (1998) FEBS Lett , vol.441 , pp. 357-360
    • Sarkar, S.1
  • 131
    • 0141673312 scopus 로고    scopus 로고
    • Platelet aggregation induced by the C-terminal peptide of thrombospondin-1 requires the docking protein LAT but is largely independent of αIIb/β3
    • Trumel C, Plantavid M, Levy-Toledano S, Ragab A, Caen JP, Aguado E, Malissen B & Payrastre B (2003) Platelet aggregation induced by the C-terminal peptide of thrombospondin-1 requires the docking protein LAT but is largely independent of αIIb/β3. J Thromb Haemost 1, 320-329.
    • (2003) J Thromb Haemost , vol.1 , pp. 320-329
    • Trumel, C.1    Plantavid, M.2    Levy-Toledano, S.3    Ragab, A.4    Caen, J.P.5    Aguado, E.6    Malissen, B.7    Payrastre, B.8
  • 132
    • 0142135123 scopus 로고    scopus 로고
    • The tyrosine phosphatase 1B regulates LAT phosphorylation and platelet aggregation upon Fcγ RIIa cross-linking
    • Ragab A, Bodin S, Viala C, Chap H, Payrastre B & Ragab-Thomas J (2003) The tyrosine phosphatase 1B regulates LAT phosphorylation and platelet aggregation upon Fcγ RIIa cross-linking. J Biol Chem 278, 40923-40932.
    • (2003) J Biol Chem , vol.278 , pp. 40923-40932
    • Ragab, A.1    Bodin, S.2    Viala, C.3    Chap, H.4    Payrastre, B.5    Ragab-Thomas, J.6
  • 133
    • 34548815900 scopus 로고    scopus 로고
    • The low-molecular-weight phosphotyrosine phosphatase is a negative regulator of FcγRIIA-mediated cell activation
    • DOI 10.1182/blood-2007-03-081414
    • Mancini F, Rigacci S, Berti A, Balduini C & Torti M (2007) The low-molecular-weight phosphotyrosine phosphatase is a negative regulator of FcγRIIA-mediated cell activation. Blood 110, 1871-1878. (Pubitemid 47443899)
    • (2007) Blood , vol.110 , Issue.6 , pp. 1871-1878
    • Mancini, F.1    Rigacci, S.2    Berti, A.3    Balduini, C.4    Torti, M.5
  • 134
    • 73249132352 scopus 로고    scopus 로고
    • Both FcγRIV and FcγRIII are essential receptors mediating type II and type III autoimmune responses via FcRgamma-LAT-dependent generation of C5a
    • Syed SN, Konrad S, Wiege K, Nieswandt B, Nimmerjahn F, Schmidt RE & Gessner JE (2009) Both FcγRIV and FcγRIII are essential receptors mediating type II and type III autoimmune responses via FcRgamma-LAT-dependent generation of C5a. Eur J Immunol 39, 3343-3356.
    • (2009) Eur J Immunol , vol.39 , pp. 3343-3356
    • Syed, S.N.1    Konrad, S.2    Wiege, K.3    Nieswandt, B.4    Nimmerjahn, F.5    Schmidt, R.E.6    Gessner, J.E.7
  • 135
    • 71749113673 scopus 로고    scopus 로고
    • Leukocyte Ig-like receptor B4 (LIL-RB4) is a potent inhibitor of FcγRI-mediated monocyte activation via dephosphorylation of multiple kinases
    • Lu HK, Rentero C, Raftery MJ, Borges L, Bryant K & Tedla N (2009) Leukocyte Ig-like receptor B4 (LIL-RB4) is a potent inhibitor of FcγRI-mediated monocyte activation via dephosphorylation of multiple kinases. J Biol Chem 284, 34839-34848.
    • (2009) J Biol Chem , vol.284 , pp. 34839-34848
    • Lu, H.K.1    Rentero, C.2    Raftery, M.J.3    Borges, L.4    Bryant, K.5    Tedla, N.6
  • 138
    • 33947277244 scopus 로고    scopus 로고
    • Kinetic proofreading of ligand-FcepsilonRI interactions may persist beyond LAT phosphorylation
    • Torigoe C, Faeder JR, Oliver JM & Goldstein B (2007) Kinetic proofreading of ligand-FcεRI interactions may persist beyond LAT phosphorylation. J Immunol 178, 3530-3535. (Pubitemid 46417618)
    • (2007) Journal of Immunology , vol.178 , Issue.6 , pp. 3530-3535
    • Torigoe, C.1    Faeder, J.R.2    Oliver, J.M.3    Goldstein, B.4
  • 139
    • 77954136683 scopus 로고    scopus 로고
    • Phospholipase δ promotes lipid microdomain-associated signaling events in mast cells
    • Lisboa FA, Peng Z, Combs CA & Beaven MA (2009) Phospholipase δ promotes lipid microdomain-associated signaling events in mast cells. J Immunol 183, 5104-5112.
    • (2009) J Immunol , vol.183 , pp. 5104-5112
    • Lisboa, F.A.1    Peng, Z.2    Combs, C.A.3    Beaven, M.A.4
  • 140
    • 71349083703 scopus 로고    scopus 로고
    • Non-T cell activation linker regulates ERK activation in Helicobacter pylori-infected epithelial cells
    • Rieke C, Kahne T, Schweitzer K, Schraven B, Wienands J, Engelke M & Naumann M (2010) Non-T cell activation linker regulates ERK activation in Helicobacter pylori-infected epithelial cells. Cell Signal 22, 395-403.
    • (2010) Cell Signal , vol.22 , pp. 395-403
    • Rieke, C.1    Kahne, T.2    Schweitzer, K.3    Schraven, B.4    Wienands, J.5    Engelke, M.6    Naumann, M.7
  • 141
    • 0035817631 scopus 로고    scopus 로고
    • High resolution mapping of mast cell membranes reveals primary and secondary domains of FcεRI and LAT
    • DOI 10.1083/jcb.200104049
    • Wilson BS, Pfeiffer JR, Surviladze Z, Gaudet EA & Oliver JM (2001) High resolution mapping of mast cell membranes reveals primary and secondary domains of FcεRI and LAT. J Cell Biol 154, 645-658. (Pubitemid 34286168)
    • (2001) Journal of Cell Biology , vol.154 , Issue.3 , pp. 645-658
    • Wilson, B.S.1    Pfeiffer, J.R.2    Surviladze, Z.3    Gaudet, E.A.4    Oliver, J.M.5
  • 142
    • 34250192556 scopus 로고    scopus 로고
    • LAT and NTAL mediate immunoglobulin E-induced sustained extracellular signal-regulated kinase activation critical for mast cell survival
    • DOI 10.1128/MCB.02109-06
    • Yamasaki S, Ishikawa E, Sakuma M, Kanagawa O, Cheng AM, Malissen B & Saito T (2007) LAT and NTAL mediate immunoglobulin E-induced sustained extracellular signal-regulated kinase activation critical for mast cell survival. Mol Cell Biol 27, 4406-4415. (Pubitemid 46906564)
    • (2007) Molecular and Cellular Biology , vol.27 , Issue.12 , pp. 4406-4415
    • Yamasaki, S.1    Ishikawa, E.2    Sakuma, M.3    Kanagawa, O.4    Cheng, A.M.5    Malissen, B.6    Saito, T.7
  • 147
    • 0034528476 scopus 로고    scopus 로고
    • Analysis of the molecular mechanism involved in 2B4-mediated NK cell activation: Evidence that human 2B4 is physically and functionally associated with the linker for activation of T cells
    • DOI 10.1002/1521-4141(200012)30:12<3718::AID-IMMU3718>3.0.CO;2-I
    • Bottino C, Augugliaro R, Castriconi R, Nanni M, Biassoni R, Moretta L & Moretta A (2000) Analysis of the molecular mechanism involved in 2B4-mediated NK cell activation: evidence that human 2B4 is physically and functionally associated with the linker for activation of T cells. Eur J Immunol 30, 3718-3722. (Pubitemid 32005246)
    • (2000) European Journal of Immunology , vol.30 , Issue.12 , pp. 3718-3722
    • Bottino, C.1    Augugliaro, R.2    Castriconi, R.3    Nanni, M.4    Biassoni, R.5    Moretta, L.6    Moretta, A.7
  • 148
    • 0036644060 scopus 로고    scopus 로고
    • 2B4 is constitutively associated with linker for the activation of T cells in glycolipid-enriched microdomains: Properties required for 2B4 lytic function
    • Klem J, Verrett PC, Kumar V & Schatzle JD (2002) 2B4 is constitutively associated with linker for the activation of T cells in glycolipid-enriched microdomains: properties required for 2B4 lytic function. J Immunol 169, 55-62. (Pubitemid 34686119)
    • (2002) Journal of Immunology , vol.169 , Issue.1 , pp. 55-62
    • Klem, J.1    Verrett, P.C.2    Kumar, V.3    Schatzle, J.D.4
  • 149
    • 0035575998 scopus 로고    scopus 로고
    • 2B4 (CD244)-mediated activation of cytotoxicity and IFN-γ release in human NK cells involves distinct pathways
    • Chuang SS, Kumaresan PR & Mathew PA (2001) 2B4 (CD244)-mediated activation of cytotoxicity and IFN-γ release in human NK cells involves distinct pathways. J Immunol 167, 6210-6216. (Pubitemid 33081549)
    • (2001) Journal of Immunology , vol.167 , Issue.11 , pp. 6210-6216
    • Chuang, S.S.1    Kumaresan, P.R.2    Mathew, P.A.3
  • 150
    • 53449085186 scopus 로고    scopus 로고
    • Analysis of the linker for activation of T cells and the linker for activation of B cells in natural killer cells reveals a novel signaling cassette, dual usage in ITAM signaling, and influence on development of the Ly49 repertoire
    • Whittaker GC, Burshtyn DN, Orr SJ, Quigley L, Hodge DL, Pascal V, Zhang W & McVicar DW (2008) Analysis of the linker for activation of T cells and the linker for activation of B cells in natural killer cells reveals a novel signaling cassette, dual usage in ITAM signaling, and influence on development of the Ly49 repertoire. Blood 112, 2869-2877.
    • (2008) Blood , vol.112 , pp. 2869-2877
    • Whittaker, G.C.1    Burshtyn, D.N.2    Orr, S.J.3    Quigley, L.4    Hodge, D.L.5    Pascal, V.6    Zhang, W.7    McVicar, D.W.8
  • 151
    • 0034933795 scopus 로고    scopus 로고
    • Association of SLP-65/BLNK with the B cell antigen receptor through a non-ITAM tyrosine of Ig-α
    • DOI 10.1002/1521-4141(200107)31:7<2126::AID-IMMU2126>3.0.CO;2-O
    • Engels N, Wollscheid B & Wienands J (2001) Association of SLP-65/BLNK with the B cell antigen receptor through a non-ITAM tyrosine of Ig-α. Eur J Immunol 31, 2126-2134. (Pubitemid 32640729)
    • (2001) European Journal of Immunology , vol.31 , Issue.7 , pp. 2126-2134
    • Engels, N.1    Wollscheid, B.2    Wienands, J.3
  • 152
    • 33846908740 scopus 로고    scopus 로고
    • The N terminus of the Non-T cell Activation Linker (NTAL) confers inhibitory effects on Pre-B cell differentiation
    • Herzog S & Jumaa H (2007) The N terminus of the non-T cell activation linker (NTAL) confers inhibitory effects on pre-B cell differentiation. J Immunol 178, 2336-2343. (Pubitemid 46233432)
    • (2007) Journal of Immunology , vol.178 , Issue.4 , pp. 2336-2343
    • Herzog, S.1    Jumaa, H.2
  • 153
    • 10944220653 scopus 로고    scopus 로고
    • The molecular requirements for LAT-mediated differentiation and the role of LAT in limiting pre-B cell expansion
    • DOI 10.1002/eji.200425445
    • Su YW, Herzog S, Lotz M, Feldhahn N, Muschen M & Jumaa H (2004) The molecular requirements for LAT-mediated differentiation and the role of LAT in limiting pre-B cell expansion. Eur J Immunol 34, 3614-3622. (Pubitemid 40012179)
    • (2004) European Journal of Immunology , vol.34 , Issue.12 , pp. 3614-3622
    • Su, Y.-W.1    Herzog, S.2    Lotz, M.3    Feldhahn, N.4    Muschen, M.5    Jumaa, H.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.