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Volumn 228, Issue 1, 2009, Pages 288-311

CD45, CD148, and Lyp/Pep: Critical phosphatases regulating Src family kinase signaling networks in immune cells

Author keywords

Autoimmunity; CD148; CD45; Pep Lyp; Phosphatase; PTPN22

Indexed keywords

CD45 ANTIGEN; PHOSPHATASE; PROTEIN TYROSINE KINASE;

EID: 61849136595     PISSN: 01052896     EISSN: 1600065X     Source Type: Journal    
DOI: 10.1111/j.1600-065X.2008.00752.x     Document Type: Article
Times cited : (137)

References (175)
  • 1
    • 50249105938 scopus 로고    scopus 로고
    • Tailoring T-cell receptor signals by proximal negative feedback mechanisms
    • Acuto O, Bartolo VD, Michel F. Tailoring T-cell receptor signals by proximal negative feedback mechanisms. Nat Rev Immunol 2008 8 : 699 712.
    • (2008) Nat Rev Immunol , vol.8 , pp. 699-712
    • Acuto, O.1    Bartolo, V.D.2    Michel, F.3
  • 2
    • 0036143017 scopus 로고    scopus 로고
    • Reciprocal regulation of lymphocyte activation by tyrosine kinases and phosphatases
    • Hermiston ML, Xu Z, Majeti R, Weiss A. Reciprocal regulation of lymphocyte activation by tyrosine kinases and phosphatases. J Clin Invest 2002 109 : 9 14.
    • (2002) J Clin Invest , vol.109 , pp. 9-14
    • Hermiston, M.L.1    Xu, Z.2    Majeti, R.3    Weiss, A.4
  • 4
    • 3042615397 scopus 로고    scopus 로고
    • Src-family kinases: Rheostats of immune cell signaling
    • Lowell CA. Src-family kinases: rheostats of immune cell signaling. Mol Immunol 2004 41 : 631 643.
    • (2004) Mol Immunol , vol.41 , pp. 631-643
    • Lowell, C.A.1
  • 5
    • 7944231534 scopus 로고    scopus 로고
    • Function of the Src-family kinases, Lck and Fyn, in T-cell development and activation
    • Palacios EH, Weiss A. Function of the Src-family kinases, Lck and Fyn, in T-cell development and activation. Oncogene 2004 23 : 7990 8000.
    • (2004) Oncogene , vol.23 , pp. 7990-8000
    • Palacios, E.H.1    Weiss, A.2
  • 6
    • 0035815288 scopus 로고    scopus 로고
    • Dynamic coupling between the SH2 and SH3 domains of c-Src and Hck underlies their inactivation by C-terminal tyrosine phosphorylation
    • Young MA, Gonfloni S, Superti-Furga G, Roux B, Kuriyan J. Dynamic coupling between the SH2 and SH3 domains of c-Src and Hck underlies their inactivation by C-terminal tyrosine phosphorylation. Cell 2001 105 : 115 126.
    • (2001) Cell , vol.105 , pp. 115-126
    • Young, M.A.1    Gonfloni, S.2    Superti-Furga, G.3    Roux, B.4    Kuriyan, J.5
  • 7
    • 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, Mustelin T. A weak Lck tail bite is necessary for Lck function in T cell antigen receptor signaling. J Biol Chem 2007 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
  • 8
    • 0027389272 scopus 로고
    • CD45 specifically modulates binding of Lck to a phosphopeptide encompassing the negative regulatory tyrosine of Lck
    • Sieh M, Bolen JB, Weiss A. CD45 specifically modulates binding of Lck to a phosphopeptide encompassing the negative regulatory tyrosine of Lck. EMBO J 1993 12 : 315 322.
    • (1993) EMBO J , vol.12 , pp. 315-322
    • Sieh, M.1    Bolen, J.B.2    Weiss, A.3
  • 10
    • 0033200308 scopus 로고    scopus 로고
    • Positive and negative regulation of Src-family membrane kinases by CD45
    • Thomas ML, Brown EJ. Positive and negative regulation of Src-family membrane kinases by CD45. Immunol Today 1999 20 : 406 411.
    • (1999) Immunol Today , vol.20 , pp. 406-411
    • Thomas, M.L.1    Brown, E.J.2
  • 11
    • 33846903073 scopus 로고    scopus 로고
    • Changes in the role of the CD45 protein tyrosine phosphatase in regulating Lck tyrosine phosphorylation during thymic development
    • Falahati R, Leitenberg D. Changes in the role of the CD45 protein tyrosine phosphatase in regulating Lck tyrosine phosphorylation during thymic development. J Immunol 2007 178 : 2056 2064.
    • (2007) J Immunol , vol.178 , pp. 2056-2064
    • Falahati, R.1    Leitenberg, D.2
  • 12
    • 0023707353 scopus 로고
    • Differential expression of the leucocyte-common antigen family
    • Thomas ML, Lefrancois L. Differential expression of the leucocyte-common antigen family. Immunol Today 1988 9 : 320 326.
    • (1988) Immunol Today , vol.9 , pp. 320-326
    • Thomas, M.L.1    Lefrancois, L.2
  • 13
    • 0038815306 scopus 로고    scopus 로고
    • CD45: A critical regulator of signaling thresholds in immune cells
    • Hermiston ML, Xu Z, Weiss A. CD45: a critical regulator of signaling thresholds in immune cells. Annu Rev Immunol 2003 21 : 107 137.
    • (2003) Annu Rev Immunol , vol.21 , pp. 107-137
    • Hermiston, M.L.1    Xu, Z.2    Weiss, A.3
  • 14
    • 33645071581 scopus 로고    scopus 로고
    • CD45: All is not yet crystal clear
    • Holmes N. CD45: all is not yet crystal clear. Immunol 2006 117 : 145 155.
    • (2006) Immunol , vol.117 , pp. 145-155
    • Holmes, N.1
  • 15
    • 0033399264 scopus 로고    scopus 로고
    • Greatly reduced efficiency of both positive and negative selection of thymocytes in CD45 tyrosine phosphatase-deficient mice
    • Mee PJ, Turner M, Basson MA, Costello PS, Zamoyska R, Tybulewicz VL. Greatly reduced efficiency of both positive and negative selection of thymocytes in CD45 tyrosine phosphatase-deficient mice. Eur J Immunol 1999 29 : 2923 2933.
    • (1999) Eur J Immunol , vol.29 , pp. 2923-2933
    • Mee, P.J.1    Turner, M.2    Basson, M.A.3    Costello, P.S.4    Zamoyska, R.5    Tybulewicz, V.L.6
  • 16
    • 0029864147 scopus 로고    scopus 로고
    • CD45-null transgenic mice reveal a positive regulatory role for CD45 in early thymocyte development, in the selection of CD4+CD8+ thymocytes, and B cell maturation
    • Byth KF, et al. CD45-null transgenic mice reveal a positive regulatory role for CD45 in early thymocyte development, in the selection of CD4+CD8+ thymocytes, and B cell maturation. J Exp Med 1996 183 : 1707 1718.
    • (1996) J Exp Med , vol.183 , pp. 1707-1718
    • Byth, K.F.1
  • 17
    • 0027296521 scopus 로고
    • Normal B lymphocyte development but impaired T cell maturation in CD45-Exon6 protein tyrosine phosphatase-deficient mice
    • Kishihara K, et al. Normal B lymphocyte development but impaired T cell maturation in CD45-Exon6 protein tyrosine phosphatase-deficient mice. Cell 1993 74 : 143 156.
    • (1993) Cell , vol.74 , pp. 143-156
    • Kishihara, K.1
  • 19
    • 0034064779 scopus 로고    scopus 로고
    • Mutations in the tyrosine phosphatase CD45 gene in a child with severe combined immunodeficiency disease
    • Kung C, et al. Mutations in the tyrosine phosphatase CD45 gene in a child with severe combined immunodeficiency disease. Nat Med 2000 6 : 343 345.
    • (2000) Nat Med , vol.6 , pp. 343-345
    • Kung, C.1
  • 20
    • 33644557158 scopus 로고    scopus 로고
    • Altered CD45 expression and disease
    • Tchilian EZ, Beverley PC. Altered CD45 expression and disease. Trends Immunol 2006 27 : 146 153.
    • (2006) Trends Immunol , vol.27 , pp. 146-153
    • Tchilian, E.Z.1    Beverley, P.C.2
  • 21
    • 53249142239 scopus 로고    scopus 로고
    • CD45 Glycosylation controls T-cell life and death
    • Earl LA, Baum LG. CD45 Glycosylation controls T-cell life and death. Immunol Cell Biol 2008 86 : 608 615.
    • (2008) Immunol Cell Biol , vol.86 , pp. 608-615
    • Earl, L.A.1    Baum, L.G.2
  • 22
    • 34547813680 scopus 로고    scopus 로고
    • T-cell activation results in microheterogeneous changes in glycosylation of CD45
    • Hernandez JD, Klein J, Van Dyken SJ, Marth JD, Baum LG. T-cell activation results in microheterogeneous changes in glycosylation of CD45. Int Immunol 2007 19 : 847 856.
    • (2007) Int Immunol , vol.19 , pp. 847-856
    • Hernandez, J.D.1    Klein, J.2    Van Dyken, S.J.3    Marth, J.D.4    Baum, L.G.5
  • 23
    • 33750126191 scopus 로고    scopus 로고
    • Regulation of effector T cells by antigen-presenting cells via interaction of the C-type lectin MGL with CD45
    • van Vliet SJ, Gringhuis SI, Geijtenbeek TB, van Kooyk Y. Regulation of effector T cells by antigen-presenting cells via interaction of the C-type lectin MGL with CD45. Nat Immunol 2006 7 : 1200 1208.
    • (2006) Nat Immunol , vol.7 , pp. 1200-1208
    • Van Vliet, S.J.1    Gringhuis, S.I.2    Geijtenbeek, T.B.3    Van Kooyk, Y.4
  • 24
    • 36849040950 scopus 로고    scopus 로고
    • Lateral compartmentalization of T cell receptor versus CD45 by galectin-N-glycan binding and microfilaments coordinate basal and activation signaling
    • Chen IJ, Chen HL, Demetriou M. Lateral compartmentalization of T cell receptor versus CD45 by galectin-N-glycan binding and microfilaments coordinate basal and activation signaling. J Biol Chem 2007 282 : 35361 35372.
    • (2007) J Biol Chem , vol.282 , pp. 35361-35372
    • Chen, I.J.1    Chen, H.L.2    Demetriou, M.3
  • 25
    • 13644253773 scopus 로고    scopus 로고
    • Structural basis for the function and regulation of the receptor protein tyrosine phosphatase CD45
    • Nam HJ, Poy F, Saito H, Frederick CA. Structural basis for the function and regulation of the receptor protein tyrosine phosphatase CD45. J Exp Med 2005 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
  • 26
    • 0027981910 scopus 로고
    • The catalytic activity of the CD45 membrane-proximal phosphatase domain is required for TCR signaling and regulation
    • Desai DM, Sap J, Silvennoinen O, Schlessinger J, Weiss A. The catalytic activity of the CD45 membrane-proximal phosphatase domain is required for TCR signaling and regulation. EMBO J 1994 13 : 4002 4010.
    • (1994) EMBO J , vol.13 , pp. 4002-4010
    • Desai, D.M.1    Sap, J.2    Silvennoinen, O.3    Schlessinger, J.4    Weiss, A.5
  • 27
    • 0039846522 scopus 로고    scopus 로고
    • Phosphorylation of CD45 by casein kinase 2. Modulation of activity and mutational analysis
    • Wang Y, Guo W, Liang L, Esselman WJ. Phosphorylation of CD45 by casein kinase 2. Modulation of activity and mutational analysis. J Biol Chem 1999 274 : 7454 7461.
    • (1999) J Biol Chem , vol.274 , pp. 7454-7461
    • Wang, Y.1    Guo, W.2    Liang, L.3    Esselman, W.J.4
  • 28
    • 0033136946 scopus 로고    scopus 로고
    • CD45 regulates tyrosine phosphorylation of CD22 and its association with the protein tyrosine phosphatase SHP-1
    • Greer SF, Justement LB. CD45 regulates tyrosine phosphorylation of CD22 and its association with the protein tyrosine phosphatase SHP-1. J Immunol 1999 162 : 5278 5286.
    • (1999) J Immunol , vol.162 , pp. 5278-5286
    • Greer, S.F.1    Justement, L.B.2
  • 29
    • 17844388845 scopus 로고    scopus 로고
    • Visualizing the mechanical activation of Src
    • Wang Y, et al. Visualizing the mechanical activation of Src. Nature 2005 434 : 1040 1045.
    • (2005) Nature , vol.434 , pp. 1040-1045
    • Wang, Y.1
  • 30
    • 0029759927 scopus 로고    scopus 로고
    • Structural basis for inhibition of receptor protein-tyrosine phosphatase-α by dimerization
    • Bilwes AM, den Hertog J, Hunter T, Noel JP. Structural basis for inhibition of receptor protein-tyrosine phosphatase-α by dimerization. Nature 1996 382 : 555 559.
    • (1996) Nature , vol.382 , pp. 555-559
    • Bilwes, A.M.1    Den Hertog, J.2    Hunter, T.3    Noel, J.P.4
  • 31
    • 0032472226 scopus 로고    scopus 로고
    • Ligand-induced dimerization regulates receptor protein tyrosine phosphatase function via an inhibitory wedge
    • Majeti R, Bilwes AM, Noel JP, Hunter T, Weiss A. Ligand-induced dimerization regulates receptor protein tyrosine phosphatase function via an inhibitory wedge. Science 1998 279 : 88 91.
    • (1998) Science , vol.279 , pp. 88-91
    • Majeti, R.1    Bilwes, A.M.2    Noel, J.P.3    Hunter, T.4    Weiss, A.5
  • 32
    • 0034704180 scopus 로고    scopus 로고
    • An inactivating point mutation in the inhibitory wedge of CD45 causes lymphoproliferation and autoimmunity
    • Majeti R, et al. An inactivating point mutation in the inhibitory wedge of CD45 causes lymphoproliferation and autoimmunity. Cell 2000 103 : 1059 1070.
    • (2000) Cell , vol.103 , pp. 1059-1070
    • Majeti, R.1
  • 33
    • 28844498739 scopus 로고    scopus 로고
    • The juxtamembrane wedge negatively regulates CD45 function in B cells
    • Hermiston ML, Tan AL, Gupta VA, Majeti R, Weiss A. The juxtamembrane wedge negatively regulates CD45 function in B cells. Immunity 2005 23 : 635 647.
    • (2005) Immunity , vol.23 , pp. 635-647
    • Hermiston, M.L.1    Tan, A.L.2    Gupta, V.A.3    Majeti, R.4    Weiss, A.5
  • 35
    • 0033986766 scopus 로고    scopus 로고
    • A model system for activation-induced alternative splicing of CD45 pre-mRNA in T cells implicates PKC and Ras
    • Lynch KW, Weiss A. A model system for activation-induced alternative splicing of CD45 pre-mRNA in T cells implicates PKC and Ras. Mol Cell Biol 2000 20 : 70 80.
    • (2000) Mol Cell Biol , vol.20 , pp. 70-80
    • Lynch, K.W.1    Weiss, A.2
  • 36
    • 10244239317 scopus 로고    scopus 로고
    • Consequences of regulated pre-mRNA splicing in the immune system
    • Lynch KW. Consequences of regulated pre-mRNA splicing in the immune system. Nat Rev Immunol 2004 4 : 931 940.
    • (2004) Nat Rev Immunol , vol.4 , pp. 931-940
    • Lynch, K.W.1
  • 37
    • 34748892292 scopus 로고    scopus 로고
    • Combinatorial control of signal-induced exon repression by hnRNP L and PSF
    • Melton AA, Jackson J, Wang J, Lynch KW. Combinatorial control of signal-induced exon repression by hnRNP L and PSF. Mol Cell Biol 2007 27 : 6972 6984.
    • (2007) Mol Cell Biol , vol.27 , pp. 6972-6984
    • Melton, A.A.1    Jackson, J.2    Wang, J.3    Lynch, K.W.4
  • 38
    • 48749100692 scopus 로고    scopus 로고
    • Regulation of CD45 alternative splicing by heterogeneous ribonucleoprotein, hnRNPLL
    • Oberdoerffer S, Moita LF, Neems D, Freitas RP, Hacohen N, Rao A. Regulation of CD45 alternative splicing by heterogeneous ribonucleoprotein, hnRNPLL. Science 2008 321 : 686 691.
    • (2008) Science , vol.321 , pp. 686-691
    • Oberdoerffer, S.1    Moita, L.F.2    Neems, D.3    Freitas, R.P.4    Hacohen, N.5    Rao, A.6
  • 39
    • 52949090808 scopus 로고    scopus 로고
    • A cell-based screen for splicing regulators identifies hnRNP LL as a distinct signal-induced repressor of CD45 variable exon 4
    • Topp JD, Jackson J, Melton AA, Lynch KW. A cell-based screen for splicing regulators identifies hnRNP LL as a distinct signal-induced repressor of CD45 variable exon 4. RNA 2008 14 : 2038 2049.
    • (2008) RNA , vol.14 , pp. 2038-2049
    • Topp, J.D.1    Jackson, J.2    Melton, A.A.3    Lynch, K.W.4
  • 40
    • 0027997103 scopus 로고
    • Specific interaction of the CD45-protein tyrosine phosphatase with tyrosine phosphorylated CD3 ζ chain
    • Furukawa T, Itoh M, Krueger NX, Streuli M, Saito H. Specific interaction of the CD45-protein tyrosine phosphatase with tyrosine phosphorylated CD3 ζ chain. Proc Natl Acad Sci USA 1994 91 : 10928 10932.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 10928-10932
    • Furukawa, T.1    Itoh, M.2    Krueger, N.X.3    Streuli, M.4    Saito, H.5
  • 41
    • 0036202768 scopus 로고    scopus 로고
    • SKAP55 coupled with CD45 positively regulates T-cell receptor-mediated gene transcription
    • Wu L, Fu J, Shen SH. SKAP55 coupled with CD45 positively regulates T-cell receptor-mediated gene transcription. Mol Cell Biol 2002 22 : 2673 2686.
    • (2002) Mol Cell Biol , vol.22 , pp. 2673-2686
    • Wu, L.1    Fu, J.2    Shen, S.H.3
  • 42
    • 0035905767 scopus 로고    scopus 로고
    • CD45 is a JAK phosphatase and negatively regulates cytokine receptor signalling
    • Irie-Sasaki J, et al. CD45 is a JAK phosphatase and negatively regulates cytokine receptor signalling. Nature 2001 409 : 349 354.
    • (2001) Nature , vol.409 , pp. 349-354
    • Irie-Sasaki, J.1
  • 43
    • 0037370491 scopus 로고    scopus 로고
    • Phosphorylation-dependent regulation of T-cell activation by PAG/Cbp, a lipid raft-associated transmembrane adaptor
    • Davidson D, Bakinowski M, Thomas ML, Horejsi V, Veillette A. Phosphorylation-dependent regulation of T-cell activation by PAG/Cbp, a lipid raft-associated transmembrane adaptor. Mol Cell Biol 2003 23 : 2017 2028.
    • (2003) Mol Cell Biol , vol.23 , pp. 2017-2028
    • Davidson, D.1    Bakinowski, M.2    Thomas, M.L.3    Horejsi, V.4    Veillette, A.5
  • 44
    • 34548683241 scopus 로고    scopus 로고
    • Why is there so much CD45 on T cells?
    • Zamoyska R. Why is there so much CD45 on T cells? Immunity 2007 27 : 421 423.
    • (2007) Immunity , vol.27 , pp. 421-423
    • Zamoyska, R.1
  • 45
    • 3242689678 scopus 로고    scopus 로고
    • CD45: Direct and indirect government of immune regulation
    • Huntington ND, Tarlinton DM. CD45: direct and indirect government of immune regulation. Immunol Lett 2004 94 : 167 174.
    • (2004) Immunol Lett , vol.94 , pp. 167-174
    • Huntington, N.D.1    Tarlinton, D.M.2
  • 46
    • 0033794973 scopus 로고    scopus 로고
    • The CD45 tyrosine phosphatase: A positive and negative regulator of immune cell function
    • Alexander DR. The CD45 tyrosine phosphatase: a positive and negative regulator of immune cell function. Semin Immunol 2000 12 : 349 359.
    • (2000) Semin Immunol , vol.12 , pp. 349-359
    • Alexander, D.R.1
  • 47
    • 0032810006 scopus 로고    scopus 로고
    • The CD45 tyrosine phosphatase regulates CD3-induced signal transduction and T cell development in recombinase-deficient mice: Restoration of pre-TCR function by active p56(lck)
    • Pingel S, Baker M, Turner M, Holmes N, Alexander DR. The CD45 tyrosine phosphatase regulates CD3-induced signal transduction and T cell development in recombinase-deficient mice: restoration of pre-TCR function by active p56(lck). Eur J Immunol 1999 29 : 2376 2384.
    • (1999) Eur J Immunol , vol.29 , pp. 2376-2384
    • Pingel, S.1    Baker, M.2    Turner, M.3    Holmes, N.4    Alexander, D.R.5
  • 48
    • 0024316870 scopus 로고
    • Expression of CD45 alters phosphorylation of the lck-encoded tyrosine protein kinase in murine lymphoma T-cell lines
    • Ostergaard HL, et al. Expression of CD45 alters phosphorylation of the lck-encoded tyrosine protein kinase in murine lymphoma T-cell lines. Proc Natl Acad Sci USA 1989 86 : 8959 8963.
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 8959-8963
    • Ostergaard, H.L.1
  • 49
    • 0026612351 scopus 로고
    • Regulation of the p59fyn protein tyrosine kinase by the CD45 phosphotyrosine phosphatase
    • Mustelin T, et al. Regulation of the p59fyn protein tyrosine kinase by the CD45 phosphotyrosine phosphatase. Eur J Immunol 1992 22 : 1173 1178.
    • (1992) Eur J Immunol , vol.22 , pp. 1173-1178
    • Mustelin, T.1
  • 52
    • 0030293791 scopus 로고    scopus 로고
    • αβ T cell development is abolished in mice lacking both Lck and Fyn protein tyrosine kinases
    • van Oers NSC, Lowin-Kropf B, Finlay D, Connolly K, Weiss A. αβ T cell development is abolished in mice lacking both Lck and Fyn protein tyrosine kinases. Immunity 1996 5 : 429 436.
    • (1996) Immunity , vol.5 , pp. 429-436
    • Van Oers, N.S.C.1    Lowin-Kropf, B.2    Finlay, D.3    Connolly, K.4    Weiss, A.5
  • 53
    • 0031172246 scopus 로고    scopus 로고
    • CD45 regulates Src family member kinase activity associated with macrophage integrin-mediated adhesion
    • Roach T, et al. CD45 regulates Src family member kinase activity associated with macrophage integrin-mediated adhesion. Curr Biol 1997 7 : 408 417.
    • (1997) Curr Biol , vol.7 , pp. 408-417
    • Roach, T.1
  • 54
    • 0033564326 scopus 로고    scopus 로고
    • Regulation of integrin-mediated T cell adhesion by the transmembrane protein tyrosine phosphatase CD45
    • Shenoi H, Seavitt J, Zheleznyak A, Thomas ML, Brown EJ. Regulation of integrin-mediated T cell adhesion by the transmembrane protein tyrosine phosphatase CD45. J Immunol 1999 162 : 7120 7127.
    • (1999) J Immunol , vol.162 , pp. 7120-7127
    • Shenoi, H.1    Seavitt, J.2    Zheleznyak, A.3    Thomas, M.L.4    Brown, E.J.5
  • 55
    • 0033199461 scopus 로고    scopus 로고
    • CD45 and Src-family kinases: And now for something completely different
    • Ashwell JD, D'Oro U. CD45 and Src-family kinases: and now for something completely different. Immunol Today 1999 20 : 412 416.
    • (1999) Immunol Today , vol.20 , pp. 412-416
    • Ashwell, J.D.1    D'Oro, U.2
  • 56
    • 0034282725 scopus 로고    scopus 로고
    • Development of T-leukaemias in CD45 tyrosine phosphatase-deficient mutatnt lck mice
    • Baker M, et al. Development of T-leukaemias in CD45 tyrosine phosphatase-deficient mutatnt lck mice. EMBO J 2000 19 : 4644 4654.
    • (2000) EMBO J , vol.19 , pp. 4644-4654
    • Baker, M.1
  • 57
    • 34548679868 scopus 로고    scopus 로고
    • The differential regulation of Lck kinase phosphorylation sites by CD45 is critical for T cell receptor signaling responses
    • McNeill L, et al. The differential regulation of Lck kinase phosphorylation sites by CD45 is critical for T cell receptor signaling responses. Immunity 2007 27 : 425 437.
    • (2007) Immunity , vol.27 , pp. 425-437
    • McNeill, L.1
  • 58
    • 0031113985 scopus 로고    scopus 로고
    • Alterations in the level of CD45 surface expression affect the outcome of thymic selection
    • Wallace VA, et al. Alterations in the level of CD45 surface expression affect the outcome of thymic selection. J Immunol 1997 158 : 3205 3214.
    • (1997) J Immunol , vol.158 , pp. 3205-3214
    • Wallace, V.A.1
  • 59
    • 58849083208 scopus 로고    scopus 로고
    • Differential impact of the CD45 juxtamembrane wedge on central and peripheral T cell receptor responses
    • doi:.
    • Hermiston ML, et al. Differential impact of the CD45 juxtamembrane wedge on central and peripheral T cell receptor responses. Prod Natl Acad Sci USA 2009 doi:.
    • (2009) Prod Natl Acad Sci USA
    • Hermiston, M.L.1
  • 60
    • 0020663062 scopus 로고
    • Severe combined immunodeficiency in the mouse
    • Bosma GC, Custer RP, Bosma MJ. Severe combined immunodeficiency in the mouse. Nature 1983 301 : 527 530.
    • (1983) Nature , vol.301 , pp. 527-530
    • Bosma, G.C.1    Custer, R.P.2    Bosma, M.J.3
  • 61
    • 0037307095 scopus 로고    scopus 로고
    • The influence of the src-family kinases, Lck and Fyn, on T cell differentiation, survival and activation
    • Zamoyska R, Basson A, Filby A, Legname G, Lovatt M, Seddon B. The influence of the src-family kinases, Lck and Fyn, on T cell differentiation, survival and activation. Immunol Rev 2003 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
  • 62
    • 29144480861 scopus 로고    scopus 로고
    • Protein tyrosine phosphatase alpha regulates Fyn activity and Cbp/PAG phosphorylation in thymocyte lipid rafts
    • Maksumova L, Le HT, Muratkhodjaev F, Davidson D, Veillette A, Pallen CJ. Protein tyrosine phosphatase alpha regulates Fyn activity and Cbp/PAG phosphorylation in thymocyte lipid rafts. J Immunol 2005 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
  • 63
    • 0033526816 scopus 로고    scopus 로고
    • B cell development in the spleen takes place in discrete steps and is determined by the quality of B cell receptor-derived signals
    • Loder F, et al. B cell development in the spleen takes place in discrete steps and is determined by the quality of B cell receptor-derived signals. J Exp Med 1999 190 : 75 89.
    • (1999) J Exp Med , vol.190 , pp. 75-89
    • Loder, F.1
  • 64
    • 4043114170 scopus 로고    scopus 로고
    • CD45-deficient mice accumulate Pro-B cells both in vivo and in vitro
    • Fleming HE, Milne CD, Paige CJ. CD45-deficient mice accumulate Pro-B cells both in vivo and in vitro. J Immunol 2004 173 : 2542 2551.
    • (2004) J Immunol , vol.173 , pp. 2542-2551
    • Fleming, H.E.1    Milne, C.D.2    Paige, C.J.3
  • 65
    • 0030070349 scopus 로고    scopus 로고
    • Immunoglobulin-mediated signal transduction in B cells from CD45-deficient mice
    • Benatar T, Carsetti R, Furlonger C, Kamalia N, Mak T, Paige CJ. Immunoglobulin-mediated signal transduction in B cells from CD45-deficient mice. J Exp Med 1996 183 : 329 334.
    • (1996) J Exp Med , vol.183 , pp. 329-334
    • Benatar, T.1    Carsetti, R.2    Furlonger, C.3    Kamalia, N.4    Mak, T.5    Paige, C.J.6
  • 66
    • 0037342034 scopus 로고    scopus 로고
    • Essential role of Src-family protein tyrosine kinases in NF-kappaB activation during B cell development
    • Saijo K, et al. Essential role of Src-family protein tyrosine kinases in NF-kappaB activation during B cell development. Nat Immunol 2003 4 : 274 279.
    • (2003) Nat Immunol , vol.4 , pp. 274-279
    • Saijo, K.1
  • 67
    • 31344479725 scopus 로고    scopus 로고
    • CD45 links the B cell receptor with cell survival and is required for the persistence of germinal centers
    • Huntington ND, et al. CD45 links the B cell receptor with cell survival and is required for the persistence of germinal centers. Nat Immunol 2006 7 : 190 198.
    • (2006) Nat Immunol , vol.7 , pp. 190-198
    • Huntington, N.D.1
  • 68
    • 39149139617 scopus 로고    scopus 로고
    • Structurally distinct phosphatases CD45 and CD148 both regulate B cell and macrophage immunoreceptor signaling
    • Zhu JW, Brdicka T, Katsumoto TR, Lin J, Weiss A. Structurally distinct phosphatases CD45 and CD148 both regulate B cell and macrophage immunoreceptor signaling. Immunity 2008 28 : 183 196.
    • (2008) Immunity , vol.28 , pp. 183-196
    • Zhu, J.W.1    Brdicka, T.2    Katsumoto, T.R.3    Lin, J.4    Weiss, A.5
  • 70
    • 0030023652 scopus 로고    scopus 로고
    • Regulation of B-lymphocyte negative and positive selection by tyrosine phosphatase CD45
    • Cyster JG, Healy JI, Kishihara K, Mak TW, Thomas ML, Goodnow CC. Regulation of B-lymphocyte negative and positive selection by tyrosine phosphatase CD45. Nature 1996 381 : 325 328.
    • (1996) Nature , vol.381 , pp. 325-328
    • Cyster, J.G.1    Healy, J.I.2    Kishihara, K.3    Mak, T.W.4    Thomas, M.L.5    Goodnow, C.C.6
  • 71
    • 0028961264 scopus 로고
    • Protein tyrosine phopshatase 1C negatively regulates antigen receptor signaling in B lymphocytes and determines thresholds for negative selection
    • Cyster JG, Goodnow CC. Protein tyrosine phopshatase 1C negatively regulates antigen receptor signaling in B lymphocytes and determines thresholds for negative selection. Immunity 1995 2 : 13 24.
    • (1995) Immunity , vol.2 , pp. 13-24
    • Cyster, J.G.1    Goodnow, C.C.2
  • 72
    • 0842328826 scopus 로고    scopus 로고
    • Dynamic regulation of Src-family kinases by CD45 in B cells
    • Shrivastava P, Katagiri T, Ogimoto M, Mizuno K, Yakura H. Dynamic regulation of Src-family kinases by CD45 in B cells. Blood 2004 103 : 1425 1432.
    • (2004) Blood , vol.103 , pp. 1425-1432
    • Shrivastava, P.1    Katagiri, T.2    Ogimoto, M.3    Mizuno, K.4    Yakura, H.5
  • 73
    • 0033178727 scopus 로고    scopus 로고
    • CD45 negatively regulates lyn activity by dephosphorylating both positive and negative regulatory tyrosine residues in immature B cells
    • Katagiri T, et al. CD45 negatively regulates lyn activity by dephosphorylating both positive and negative regulatory tyrosine residues in immature B cells. J Immunol 1999 163 : 1321 1326.
    • (1999) J Immunol , vol.163 , pp. 1321-1326
    • Katagiri, T.1
  • 74
    • 0028863574 scopus 로고
    • Selective regulation of Lyn tyrosine kinase by CD45 in immature B cells
    • Katagiri T, Ogimoto M, Hasegawa K, Mizuno K, Yakura H. Selective regulation of Lyn tyrosine kinase by CD45 in immature B cells. J Biol Chem 1995 270 : 27987 27990.
    • (1995) J Biol Chem , vol.270 , pp. 27987-27990
    • Katagiri, T.1    Ogimoto, M.2    Hasegawa, K.3    Mizuno, K.4    Yakura, H.5
  • 75
    • 0032492994 scopus 로고    scopus 로고
    • Defective negative regulation of antigen receptor signaling in Lyn-deficient B lymphocytes
    • Chan VW, Lowell CA, DeFranco AL. Defective negative regulation of antigen receptor signaling in Lyn-deficient B lymphocytes. Curr Biol 1998 8 : 545 553.
    • (1998) Curr Biol , vol.8 , pp. 545-553
    • Chan, V.W.1    Lowell, C.A.2    Defranco, A.L.3
  • 76
    • 0028784215 scopus 로고
    • Multiple defects in the immune system of Lyn-deficient mice, culminating in autoimmune disease
    • Hibbs ML, et al. Multiple defects in the immune system of Lyn-deficient mice, culminating in autoimmune disease. Cell 1995 83 : 301 311.
    • (1995) Cell , vol.83 , pp. 301-311
    • Hibbs, M.L.1
  • 77
    • 0037121973 scopus 로고    scopus 로고
    • Sustained activation of Lyn tyrosine kinase in vivo leads to autoimmunity
    • Hibbs ML, et al. Sustained activation of Lyn tyrosine kinase in vivo leads to autoimmunity. J Exp Med 2002 196 : 1593 1604.
    • (2002) J Exp Med , vol.196 , pp. 1593-1604
    • Hibbs, M.L.1
  • 78
    • 0037204949 scopus 로고    scopus 로고
    • B cell antigen receptor signaling: Roles in cell development and disease
    • Gauld SB, Dal Porto JM, Cambier JC. B cell antigen receptor signaling: roles in cell development and disease. Science 2002 296 : 1641 1642.
    • (2002) Science , vol.296 , pp. 1641-1642
    • Gauld, S.B.1    Dal Porto, J.M.2    Cambier, J.C.3
  • 79
    • 0030586542 scopus 로고    scopus 로고
    • Enhanced generation of NK cells with intact cytotoxic function in CD45 exon 6-deficient mice
    • Yamada H, Kishihara K, Kong YY, Nomoto K. Enhanced generation of NK cells with intact cytotoxic function in CD45 exon 6-deficient mice. J Immunol 1996 157 : 1523 1528.
    • (1996) J Immunol , vol.157 , pp. 1523-1528
    • Yamada, H.1    Kishihara, K.2    Kong, Y.Y.3    Nomoto, K.4
  • 80
    • 33646491409 scopus 로고    scopus 로고
    • Dysregulation of signaling pathways in CD45-deficient NK cells leads to differentially regulated cytotoxicity and cytokine production
    • Hesslein DG, Takaki R, Hermiston ML, Weiss A, Lanier LL. Dysregulation of signaling pathways in CD45-deficient NK cells leads to differentially regulated cytotoxicity and cytokine production. Proc Natl Acad Sci USA 2006 103 : 7012 7017.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 7012-7017
    • Hesslein, D.G.1    Takaki, R.2    Hermiston, M.L.3    Weiss, A.4    Lanier, L.L.5
  • 81
    • 18644385629 scopus 로고    scopus 로고
    • A requirement for CD45 distinguishes Ly49D-mediated cytokine and chemokine production from killing in primary natural killer cells
    • Huntington ND, Xu Y, Nutt SL, Tarlinton DM. A requirement for CD45 distinguishes Ly49D-mediated cytokine and chemokine production from killing in primary natural killer cells. J Exp Med 2005 201 : 1421 1433.
    • (2005) J Exp Med , vol.201 , pp. 1421-1433
    • Huntington, N.D.1    Xu, Y.2    Nutt, S.L.3    Tarlinton, D.M.4
  • 82
    • 33646875354 scopus 로고    scopus 로고
    • Regulation of Ly49D/DAP12 signal transduction by Src-family kinases and CD45
    • Mason LH, Willette-Brown J, Taylor LS, McVicar DW. Regulation of Ly49D/DAP12 signal transduction by Src-family kinases and CD45. J Immunol 2006 176 : 6615 6623.
    • (2006) J Immunol , vol.176 , pp. 6615-6623
    • Mason, L.H.1    Willette-Brown, J.2    Taylor, L.S.3    McVicar, D.W.4
  • 83
    • 0028358822 scopus 로고
    • Leukocyte common antigen (CD45) is required for immunoglobulin E-mediated degranulation of mast cells
    • Berger SA, Mak TW, Paige CJ. Leukocyte common antigen (CD45) is required for immunoglobulin E-mediated degranulation of mast cells. J Exp Med 1994 180 : 471 476.
    • (1994) J Exp Med , vol.180 , pp. 471-476
    • Berger, S.A.1    Mak, T.W.2    Paige, C.J.3
  • 84
    • 50949119734 scopus 로고    scopus 로고
    • CD45 regulates TLR-induced proinflammatory cytokine and IFN-beta secretion in dendritic cells
    • Cross JL, Kott K, Miletic T, Johnson P. CD45 regulates TLR-induced proinflammatory cytokine and IFN-beta secretion in dendritic cells. J Immunol 2008 180 : 8020 8029.
    • (2008) J Immunol , vol.180 , pp. 8020-8029
    • Cross, J.L.1    Kott, K.2    Miletic, T.3    Johnson, P.4
  • 85
    • 33646587386 scopus 로고    scopus 로고
    • CD45 negatively regulates tumour necrosis factor and interleukin-6 production in dendritic cells
    • Piercy J, Petrova S, Tchilian EZ, Beverley PC. CD45 negatively regulates tumour necrosis factor and interleukin-6 production in dendritic cells. Immunol 2006 118 : 250 256.
    • (2006) Immunol , vol.118 , pp. 250-256
    • Piercy, J.1    Petrova, S.2    Tchilian, E.Z.3    Beverley, P.C.4
  • 86
    • 33747435487 scopus 로고    scopus 로고
    • CD45 is required for type i IFN production by dendritic cells
    • Montoya M, et al. CD45 is required for type I IFN production by dendritic cells. Eur J Immunol 2006 36 : 2150 2158.
    • (2006) Eur J Immunol , vol.36 , pp. 2150-2158
    • Montoya, M.1
  • 87
    • 13844276957 scopus 로고    scopus 로고
    • The Src family kinases Hck and Fgr negatively regulate neutrophil and dendritic cell chemokine signaling via PIR-B
    • Zhang H, Meng F, Chu CL, Takai T, Lowell CA. The Src family kinases Hck and Fgr negatively regulate neutrophil and dendritic cell chemokine signaling via PIR-B. Immunity 2005 22 : 235 246.
    • (2005) Immunity , vol.22 , pp. 235-246
    • Zhang, H.1    Meng, F.2    Chu, C.L.3    Takai, T.4    Lowell, C.A.5
  • 88
    • 20644443886 scopus 로고    scopus 로고
    • Enhanced Toll-like receptor responses in the absence of signaling adaptor DAP12
    • Hamerman JA, Tchao NK, Lowell CA, Lanier LL. Enhanced Toll-like receptor responses in the absence of signaling adaptor DAP12. Nat Immunol 2005 6 : 579 586.
    • (2005) Nat Immunol , vol.6 , pp. 579-586
    • Hamerman, J.A.1    Tchao, N.K.2    Lowell, C.A.3    Lanier, L.L.4
  • 89
    • 0037097673 scopus 로고    scopus 로고
    • Apoptosis mediated through CD45 is independent of its phosphatase activity and association with leukocyte phosphatase-associated phosphoprotein
    • Fortin M, et al. Apoptosis mediated through CD45 is independent of its phosphatase activity and association with leukocyte phosphatase-associated phosphoprotein. J Immunol 2002 168 : 6084 6089.
    • (2002) J Immunol , vol.168 , pp. 6084-6089
    • Fortin, M.1
  • 90
    • 33744960104 scopus 로고    scopus 로고
    • HIV-1 gp120-mediated apoptosis of T cells is regulated by the membrane tyrosine phosphatase CD45
    • Anand AR, Ganju RK. HIV-1 gp120-mediated apoptosis of T cells is regulated by the membrane tyrosine phosphatase CD45. J Biol Chem 2006 281 : 12289 12299.
    • (2006) J Biol Chem , vol.281 , pp. 12289-12299
    • Anand, A.R.1    Ganju, R.K.2
  • 92
    • 38649093325 scopus 로고    scopus 로고
    • Involvement of CD45 in DNA fragmentation in apoptosis induced by mitochondrial perturbing agents
    • Desharnais P, Dupere-Minier G, Hamelin C, Devine P, Bernier J. Involvement of CD45 in DNA fragmentation in apoptosis induced by mitochondrial perturbing agents. Apoptosis 2008 13 : 197 212.
    • (2008) Apoptosis , vol.13 , pp. 197-212
    • Desharnais, P.1    Dupere-Minier, G.2    Hamelin, C.3    Devine, P.4    Bernier, J.5
  • 93
    • 0030584787 scopus 로고    scopus 로고
    • CD45 ligation induces programmed cell death in T and B lymphocytes
    • Klaus SJ, Sidorenko SP, Clark EA. CD45 ligation induces programmed cell death in T and B lymphocytes. J Immunol 1996 156 : 2743 2753.
    • (1996) J Immunol , vol.156 , pp. 2743-2753
    • Klaus, S.J.1    Sidorenko, S.P.2    Clark, E.A.3
  • 94
    • 34249338061 scopus 로고    scopus 로고
    • Collagen-mediated survival signaling is modulated by CD45 in Jurkat T cells
    • Bijian K, Zhang L, Shen SH. Collagen-mediated survival signaling is modulated by CD45 in Jurkat T cells. Mol Immunol 2007 44 : 3682 3690.
    • (2007) Mol Immunol , vol.44 , pp. 3682-3690
    • Bijian, K.1    Zhang, L.2    Shen, S.H.3
  • 95
    • 58149296185 scopus 로고    scopus 로고
    • B cells drive lymphocyte activation and expansion in mice with the CD45 wedge mutation and Fas deficiency
    • Gupta VA, Hermiston ML, Cassafer G, Daikh DI, Weiss A. B cells drive lymphocyte activation and expansion in mice with the CD45 wedge mutation and Fas deficiency. J Exp Med 2008 12 : 2755 2761.
    • (2008) J Exp Med , vol.12 , pp. 2755-2761
    • Gupta, V.A.1    Hermiston, M.L.2    Cassafer, G.3    Daikh, D.I.4    Weiss, A.5
  • 96
    • 0025913892 scopus 로고
    • The B lymphocyte adhesion molecule CD22 interacts with leukocyte common antigen CD45RO on T cells and α2-6 sialyltransferase, CD75, on B cells
    • Stamenkovic I, Sgroi D, Aruffo A, Sy MS, Anderson T. The B lymphocyte adhesion molecule CD22 interacts with leukocyte common antigen CD45RO on T cells and α2-6 sialyltransferase, CD75, on B cells. Cell 1991 66 : 1133 1144.
    • (1991) Cell , vol.66 , pp. 1133-1144
    • Stamenkovic, I.1    Sgroi, D.2    Aruffo, A.3    Sy, M.S.4    Anderson, T.5
  • 97
    • 0033561213 scopus 로고    scopus 로고
    • Galectin-1, a natural ligand for the receptor-type protein tyrosine phosphatase CD45
    • Walzel H, Schulz U, Neels P, Brock J. Galectin-1, a natural ligand for the receptor-type protein tyrosine phosphatase CD45. Immunol Lett 1999 67 : 193 202.
    • (1999) Immunol Lett , vol.67 , pp. 193-202
    • Walzel, H.1    Schulz, U.2    Neels, P.3    Brock, J.4
  • 98
    • 0034644696 scopus 로고    scopus 로고
    • Specific isoforms of the resident endoplasmic reticulum protein glucosidase II associate with the CD45 protein-tyrosine phosphatase via a lectin-like interaction
    • Baldwin TA, Gogela-Spehar M, Ostergaard HL. Specific isoforms of the resident endoplasmic reticulum protein glucosidase II associate with the CD45 protein-tyrosine phosphatase via a lectin-like interaction. J Biol Chem 2000 275 : 32071 32076.
    • (2000) J Biol Chem , vol.275 , pp. 32071-32076
    • Baldwin, T.A.1    Gogela-Spehar, M.2    Ostergaard, H.L.3
  • 99
    • 0032504217 scopus 로고    scopus 로고
    • Characterization of recombinant CD45 cytoplasmic domain proteins. Evidence for intramolecular and intermolecular interactions
    • Felberg J, Johnson P. Characterization of recombinant CD45 cytoplasmic domain proteins. Evidence for intramolecular and intermolecular interactions. J Biol Chem 1998 273 : 17839 17845.
    • (1998) J Biol Chem , vol.273 , pp. 17839-17845
    • Felberg, J.1    Johnson, P.2
  • 100
    • 0026714979 scopus 로고
    • Evidence for monomeric and dimeric forms of CD45 associated with a 30-kDa phosphorylated protein
    • Takeda A, Wu JJ, Maizel AL. Evidence for monomeric and dimeric forms of CD45 associated with a 30-kDa phosphorylated protein. J Biol Chem 1992 267 : 16651 16659.
    • (1992) J Biol Chem , vol.267 , pp. 16651-16659
    • Takeda, A.1    Wu, J.J.2    Maizel, A.L.3
  • 101
    • 18544371851 scopus 로고    scopus 로고
    • Differential association of CD45 isoforms with CD4 and CD8 regulates the actions of specific pools of p56lck tyrosine kinase in T cell antigen receptor signal transduction
    • Dornan S, et al. Differential association of CD45 isoforms with CD4 and CD8 regulates the actions of specific pools of p56lck tyrosine kinase in T cell antigen receptor signal transduction. J Biol Chem 2002 277 : 1912 1918.
    • (2002) J Biol Chem , vol.277 , pp. 1912-1918
    • Dornan, S.1
  • 102
    • 0036346992 scopus 로고    scopus 로고
    • Negative regulation of CD45 by differential homodimerization of the alternatively spliced isoforms
    • Xu Z, Weiss A. Negative regulation of CD45 by differential homodimerization of the alternatively spliced isoforms. Nat Immunol 2002 3 : 764 771.
    • (2002) Nat Immunol , vol.3 , pp. 764-771
    • Xu, Z.1    Weiss, A.2
  • 103
    • 0027266773 scopus 로고
    • Ligand-mediated negative regulation of a chimeric transmembrane receptor tyrosine phosphatase
    • Desai DM, Sap J, Schlessinger J, Weiss A. Ligand-mediated negative regulation of a chimeric transmembrane receptor tyrosine phosphatase. Cell 1993 73 : 541 554.
    • (1993) Cell , vol.73 , pp. 541-554
    • Desai, D.M.1    Sap, J.2    Schlessinger, J.3    Weiss, A.4
  • 104
    • 0037561996 scopus 로고    scopus 로고
    • Redox-regulated rotational coupling of receptor protein-tyrosine phosphatase alpha dimers
    • van der Wijk T, Blanchetot C, Overvoorde J, den Hertog J. Redox-regulated rotational coupling of receptor protein-tyrosine phosphatase alpha dimers. J Biol Chem 2003 278 : 13968 13974.
    • (2003) J Biol Chem , vol.278 , pp. 13968-13974
    • Van Der Wijk, T.1    Blanchetot, C.2    Overvoorde, J.3    Den Hertog, J.4
  • 105
    • 55849090253 scopus 로고    scopus 로고
    • Hunter to gatherer and back: Immunological synapses and kinapses as variations on the theme of amoeboid locomotion
    • Dustin ML. Hunter to gatherer and back: immunological synapses and kinapses as variations on the theme of amoeboid locomotion. Annu Rev Cell Dev Biol 2008 24 : 577 596.
    • (2008) Annu Rev Cell Dev Biol , vol.24 , pp. 577-596
    • Dustin, M.L.1
  • 106
    • 20444404267 scopus 로고    scopus 로고
    • Single-molecule microscopy reveals plasma membrane microdomains created by protein-protein networks that exclude or trap signaling molecules in T cells
    • Douglass AD, Vale RD. Single-molecule microscopy reveals plasma membrane microdomains created by protein-protein networks that exclude or trap signaling molecules in T cells. Cell 2005 121 : 937 950.
    • (2005) Cell , vol.121 , pp. 937-950
    • Douglass, A.D.1    Vale, R.D.2
  • 107
    • 34447286463 scopus 로고    scopus 로고
    • Molecular mechanisms involved in T cell receptor triggering
    • Choudhuri K, van der Merwe PA. Molecular mechanisms involved in T cell receptor triggering. Semin Immunol 2007 19 : 255 261.
    • (2007) Semin Immunol , vol.19 , pp. 255-261
    • Choudhuri, K.1    Van Der Merwe, P.A.2
  • 108
    • 33746011209 scopus 로고    scopus 로고
    • T cell receptor-proximal signals are sustained in peripheral microclusters and terminated in the central supramolecular activation cluster
    • Varma R, Campi G, Yokosuka T, Saito T, Dustin ML. T cell receptor-proximal signals are sustained in peripheral microclusters and terminated in the central supramolecular activation cluster. Immunity 2006 25 : 117 127.
    • (2006) Immunity , vol.25 , pp. 117-127
    • Varma, R.1    Campi, G.2    Yokosuka, T.3    Saito, T.4    Dustin, M.L.5
  • 109
    • 30044441433 scopus 로고    scopus 로고
    • Newly generated T cell receptor microclusters initiate and sustain T cell activation by recruitment of Zap70 and SLP-76
    • Yokosuka T, et al. Newly generated T cell receptor microclusters initiate and sustain T cell activation by recruitment of Zap70 and SLP-76. Nat Immunol 2005 6 : 1253 1262.
    • (2005) Nat Immunol , vol.6 , pp. 1253-1262
    • Yokosuka, T.1
  • 110
    • 27544441784 scopus 로고    scopus 로고
    • Actin and agonist MHC-peptide complex-dependent T cell receptor microclusters as scaffolds for signaling
    • Campi G, Varma R, Dustin ML. Actin and agonist MHC-peptide complex-dependent T cell receptor microclusters as scaffolds for signaling. J Exp Med 2005 202 : 1031 1036.
    • (2005) J Exp Med , vol.202 , pp. 1031-1036
    • Campi, G.1    Varma, R.2    Dustin, M.L.3
  • 111
    • 0036737124 scopus 로고    scopus 로고
    • Targeting of CD45 protein tyrosine phosphatase activity to lipid microdomains on the T cell surface inhibits TCR signaling
    • He X, Woodford-Thomas TA, Johnson KG, Shah DD, Thomas ML. Targeting of CD45 protein tyrosine phosphatase activity to lipid microdomains on the T cell surface inhibits TCR signaling. Eur J Immunol 2002 32 : 2578 2587.
    • (2002) Eur J Immunol , vol.32 , pp. 2578-2587
    • He, X.1    Woodford-Thomas, T.A.2    Johnson, K.G.3    Shah, D.D.4    Thomas, M.L.5
  • 112
    • 0035869308 scopus 로고    scopus 로고
    • Targeting Src homology 2 domain-containing tyrosine phosphatase (SHP-1) into lipid rafts inhibits CD3-induced T cell activation
    • Su MW, Yu CL, Burakoff SJ, Jin YJ. Targeting Src homology 2 domain-containing tyrosine phosphatase (SHP-1) into lipid rafts inhibits CD3-induced T cell activation. J Immunol 2001 166 : 3975 3982.
    • (2001) J Immunol , vol.166 , pp. 3975-3982
    • Su, M.W.1    Yu, C.L.2    Burakoff, S.J.3    Jin, Y.J.4
  • 113
    • 0036063264 scopus 로고    scopus 로고
    • Immature CD4(+)CD8(+) thymocytes form a multifocal immunological synapse with sustained tyrosine phosphorylation
    • Hailman E, Burack WR, Shaw AS, Dustin ML, Allen PM. Immature CD4(+)CD8(+) thymocytes form a multifocal immunological synapse with sustained tyrosine phosphorylation. Immunity 2002 16 : 839 848.
    • (2002) Immunity , vol.16 , pp. 839-848
    • Hailman, E.1    Burack, W.R.2    Shaw, A.S.3    Dustin, M.L.4    Allen, P.M.5
  • 114
    • 0024327898 scopus 로고
    • The leukocyte common antigen family
    • Thomas M. The leukocyte common antigen family. Annu Rev Immunol 1989 7 : 339 370.
    • (1989) Annu Rev Immunol , vol.7 , pp. 339-370
    • Thomas, M.1
  • 115
    • 0037318863 scopus 로고    scopus 로고
    • CD45 ectodomain controls interaction with GEMs and Lck activity for optimal TCR signaling
    • Irles C, Symons A, Michel F, Bakker TR, van der Merwe PA, Acuto O. CD45 ectodomain controls interaction with GEMs and Lck activity for optimal TCR signaling. Nat Immunol 2003 4 : 189 197.
    • (2003) Nat Immunol , vol.4 , pp. 189-197
    • Irles, C.1    Symons, A.2    Michel, F.3    Bakker, T.R.4    Van Der Merwe, P.A.5    Acuto, O.6
  • 116
    • 0036754181 scopus 로고    scopus 로고
    • The spectrin-ankyrin skeleton controls CD45 surface display and interleukin-2 production
    • Pradhan D, Morrow J. The spectrin-ankyrin skeleton controls CD45 surface display and interleukin-2 production. Immunity 2002 17 : 303 315.
    • (2002) Immunity , vol.17 , pp. 303-315
    • Pradhan, D.1    Morrow, J.2
  • 117
    • 26844436431 scopus 로고    scopus 로고
    • Inefficient cell spreading and cytoskeletal polarization by CD4+CD8+ thymocytes: Regulation by the thymic environment
    • Hailman E, Allen PM. Inefficient cell spreading and cytoskeletal polarization by CD4+CD8+ thymocytes: regulation by the thymic environment. J Immunol 2005 175 : 4847 4857.
    • (2005) J Immunol , vol.175 , pp. 4847-4857
    • Hailman, E.1    Allen, P.M.2
  • 118
    • 0028036712 scopus 로고
    • LPAP, a novel 32-kDa phosphoprotein that interacts with CD45 in human lymphocytes
    • Schraven B, et al. LPAP, a novel 32-kDa phosphoprotein that interacts with CD45 in human lymphocytes. J Biol Chem 1994 269 : 29102 29111.
    • (1994) J Biol Chem , vol.269 , pp. 29102-29111
    • Schraven, B.1
  • 119
    • 34447097283 scopus 로고    scopus 로고
    • CD45-associated protein promotes the response of primary CD4 T cells to low-potency T-cell receptor (TCR) stimulation and facilitates CD45 association with CD3/TCR and lck
    • Leitenberg D, Falahati R, Lu DD, Takeda A. CD45-associated protein promotes the response of primary CD4 T cells to low-potency T-cell receptor (TCR) stimulation and facilitates CD45 association with CD3/TCR and lck. Immunol 2007 121 : 545 554.
    • (2007) Immunol , vol.121 , pp. 545-554
    • Leitenberg, D.1    Falahati, R.2    Lu, D.D.3    Takeda, A.4
  • 120
    • 0032101050 scopus 로고    scopus 로고
    • Disruption of lymphocyte function and signaling in CD45-associated protein-null mice
    • Matsuda A, Motoya S, Kimura S, McInnis R, Maizel AL, Takeda A. Disruption of lymphocyte function and signaling in CD45-associated protein-null mice. J Exp Med 1998 187 : 1863 1870.
    • (1998) J Exp Med , vol.187 , pp. 1863-1870
    • Matsuda, A.1    Motoya, S.2    Kimura, S.3    McInnis, R.4    Maizel, A.L.5    Takeda, A.6
  • 121
    • 0032709886 scopus 로고    scopus 로고
    • Biochemical and functional analysis of mice deficient in expression of the CD45-associated phosphoprotein LPAP
    • Ding I, et al. Biochemical and functional analysis of mice deficient in expression of the CD45-associated phosphoprotein LPAP. Eur J Immunol 1999 29 : 3956 3961.
    • (1999) Eur J Immunol , vol.29 , pp. 3956-3961
    • Ding, I.1
  • 122
    • 0032711859 scopus 로고    scopus 로고
    • CD45-associated protein is not essential for the regulation of antigen receptor-mediated signal transduction
    • Kung C, et al. CD45-associated protein is not essential for the regulation of antigen receptor-mediated signal transduction. Eur J Immunol 1999 29 : 3951 3955.
    • (1999) Eur J Immunol , vol.29 , pp. 3951-3955
    • Kung, C.1
  • 123
    • 0025901099 scopus 로고
    • Protein-tyrosine-phosphatase CD45 is phosphorylated transiently on tyrosine upon activation of Jurkat T cells
    • Stover DR, Charbonneau H, Tonks NK, Walsh KA. Protein-tyrosine- phosphatase CD45 is phosphorylated transiently on tyrosine upon activation of Jurkat T cells. Proc Natl Acad Sci USA 1991 88 : 7704 7707.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 7704-7707
    • Stover, D.R.1    Charbonneau, H.2    Tonks, N.K.3    Walsh, K.A.4
  • 124
    • 0028013487 scopus 로고
    • lck tyrosine kinase and activates the phosphatase
    • lck tyrosine kinase and activates the phosphatase. Mol Cell Biol 1994 14 : 1308 1321.
    • (1994) Mol Cell Biol , vol.14 , pp. 1308-1321
    • Autero, M.1
  • 125
    • 0031154586 scopus 로고    scopus 로고
    • Inhibition of CD45 during neutrophil activation
    • Fialkow L, Chan CK, Downey GP. Inhibition of CD45 during neutrophil activation. J Immunol 1997 158 : 5409 5417.
    • (1997) J Immunol , vol.158 , pp. 5409-5417
    • Fialkow, L.1    Chan, C.K.2    Downey, G.P.3
  • 126
    • 36048945330 scopus 로고    scopus 로고
    • Altered CD45 isoform expression in C77G carriers influences cytokine responsiveness and adhesion properties of T cells
    • Windhagen A, Sonmez D, Hornig-Do HT, Kalinowsky A, Schwinzer R. Altered CD45 isoform expression in C77G carriers influences cytokine responsiveness and adhesion properties of T cells. Clin Exp Immunol 2007 150 : 509 517.
    • (2007) Clin Exp Immunol , vol.150 , pp. 509-517
    • Windhagen, A.1    Sonmez, D.2    Hornig-Do, H.T.3    Kalinowsky, A.4    Schwinzer, R.5
  • 127
  • 129
    • 0035102841 scopus 로고    scopus 로고
    • Protein tyrosine phosphatase CD148-mediated inhibition of T-cell receptor signal transduction is associated with reduced LAT and phospholipase C gamma1 phosphorylation
    • Baker JE, Majeti R, Tangye SG, Weiss A. Protein tyrosine phosphatase CD148-mediated inhibition of T-cell receptor signal transduction is associated with reduced LAT and phospholipase C gamma1 phosphorylation. Mol Cell Biol 2001 21 : 2393 2403.
    • (2001) Mol Cell Biol , vol.21 , pp. 2393-2403
    • Baker, J.E.1    Majeti, R.2    Tangye, S.G.3    Weiss, A.4
  • 130
    • 9444227665 scopus 로고    scopus 로고
    • Cloning and characterization of rat density-enhanced phosphatase-1, a protein tyrosine phosphatase expressed by vascular cells
    • Borges LG, et al. Cloning and characterization of rat density-enhanced phosphatase-1, a protein tyrosine phosphatase expressed by vascular cells. Circ Res 1996 79 : 570 580.
    • (1996) Circ Res , vol.79 , pp. 570-580
    • Borges, L.G.1
  • 131
    • 0032749780 scopus 로고    scopus 로고
    • CD148, a new membrane tyrosine phosphatase involved in leukocyte function
    • Gaya A, et al. CD148, a new membrane tyrosine phosphatase involved in leukocyte function. Leuk Lymphoma 1999 35 : 237 243.
    • (1999) Leuk Lymphoma , vol.35 , pp. 237-243
    • Gaya, A.1
  • 132
    • 0030068060 scopus 로고    scopus 로고
    • Molecular cloning and characterization of Byp, a murine receptor-type tyrosine phosphatase similar to human DEP-1
    • Kuramochi S, Matsuda S, Matsuda Y, Saitoh T, Ohsugi M, Yamamoto T. Molecular cloning and characterization of Byp, a murine receptor-type tyrosine phosphatase similar to human DEP-1. FEBS Lett 1996 378 : 7 14.
    • (1996) FEBS Lett , vol.378 , pp. 7-14
    • Kuramochi, S.1    Matsuda, S.2    Matsuda, Y.3    Saitoh, T.4    Ohsugi, M.5    Yamamoto, T.6
  • 133
    • 4043107043 scopus 로고    scopus 로고
    • Regulated expression of the receptor-like tyrosine phosphatase CD148 on hemopoietic cells
    • Lin J, Zhu JW, Baker JE, Weiss A. Regulated expression of the receptor-like tyrosine phosphatase CD148 on hemopoietic cells. J Immunol 2004 173 : 2324 2330.
    • (2004) J Immunol , vol.173 , pp. 2324-2330
    • Lin, J.1    Zhu, J.W.2    Baker, J.E.3    Weiss, A.4
  • 134
    • 33749817962 scopus 로고    scopus 로고
    • DEP-1 protein tyrosine phosphatase inhibits proliferation and migration of colon carcinoma cells and is upregulated by protective nutrients
    • Balavenkatraman KK, et al. DEP-1 protein tyrosine phosphatase inhibits proliferation and migration of colon carcinoma cells and is upregulated by protective nutrients. Oncogene 2006 25 : 6319 6324.
    • (2006) Oncogene , vol.25 , pp. 6319-6324
    • Balavenkatraman, K.K.1
  • 135
    • 0029789246 scopus 로고    scopus 로고
    • The protein tyrosine phosphatase DEP-1 is induced during differentiation and inhibits growth of breast cancer cells
    • Keane MM, Lowrey GA, Ettenberg SA, Dayton MA, Lipkowitz S. The protein tyrosine phosphatase DEP-1 is induced during differentiation and inhibits growth of breast cancer cells. Cancer Res 1996 56 : 4236 4243.
    • (1996) Cancer Res , vol.56 , pp. 4236-4243
    • Keane, M.M.1    Lowrey, G.A.2    Ettenberg, S.A.3    Dayton, M.A.4    Lipkowitz, S.5
  • 136
    • 0034458955 scopus 로고    scopus 로고
    • Rat protein tyrosine phosphatase eta suppresses the neoplastic phenotype of retrovirally transformed thyroid cells through the stabilization of p27(Kip1)
    • Trapasso F, et al. Rat protein tyrosine phosphatase eta suppresses the neoplastic phenotype of retrovirally transformed thyroid cells through the stabilization of p27(Kip1). Mol Cell Biol 2000 20 : 9236 9246.
    • (2000) Mol Cell Biol , vol.20 , pp. 9236-9246
    • Trapasso, F.1
  • 137
    • 8844236892 scopus 로고    scopus 로고
    • Restoration of receptor-type protein tyrosine phosphatase eta function inhibits human pancreatic carcinoma cell growth in vitro and in vivo
    • Trapasso F, et al. Restoration of receptor-type protein tyrosine phosphatase eta function inhibits human pancreatic carcinoma cell growth in vitro and in vivo. Carcinogenesis 2004 25 : 2107 2114.
    • (2004) Carcinogenesis , vol.25 , pp. 2107-2114
    • Trapasso, F.1
  • 138
    • 0032703176 scopus 로고    scopus 로고
    • Expression of the membrane protein tyrosine phosphatase CD148 in human tissues
    • Autschbach F, et al. Expression of the membrane protein tyrosine phosphatase CD148 in human tissues. Tissue Antigens 1999 54 : 485 498.
    • (1999) Tissue Antigens , vol.54 , pp. 485-498
    • Autschbach, F.1
  • 139
    • 0032194157 scopus 로고    scopus 로고
    • CD148: A receptor-like protein tyrosine phosphatase involved in the regulation of human T cell activation
    • Tangye SG, Phillips JH, Lanier LL, deVries JE, Aversa G. CD148: a receptor-like protein tyrosine phosphatase involved in the regulation of human T cell activation. J Immunol 1998 161 : 3249 3255.
    • (1998) J Immunol , vol.161 , pp. 3249-3255
    • Tangye, S.G.1    Phillips, J.H.2    Lanier, L.L.3    Devries, J.E.4    Aversa, G.5
  • 140
    • 0038118340 scopus 로고    scopus 로고
    • LOH of PTPRJ occurs early in colorectal cancer and is associated with chromosomal loss of 18q12-21
    • Ruivenkamp C, et al. LOH of PTPRJ occurs early in colorectal cancer and is associated with chromosomal loss of 18q12-21. Oncogene 2003 22 : 3472 3474.
    • (2003) Oncogene , vol.22 , pp. 3472-3474
    • Ruivenkamp, C.1
  • 141
    • 0036649023 scopus 로고    scopus 로고
    • Ptprj is a candidate for the mouse colon-cancer susceptibility locus Scc1 and is frequently deleted in human cancers
    • Ruivenkamp CA, et al. Ptprj is a candidate for the mouse colon-cancer susceptibility locus Scc1 and is frequently deleted in human cancers. Nat Genet 2002 31 : 295 300.
    • (2002) Nat Genet , vol.31 , pp. 295-300
    • Ruivenkamp, C.A.1
  • 142
    • 0037152076 scopus 로고    scopus 로고
    • Autoantibodies to inner ear and endothelial antigens in Cogan's syndrome
    • Lunardi C, et al. Autoantibodies to inner ear and endothelial antigens in Cogan's syndrome. Lancet 2002 360 : 915 921.
    • (2002) Lancet , vol.360 , pp. 915-921
    • Lunardi, C.1
  • 143
    • 0037057319 scopus 로고    scopus 로고
    • The transmembrane receptor protein tyrosine phosphatase DEP1 interacts with p120(ctn)
    • Holsinger LJ, Ward K, Duffield B, Zachwieja J, Jallal B. The transmembrane receptor protein tyrosine phosphatase DEP1 interacts with p120(ctn). Oncogene 2002 21 : 7067 7076.
    • (2002) Oncogene , vol.21 , pp. 7067-7076
    • Holsinger, L.J.1    Ward, K.2    Duffield, B.3    Zachwieja, J.4    Jallal, B.5
  • 144
    • 0034717163 scopus 로고    scopus 로고
    • Site-selective dephosphorylation of the platelet-derived growth factor beta-receptor by the receptor-like protein-tyrosine phosphatase DEP-1
    • Kovalenko M, et al. Site-selective dephosphorylation of the platelet-derived growth factor beta-receptor by the receptor-like protein-tyrosine phosphatase DEP-1. J Biol Chem 2000 275 : 16219 16226.
    • (2000) J Biol Chem , vol.275 , pp. 16219-16226
    • Kovalenko, M.1
  • 145
    • 0037458646 scopus 로고    scopus 로고
    • Hepatocyte growth factor receptor tyrosine kinase met is a substrate of the receptor protein-tyrosine phosphatase DEP-1
    • Palka HL, Park M, Tonks NK. Hepatocyte growth factor receptor tyrosine kinase met is a substrate of the receptor protein-tyrosine phosphatase DEP-1. J Biol Chem 2003 278 : 5728 5735.
    • (2003) J Biol Chem , vol.278 , pp. 5728-5735
    • Palka, H.L.1    Park, M.2    Tonks, N.K.3
  • 146
    • 21044452876 scopus 로고    scopus 로고
    • The rat tyrosine phosphatase eta increases cell adhesion by activating c-Src through dephosphorylation of its inhibitory phosphotyrosine residue
    • Pera IL, et al. The rat tyrosine phosphatase eta increases cell adhesion by activating c-Src through dephosphorylation of its inhibitory phosphotyrosine residue. Oncogene 2005 24 : 3187 3195.
    • (2005) Oncogene , vol.24 , pp. 3187-3195
    • Pera, I.L.1
  • 147
    • 0037165628 scopus 로고    scopus 로고
    • Primary sequence determinants responsible for site-selective dephosphorylation of the PDGF beta-receptor by the receptor-like protein tyrosine phosphatase DEP-1
    • Persson C, Engstrom U, Mowbray SL, Ostman A. Primary sequence determinants responsible for site-selective dephosphorylation of the PDGF beta-receptor by the receptor-like protein tyrosine phosphatase DEP-1. FEBS Lett 2002 517 : 27 31.
    • (2002) FEBS Lett , vol.517 , pp. 27-31
    • Persson, C.1    Engstrom, U.2    Mowbray, S.L.3    Ostman, A.4
  • 148
    • 46249118646 scopus 로고    scopus 로고
    • The tyrosine phosphatase CD148 interacts with the p85 regulatory subunit of phosphoinositide 3-kinase
    • Tsuboi N, et al. The tyrosine phosphatase CD148 interacts with the p85 regulatory subunit of phosphoinositide 3-kinase. Biochem J 2008 413 : 193 200.
    • (2008) Biochem J , vol.413 , pp. 193-200
    • Tsuboi, N.1
  • 149
    • 0041976988 scopus 로고    scopus 로고
    • The tyrosine phosphatase CD148 is excluded from the immunologic synapse and down-regulates prolonged T cell signaling
    • Lin J, Weiss A. The tyrosine phosphatase CD148 is excluded from the immunologic synapse and down-regulates prolonged T cell signaling. J Cell Biol 2003 162 : 673 682.
    • (2003) J Cell Biol , vol.162 , pp. 673-682
    • Lin, J.1    Weiss, A.2
  • 150
    • 0037369897 scopus 로고    scopus 로고
    • A mutant receptor tyrosine phosphatase, CD148, causes defects in vascular development
    • Takahashi T, et al. A mutant receptor tyrosine phosphatase, CD148, causes defects in vascular development. Mol Cell Biol 2003 23 : 1817 1831.
    • (2003) Mol Cell Biol , vol.23 , pp. 1817-1831
    • Takahashi, T.1
  • 151
    • 33745457190 scopus 로고    scopus 로고
    • Genetic ablation of Ptprj, a mouse cancer susceptibility gene, results in normal growth and development and does not predispose to spontaneous tumorigenesis
    • Trapasso F, et al. Genetic ablation of Ptprj, a mouse cancer susceptibility gene, results in normal growth and development and does not predispose to spontaneous tumorigenesis. DNA Cell Biol 2006 25 : 376 382.
    • (2006) DNA Cell Biol , vol.25 , pp. 376-382
    • Trapasso, F.1
  • 152
    • 0026742211 scopus 로고
    • Characterization of hematopoietic intracellular protein tyrosine phosphatases: Description of a phosphatase containing an SH2 domain and another enriched in proline-, glutamic acid-, serine-, and threonine-rich sequences
    • Matthews RJ, Bowne DB, Flores E, Thomas ML. Characterization of hematopoietic intracellular protein tyrosine phosphatases: description of a phosphatase containing an SH2 domain and another enriched in proline-, glutamic acid-, serine-, and threonine-rich sequences. Mol Cell Biol 1992 12 : 2396 2405.
    • (1992) Mol Cell Biol , vol.12 , pp. 2396-2405
    • Matthews, R.J.1    Bowne, D.B.2    Flores, E.3    Thomas, M.L.4
  • 153
    • 0033559313 scopus 로고    scopus 로고
    • Cloning and characterization of a lymphoid-specific, inducible human protein tyrosine phosphatase, Lyp
    • Cohen S, Dadi H, Shaoul E, Sharfe N, Roifman CM. Cloning and characterization of a lymphoid-specific, inducible human protein tyrosine phosphatase, Lyp. Blood 1999 93 : 2013 2024.
    • (1999) Blood , vol.93 , pp. 2013-2024
    • Cohen, S.1    Dadi, H.2    Shaoul, E.3    Sharfe, N.4    Roifman, C.M.5
  • 154
    • 0029819526 scopus 로고    scopus 로고
    • csk with protein tyrosine phosphatase PEP in T cells and other hemopoietic cells
    • csk with protein tyrosine phosphatase PEP in T cells and other hemopoietic cells. EMBO J 1996 15 : 4909 4918.
    • (1996) EMBO J , vol.15 , pp. 4909-4918
    • Cloutier, J.1    Veillette, A.2
  • 155
    • 0033521596 scopus 로고    scopus 로고
    • Cooperative inhibition of T-cell antigen receptor signaling by a complex between a kinase and a phosphatase
    • Cloutier JF, Veillette A. Cooperative inhibition of T-cell antigen receptor signaling by a complex between a kinase and a phosphatase. J Exp Med 1999 189 : 111 121.
    • (1999) J Exp Med , vol.189 , pp. 111-121
    • Cloutier, J.F.1    Veillette, A.2
  • 156
    • 0242712698 scopus 로고    scopus 로고
    • Characterization of TCR-induced receptor-proximal signaling events negatively regulated by the protein tyrosine phosphatase PEP
    • Gjorloff-Wingren A, Saxena M, Williams S, Hammi D, Mustelin T. Characterization of TCR-induced receptor-proximal signaling events negatively regulated by the protein tyrosine phosphatase PEP. Eur J Immunol 1999 29 : 3845 3854.
    • (1999) Eur J Immunol , vol.29 , pp. 3845-3854
    • Gjorloff-Wingren, A.1    Saxena, M.2    Williams, S.3    Hammi, D.4    Mustelin, T.5
  • 157
    • 33744949634 scopus 로고    scopus 로고
    • Identification of substrates of human protein-tyrosine phosphatase PTPN22
    • Wu J, et al. Identification of substrates of human protein-tyrosine phosphatase PTPN22. J Biol Chem 2006 281 : 11002 11010.
    • (2006) J Biol Chem , vol.281 , pp. 11002-11010
    • Wu, J.1
  • 158
    • 0342313755 scopus 로고    scopus 로고
    • 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
    • Brdicka T, et al. 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 2000 191 : 1591 1604.
    • (2000) J Exp Med , vol.191 , pp. 1591-1604
    • Brdicka, T.1
  • 159
    • 0034720166 scopus 로고    scopus 로고
    • Transmembrane phosphoprotein Cbp regulates the activities of Src-family tyrosine kinases
    • Kawabuchi M, et al. Transmembrane phosphoprotein Cbp regulates the activities of Src-family tyrosine kinases. Nature 2000 404 : 999 1003.
    • (2000) Nature , vol.404 , pp. 999-1003
    • Kawabuchi, M.1
  • 160
    • 0030796443 scopus 로고    scopus 로고
    • Inhibitory tyrosine protein kinase p50csk is associated with protein-tyrosine phosphatase PTP-PEST in hemopoietic and non-hemopoietic cells
    • Davidson D, Cloutier JF, Gregorieff A, Veillette A. Inhibitory tyrosine protein kinase p50csk is associated with protein-tyrosine phosphatase PTP-PEST in hemopoietic and non-hemopoietic cells. J Biol Chem 1997 272 : 23455 23462.
    • (1997) J Biol Chem , vol.272 , pp. 23455-23462
    • Davidson, D.1    Cloutier, J.F.2    Gregorieff, A.3    Veillette, A.4
  • 161
    • 0032557659 scopus 로고    scopus 로고
    • Sequence requirements for association of protein-tyrosine phosphatase PEP with the Src homology 3 domain of inhibitory tyrosine protein kinase p50(csk)
    • Gregorieff A, Cloutier JF, Veillette A. Sequence requirements for association of protein-tyrosine phosphatase PEP with the Src homology 3 domain of inhibitory tyrosine protein kinase p50(csk). J Biol Chem 1998 273 : 13217 13222.
    • (1998) J Biol Chem , vol.273 , pp. 13217-13222
    • Gregorieff, A.1    Cloutier, J.F.2    Veillette, A.3
  • 162
    • 0035796465 scopus 로고    scopus 로고
    • PTP-PEST, a scaffold protein tyrosine phosphatase, negatively regulates lymphocyte activation by targeting a unique set of substrates
    • Davidson D, Veillette A. PTP-PEST, a scaffold protein tyrosine phosphatase, negatively regulates lymphocyte activation by targeting a unique set of substrates. EMBO J 2001 20 : 3414 3426.
    • (2001) EMBO J , vol.20 , pp. 3414-3426
    • Davidson, D.1    Veillette, A.2
  • 163
    • 0942279640 scopus 로고    scopus 로고
    • PEST domain-enriched tyrosine phosphatase (PEP) regulation of effector/memory T cells
    • Hasegawa K, Martin F, Huang G, Tumas D, Diehl L, Chan AC. PEST domain-enriched tyrosine phosphatase (PEP) regulation of effector/memory T cells. Science 2004 303 : 685 689.
    • (2004) Science , vol.303 , pp. 685-689
    • Hasegawa, K.1    Martin, F.2    Huang, G.3    Tumas, D.4    Diehl, L.5    Chan, A.C.6
  • 164
    • 38049160121 scopus 로고    scopus 로고
    • Structure, inhibitor, and regulatory mechanism of Lyp, a lymphoid-specific tyrosine phosphatase implicated in autoimmune diseases
    • Yu X, et al. Structure, inhibitor, and regulatory mechanism of Lyp, a lymphoid-specific tyrosine phosphatase implicated in autoimmune diseases. Proc Natl Acad Sci USA 2007 104 : 19767 19772.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 19767-19772
    • Yu, X.1
  • 165
    • 3242713277 scopus 로고    scopus 로고
    • A missense single-nucleotide polymorphism in a gene encoding a protein tyrosine phosphatase (PTPN22) is associated with rheumatoid arthritis
    • Begovich AB, et al. A missense single-nucleotide polymorphism in a gene encoding a protein tyrosine phosphatase (PTPN22) is associated with rheumatoid arthritis. Am J Hum Genet 2004 75 : 330 337.
    • (2004) Am J Hum Genet , vol.75 , pp. 330-337
    • Begovich, A.B.1
  • 166
    • 12144291502 scopus 로고    scopus 로고
    • A functional variant of lymphoid tyrosine phosphatase is associated with type i diabetes
    • Bottini N, et al. A functional variant of lymphoid tyrosine phosphatase is associated with type I diabetes. Nat Genet 2004 36 : 337 338.
    • (2004) Nat Genet , vol.36 , pp. 337-338
    • Bottini, N.1
  • 167
    • 4143105691 scopus 로고    scopus 로고
    • Genetic association of the R620W polymorphism of protein tyrosine phosphatase PTPN22 with human SLE
    • Kyogoku C, et al. Genetic association of the R620W polymorphism of protein tyrosine phosphatase PTPN22 with human SLE. Am J Hum Genet 2004 75 : 504 507.
    • (2004) Am J Hum Genet , vol.75 , pp. 504-507
    • Kyogoku, C.1
  • 168
    • 34548849168 scopus 로고    scopus 로고
    • TRAF1-C5 as a risk locus for rheumatoid arthritis - A genomewide study
    • Plenge RM, et al. TRAF1-C5 as a risk locus for rheumatoid arthritis - a genomewide study. N Engl J Med 2007 357 : 1199 1209.
    • (2007) N Engl J Med , vol.357 , pp. 1199-1209
    • Plenge, R.M.1
  • 170
    • 39549114063 scopus 로고    scopus 로고
    • Associations between human leukocyte antigen, PTPN22, CTLA4 genotypes and rheumatoid arthritis phenotypes of autoantibody status, age at diagnosis and erosions in a large cohort study
    • Karlson EW, et al. Associations between human leukocyte antigen, PTPN22, CTLA4 genotypes and rheumatoid arthritis phenotypes of autoantibody status, age at diagnosis and erosions in a large cohort study. Ann Rheum Dis 2008 67 : 358 363.
    • (2008) Ann Rheum Dis , vol.67 , pp. 358-363
    • Karlson, E.W.1
  • 171
    • 46649095805 scopus 로고    scopus 로고
    • PTPN22 R620W promotes production of anti-AChR autoantibodies and IL-2 in myasthenia gravis
    • Lefvert AK, Zhao Y, Ramanujam R, Yu S, Pirskanen R, Hammarstrom L. PTPN22 R620W promotes production of anti-AChR autoantibodies and IL-2 in myasthenia gravis. J Neuroimmunol 2008 197 : 110 113.
    • (2008) J Neuroimmunol , vol.197 , pp. 110-113
    • Lefvert, A.K.1    Zhao, Y.2    Ramanujam, R.3    Yu, S.4    Pirskanen, R.5    Hammarstrom, L.6
  • 172
    • 33745652977 scopus 로고    scopus 로고
    • Genetic influence of PTPN22 R620W polymorphism in tuberculosis
    • Gomez LM, Anaya JM, Martin J. Genetic influence of PTPN22 R620W polymorphism in tuberculosis. Hum Immunol 2005 66 : 1242 1247.
    • (2005) Hum Immunol , vol.66 , pp. 1242-1247
    • Gomez, L.M.1    Anaya, J.M.2    Martin, J.3
  • 173
    • 28444469783 scopus 로고    scopus 로고
    • Autoimmune-associated lymphoid tyrosine phosphatase is a gain-of-function variant
    • Vang T, et al. Autoimmune-associated lymphoid tyrosine phosphatase is a gain-of-function variant. Nat Genet 2005 37 : 1317 1319.
    • (2005) Nat Genet , vol.37 , pp. 1317-1319
    • Vang, T.1
  • 175
    • 43849091645 scopus 로고    scopus 로고
    • Reduced CD4+ T cell activation in children with type 1 diabetes carrying the PTPN22/Lyp 620Trp variant
    • Aarnisalo J, et al. Reduced CD4+ T cell activation in children with type 1 diabetes carrying the PTPN22/Lyp 620Trp variant. J Autoimmun 2008 31 : 13 21.
    • (2008) J Autoimmun , vol.31 , pp. 13-21
    • Aarnisalo, J.1


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