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Volumn 5, Issue 1, 2005, Pages 43-57

Protein tyrosine phosphatases and the immune response

Author keywords

[No Author keywords available]

Indexed keywords

PHOSPHATASE; PHOSPHOTRANSFERASE; PROTEIN TYROSINE PHOSPHATASE;

EID: 11244277091     PISSN: 14741733     EISSN: None     Source Type: Journal    
DOI: 10.1038/nri1530     Document Type: Review
Times cited : (300)

References (139)
  • 1
    • 0000109995 scopus 로고
    • Transforming gene product of Rous sarcoma virus phosphorylates tyrosine
    • Hunter, T. & Sefton, B. M. Transforming gene product of Rous sarcoma virus phosphorylates tyrosine. Proc. Natl Acad. Sci. USA 77, 1311-1315 (1980).
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 1311-1315
    • Hunter, T.1    Sefton, B.M.2
  • 4
    • 0037304929 scopus 로고    scopus 로고
    • Role of protein tyrosine phosphatases in T cell activation
    • Mustelin, T., Rahmouni, S., Bottini, N. & Alonso, A. Role of protein tyrosine phosphatases in T cell activation. Immunol. Rev. 192, 139-147 (2003).
    • (2003) Immunol. Rev. , vol.192 , pp. 139-147
    • Mustelin, T.1    Rahmouni, S.2    Bottini, N.3    Alonso, A.4
  • 5
    • 0037392883 scopus 로고    scopus 로고
    • Positive and negative regulation of T cell activation through kinases and phosphatases
    • Mustelin, T. & Taskén, K. Positive and negative regulation of T cell activation through kinases and phosphatases. Biochem. J. 371, 15-27 (2003).
    • (2003) Biochem. J. , vol.371 , pp. 15-27
    • Mustelin, T.1    Taskén, K.2
  • 6
    • 2942581416 scopus 로고    scopus 로고
    • Protein tyrosine phosphatases in the human genome
    • Alonso, A. et al. Protein tyrosine phosphatases in the human genome. Cell 117, 699-711 (2004). This paper reviews the entire complement of 107 PTP genes in the human genome.
    • (2004) Cell , vol.117 , pp. 699-711
    • Alonso, A.1
  • 7
    • 0347285350 scopus 로고    scopus 로고
    • A genomic perspective on protein tyrosine phosphatases: Gene structure, pseudogenes, and genetic disease linkage
    • Andersen, J. N. et al. A genomic perspective on protein tyrosine phosphatases: gene structure, pseudogenes, and genetic disease linkage. FASEB J. 18, 8-13 (2004).
    • (2004) FASEB J. , vol.18 , pp. 8-13
    • Andersen, J.N.1
  • 8
    • 0022993986 scopus 로고
    • Antigen activation of murine T cells induces tyrosine phosphorylation of a polypeptide associated with the T cell antigen receptor
    • Samelson, L. E., Patel, M. D., Weissman, A. M., Harford, J. B. & Klausner, R. D. Antigen activation of murine T cells induces tyrosine phosphorylation of a polypeptide associated with the T cell antigen receptor. Cell 46, 1083-1090 (1986).
    • (1986) Cell , vol.46 , pp. 1083-1090
    • Samelson, L.E.1    Patel, M.D.2    Weissman, A.M.3    Harford, J.B.4    Klausner, R.D.5
  • 9
    • 0024380698 scopus 로고
    • T cell activation induces rapid tyrosine phosphorylation of a limited number of cellular substrates
    • Hsi, E. D. et al. T cell activation induces rapid tyrosine phosphorylation of a limited number of cellular substrates. J. Biol. Chem. 264, 10836-10842 (1989).
    • (1989) J. Biol. Chem. , vol.264 , pp. 10836-10842
    • Hsi, E.D.1
  • 10
    • 0025332477 scopus 로고
    • Tyrosine phosphorylation is required for T cell antigen receptor-mediated activation of phospholipase C
    • Mustelin, T., Coggeshall, K. M., Isakov, N. & Altman, A. Tyrosine phosphorylation is required for T cell antigen receptor-mediated activation of phospholipase C. Science 247, 1584-1587 (1990).
    • (1990) Science , vol.247 , pp. 1584-1587
    • Mustelin, T.1    Coggeshall, K.M.2    Isakov, N.3    Altman, A.4
  • 11
    • 0023884930 scopus 로고
    • Activation of a tyrosine protein kinase is an early event in the stimulation of T lymphocytes by interleukin-2
    • Saltzman, E. M., Thom, R. R. & Casnellie, J. E. Activation of a tyrosine protein kinase is an early event in the stimulation of T lymphocytes by interleukin-2. J. Biol. Chem. 263, 6956-6959 (1988).
    • (1988) J. Biol. Chem. , vol.263 , pp. 6956-6959
    • Saltzman, E.M.1    Thom, R.R.2    Casnellie, J.E.3
  • 12
    • 0026353504 scopus 로고
    • Tyrosine phosphorylation of components of the B cell antigen receptors following receptor crosslinking
    • Gold, M. R., Matsuuchi, L., Kelly, R. B. & DeFranco, A. L. Tyrosine phosphorylation of components of the B cell antigen receptors following receptor crosslinking. Proc. Natl Acad. Sci. USA 88, 3436-3440 (1991).
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 3436-3440
    • Gold, M.R.1    Matsuuchi, L.2    Kelly, R.B.3    DeFranco, A.L.4
  • 13
    • 0028483672 scopus 로고
    • T cell antigen receptor signaling: Three families of tyrosine kinases and a phosphatase
    • Mustelin, T. T cell antigen receptor signaling: three families of tyrosine kinases and a phosphatase. Immunity 1, 351-356 (1994).
    • (1994) Immunity , vol.1 , pp. 351-356
    • Mustelin, T.1
  • 14
    • 0027315182 scopus 로고
    • T cell antigen receptor signal transduction: A tale of tails and cytoplasmic protein-tyrosine kinases
    • Weiss, A. T cell antigen receptor signal transduction: a tale of tails and cytoplasmic protein-tyrosine kinases. Cell 73, 209-212 (1993).
    • (1993) Cell , vol.73 , pp. 209-212
    • Weiss, A.1
  • 15
    • 0036357680 scopus 로고    scopus 로고
    • Protein tyrosine phosphatases
    • Mustelin, T. et al. Protein tyrosine phosphatases. Front. Biosci. 7, 85-142 (2002).
    • (2002) Front. Biosci. , vol.7 , pp. 85-142
    • Mustelin, T.1
  • 16
    • 0025224548 scopus 로고
    • Phosphotyrosine phosphatases are involved in reversion of T lymphoblastic proliferation
    • Iivanainen, A. V., Lindqvist, C., Mustelin, T. & Andersson, L. C. Phosphotyrosine phosphatases are involved in reversion of T lymphoblastic proliferation. Eur. J. Immunol. 20, 2509-2512 (1990).
    • (1990) Eur. J. Immunol. , vol.20 , pp. 2509-2512
    • Iivanainen, A.V.1    Lindqvist, C.2    Mustelin, T.3    Andersson, L.C.4
  • 17
    • 0026475905 scopus 로고
    • Activation of human peripheral blood T lymphocytes by pharmacological induction of protein-tyrosine phosphorylation
    • O'Shea, J. J., McVicar, D. W., Bailey, T. L., Burns, C. & Smyth, M. J. Activation of human peripheral blood T lymphocytes by pharmacological induction of protein-tyrosine phosphorylation. Proc. Natl Acad. Sci. USA 89, 10306-10310 (1992).
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 10306-10310
    • O'Shea, J.J.1    McVicar, D.W.2    Bailey, T.L.3    Burns, C.4    Smyth, M.J.5
  • 18
    • 0027417482 scopus 로고
    • Stimulatory effects of the protein tyrosine phosphatase inhibitor, pervanadate, on T-cell activation events
    • Secrist, J. P., Burns, L. A., Karnitz, L., Koretzky, G. A. & Abraham, R. T. Stimulatory effects of the protein tyrosine phosphatase inhibitor, pervanadate, on T-cell activation events. J. Biol. Chem. 268, 5886-5893 (1993). References 17 and 18 were the first papers to show that acute inhibition of PTPs is sufficient to cause T-cell activation.
    • (1993) J. Biol. Chem. , vol.268 , pp. 5886-5893
    • Secrist, J.P.1    Burns, L.A.2    Karnitz, L.3    Koretzky, G.A.4    Abraham, R.T.5
  • 19
    • 0026715644 scopus 로고
    • Phenylarsine oxide augments tyrosine phosphorylation in hematopoietic cells
    • Oetken., C. et al. Phenylarsine oxide augments tyrosine phosphorylation in hematopoietic cells. Eur. J. Haematol. 49, 208-214 (1992).
    • (1992) Eur. J. Haematol. , vol.49 , pp. 208-214
    • Oetken, C.1
  • 20
    • 0021260393 scopus 로고
    • Membranes from T and B lymphocytes have different patterns of tyrosine phosphorylation
    • Earp, H. S., Austin, K. S., Buessow, S. C. & Gillespie, G. Y. Membranes from T and B lymphocytes have different patterns of tyrosine phosphorylation. Proc. Natl Acad. Sci. USA 81, 2347-2351 (1984).
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 2347-2351
    • Earp, H.S.1    Austin, K.S.2    Buessow, S.C.3    Gillespie, G.Y.4
  • 22
    • 0033842973 scopus 로고    scopus 로고
    • Subcellular localization of intracellular protein tyrosine phosphatases in T cells
    • Gjörloff-Wingren, A. et al. Subcellular localization of intracellular protein tyrosine phosphatases in T cells. Eur. J. Immunol. 30, 2412-2421 (2000).
    • (2000) Eur. J. Immunol. , vol.30 , pp. 2412-2421
    • Gjörloff-Wingren, A.1
  • 23
    • 0242712698 scopus 로고    scopus 로고
    • Characterization of TCP-induced receptor-proximal signaling events negatively regulated by the protein tyrosine phosphatase PEP
    • Gjörloff-Wingren, A., Saxena, M., Williams, S., Hammi, D. & Mustelin, T. Characterization of TCP-induced receptor-proximal signaling events negatively regulated by the protein tyrosine phosphatase PEP. Eur. J. Immunol. 29, 3845-3854 (1999).
    • (1999) Eur. J. Immunol. , vol.29 , pp. 3845-3854
    • Gjörloff-Wingren, A.1    Saxena, M.2    Williams, S.3    Hammi, D.4    Mustelin, T.5
  • 24
    • 0034108451 scopus 로고    scopus 로고
    • Cytoskeletal protein tyrosine phosphatase PTPH1 reduces T cell antigen receptor signaling
    • Han, S., Williams, S. & Mustelin, T. Cytoskeletal protein tyrosine phosphatase PTPH1 reduces T cell antigen receptor signaling. Eur. J. Immunol. 30, 1318-1325 (2000).
    • (2000) Eur. J. Immunol. , vol.30 , pp. 1318-1325
    • Han, S.1    Williams, S.2    Mustelin, T.3
  • 25
    • 0037025315 scopus 로고    scopus 로고
    • Activation of ZAP-70 through specific dephosphorylation at the inhibitory Tyr-292 by the low molecular weight phosphotyrosine phosphatase (LMPTP)
    • Bottini, N. et al. Activation of ZAP-70 through specific dephosphorylation at the inhibitory Tyr-292 by the low molecular weight phosphotyrosine phosphatase (LMPTP). J. Biol. Chem. 277, 24220-24224 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 24220-24224
    • Bottini, N.1
  • 26
    • 0027769335 scopus 로고
    • Inhibition of the activity of protein tyrosine phosphatase 1C by its SH2 domains
    • Townley, P., Shen, S.-H., Banville, D. & Ramachandran, C. Inhibition of the activity of protein tyrosine phosphatase 1C by its SH2 domains. Biochemistry 32, 13414-13418 (1993).
    • (1993) Biochemistry , vol.32 , pp. 13414-13418
    • Townley, P.1    Shen, S.-H.2    Banville, D.3    Ramachandran, C.4
  • 27
    • 0028580116 scopus 로고
    • Intramolecular regulation of protein tyrosine phosphatase SH-PTP1: A new function for Src homology 2 domains
    • Pei, D., Lorenz, U., Klingmüller, U., Neel, B. G. & Walsh, C. T. Intramolecular regulation of protein tyrosine phosphatase SH-PTP1: a new function for Src homology 2 domains. Biochemistry 33, 15483-15493 (1994).
    • (1994) Biochemistry , vol.33 , pp. 15483-15493
    • Pei, D.1    Lorenz, U.2    Klingmüller, U.3    Neel, B.G.4    Walsh, C.T.5
  • 28
    • 0028322113 scopus 로고
    • Purification and characterization of PTP2C, a widely distributed protein tyrosine phosphatase containing two SH2 domains
    • Zhao, Z., Larocque, R., Ho, W.-T., Fischer, E. H. & Shen, S.-H. Purification and characterization of PTP2C, a widely distributed protein tyrosine phosphatase containing two SH2 domains. J. Biol. Chem. 269, 8780-8785 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 8780-8785
    • Zhao, Z.1    Larocque, R.2    Ho, W.-T.3    Fischer, E.H.4    Shen, S.-H.5
  • 29
    • 0030061843 scopus 로고    scopus 로고
    • Differential functions of the two Src homology 2 domains in protein tyrosine phosphatase SH-PTP1
    • Pei, D., Wang, J. & Walsh, C. T. Differential functions of the two Src homology 2 domains in protein tyrosine phosphatase SH-PTP1. Proc. Natl Acad. Sci. USA 93, 1141-1145 (1996).
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 1141-1145
    • Pei, D.1    Wang, J.2    Walsh, C.T.3
  • 30
    • 0032548830 scopus 로고    scopus 로고
    • Crystal structure of the tyrosine phosphatase SHP-2
    • Hof, P., Pluskey, S., Dhe-Paganon, S., Eck, M. J. & Shoelson, S. E. Crystal structure of the tyrosine phosphatase SHP-2. Cell 92, 441-450 (1998).
    • (1998) Cell , vol.92 , pp. 441-450
    • Hof, P.1    Pluskey, S.2    Dhe-Paganon, S.3    Eck, M.J.4    Shoelson, S.E.5
  • 31
    • 2942552996 scopus 로고    scopus 로고
    • VHY, a novel, myristoylated testis-restricted dual specificity protein phosphatase related to VHX
    • Alonso, A. et al. VHY, a novel, myristoylated testis-restricted dual specificity protein phosphatase related to VHX. J. Biol. Chem. 279, 32586-32591 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 32586-32591
    • Alonso, A.1
  • 32
    • 0000072679 scopus 로고
    • lck by the CD45 phosphotyrosine phosphatase
    • lck by the CD45 phosphotyrosine phosphatase. Proc. Natl Acad. Sci. USA 86, 6302-6306 (1989). This paper was the first to show that the PTP CD45 can activate the PTK LCK by direct dephosphorylation.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 6302-6306
    • Mustelin, T.1    Coggeshall, K.M.2    Altman, A.3
  • 33
    • 0025303196 scopus 로고
    • lck by the leukocyte common antigen (CD45)
    • lck by the leukocyte common antigen (CD45). Oncogene 5, 809-813 (1990).
    • (1990) Oncogene , vol.5 , pp. 809-813
    • Mustelin, T.1    Altman, A.2
  • 34
    • 0026612351 scopus 로고
    • lyn protein tyrosine kinase by the CD45 phosphotyrosine phosphatase
    • lyn protein tyrosine kinase by the CD45 phosphotyrosine phosphatase. Eur. J. Immunol. 22, 1173-1178 (1992).
    • (1992) Eur. J. Immunol. , vol.22 , pp. 1173-1178
    • Mustelin, T.1
  • 35
    • 0032767536 scopus 로고    scopus 로고
    • Dephosphorylation of ZAP-70 and inhibition of T cell activation by activated SHP1
    • Brockdorff, J., Williams, S., Couture, C. & Mustelin, T. Dephosphorylation of ZAP-70 and inhibition of T cell activation by activated SHP1. Eur. J. Immunol. 29, 2539-2550 (1999).
    • (1999) Eur. J. Immunol. , vol.29 , pp. 2539-2550
    • Brockdorff, J.1    Williams, S.2    Couture, C.3    Mustelin, T.4
  • 36
    • 0026705734 scopus 로고
    • c-src by overexpression of a protein tyrosine phosphatase
    • c-src by overexpression of a protein tyrosine phosphatase. Nature 359, 336-339 (1992).
    • (1992) Nature , vol.359 , pp. 336-339
    • Zheng, X.M.1    Wang, Y.2    Pallen, C.J.3
  • 37
    • 0037082201 scopus 로고    scopus 로고
    • Meeting at mitosis: Cell cycle-specific regulation of c-Src by RPTPα
    • Mustelin, T. & Hunter, T. Meeting at mitosis: cell cycle-specific regulation of c-Src by RPTPα. Sci. STKE [online] 2002, PE3 (2002).
    • (2002) Sci. STKE [Online] , vol.2002
    • Mustelin, T.1    Hunter, T.2
  • 38
    • 0038411479 scopus 로고    scopus 로고
    • Redox regulation of protein tyrosine phosphatase 1B involves a sulphenyl-amide intermediate
    • Salmeen, A. et al. Redox regulation of protein tyrosine phosphatase 1B involves a sulphenyl-amide intermediate. Nature 423, 769-773 (2003).
    • (2003) Nature , vol.423 , pp. 769-773
    • Salmeen, A.1
  • 39
    • 0038749600 scopus 로고    scopus 로고
    • Oxidation state of the active-site cysteine in protein tyrosine phosphatase 1B
    • van Montfort, R. L. M., Congreve, M., Tisi, D., Carr, R. & Jhoti, H. Oxidation state of the active-site cysteine in protein tyrosine phosphatase 1B. Nature 423, 773-777 (2003). References 38 and 39 report the crystallization of oxidized PTP1B and reveal that oxidation of the catalytic cysteine residue results in the formation of a sulphenyl amide moiety, which is resistant to further oxidation (which would be irreversible) and can be reduced back to the catalytically active free cysteinyl.
    • (2003) Nature , vol.423 , pp. 773-777
    • Van Montfort, R.L.M.1    Congreve, M.2    Tisi, D.3    Carr, R.4    Jhoti, H.5
  • 40
    • 4444233558 scopus 로고    scopus 로고
    • Regulation of insulin signaling through reversible oxidation of the protein-tyrosine phosphatases TC45 and PTP1B
    • Meng, T.-C., Buckley, D. A., Galic, S., Tiganis, T. & Tonks, N. K. Regulation of insulin signaling through reversible oxidation of the protein-tyrosine phosphatases TC45 and PTP1B. J. Biol. Chem. 279, 37716-37725 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 37716-37725
    • Meng, T.-C.1    Buckley, D.A.2    Galic, S.3    Tiganis, T.4    Tonks, N.K.5
  • 41
    • 0343621512 scopus 로고    scopus 로고
    • The tumor suppressor PTEN regulates T cell survival and antigen receptor signaling by acting as a phosphatidylinositol 3-phosphatase
    • Wang, X. et al. The tumor suppressor PTEN regulates T cell survival and antigen receptor signaling by acting as a phosphatidylinositol 3-phosphatase. J. Immunol. 164, 1934-1939 (2000).
    • (2000) J. Immunol. , vol.164 , pp. 1934-1939
    • Wang, X.1
  • 42
    • 0035865690 scopus 로고    scopus 로고
    • Requirement of Shp-2 tyrosine phosphatase in lymphoid and hematopoietic cell development
    • Qu, C.-K., Nguyen, S., Chen, J. & Feng, G.-S. Requirement of Shp-2 tyrosine phosphatase in lymphoid and hematopoietic cell development. Blood 97, 911-914 (2001).
    • (2001) Blood , vol.97 , pp. 911-914
    • Qu, C.-K.1    Nguyen, S.2    Chen, J.3    Feng, G.-S.4
  • 43
    • 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 74, 143-156 (1993).
    • (1993) Cell , vol.74 , pp. 143-156
    • Kishihara, K.1
  • 44
    • 0034802515 scopus 로고    scopus 로고
    • Hematopoietic protein tyrosine phosphatase suppresses extracellular stimulus-regulated kinase activation
    • Gronda, M., Arab, S., Iafrate, B., Suzuki, H. & Zanke, B. Hematopoietic protein tyrosine phosphatase suppresses extracellular stimulus-regulated kinase activation. Mol. Cell. Biol. 21, 6851-6858 (2001).
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 6851-6858
    • Gronda, M.1    Arab, S.2    Iafrate, B.3    Suzuki, H.4    Zanke, B.5
  • 45
    • 0033525870 scopus 로고    scopus 로고
    • Increased insulin sensitivity and obesity resistance in mice lacking the protein tyrosine phosphatase-1B gene
    • Elchebly, M. et al. Increased insulin sensitivity and obesity resistance in mice lacking the protein tyrosine phosphatase-1B gene. Science 283, 1544-1548 (1999).
    • (1999) Science , vol.283 , pp. 1544-1548
    • Elchebly, M.1
  • 46
    • 0030769147 scopus 로고    scopus 로고
    • Impaired bone marrow microenvironment and immune function in T cell protein tyrosine phosphatase-deficient mice
    • You-Ten, K. E. et al. Impaired bone marrow microenvironment and immune function in T cell protein tyrosine phosphatase-deficient mice. J. Exp. Med. 186, 683-693 (1997).
    • (1997) J. Exp. Med. , vol.186 , pp. 683-693
    • You-Ten, K.E.1
  • 47
    • 0011185737 scopus 로고
    • Tine leukocyte common antigen (CD45): A putative receptor-linked protein tyrosine phosphatase
    • Charbonneau, H., Tonks, N. K., Walsh, K. A. & Fischer, E. H. Tine leukocyte common antigen (CD45): a putative receptor-linked protein tyrosine phosphatase. Proc. Natl Acad. Sci. USA 85, 7182-7186 (1988).
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 7182-7186
    • Charbonneau, H.1    Tonks, N.K.2    Walsh, K.A.3    Fischer, E.H.4
  • 48
    • 0024206455 scopus 로고
    • Demonstration that the leukocyte common antigen CD45 is a protein tyrosine phosphatase
    • Tonks, N. K., Charbonneau, H., Diltz, C. D., Fischer, E. H. & Walsh, K. A. Demonstration that the leukocyte common antigen CD45 is a protein tyrosine phosphatase. Biochemistry 27, 8695-8701 (1988). Although reference 47 was the first to report that CD45 has a high degree of homology with the first identified PTP, PTP1B, and therefore was likely to be a PTP itself, reference 48 directly showed this by providing evidence that CD45 has tyrosine-phosphatase activity.
    • (1988) Biochemistry , vol.27 , pp. 8695-8701
    • Tonks, N.K.1    Charbonneau, H.2    Diltz, C.D.3    Fischer, E.H.4    Walsh, K.A.5
  • 49
    • 0024416009 scopus 로고
    • Evidence that the leukocyte-common antigen is required for antigen-induced T lymphocyte proliferation
    • Pingel, J. T. & Thomas, M. L. Evidence that the leukocyte-common antigen is required for antigen-induced T lymphocyte proliferation. Cell 58, 1055-1065 (1989). This paper was the first to show that expression of CD45 is important for T-cell activation.
    • (1989) Cell , vol.58 , pp. 1055-1065
    • Pingel, J.T.1    Thomas, M.L.2
  • 50
    • 0038815306 scopus 로고    scopus 로고
    • CD45: A critical regulator of signaling thresholds in immune cells
    • Hermiston, M. L., Xu, Z. & Weiss, A. CD45: a critical regulator of signaling thresholds in immune cells. Annu. Rev. Immunol. 21, 107-137 (2003).
    • (2003) Annu. Rev. Immunol. , vol.21 , pp. 107-137
    • Hermiston, M.L.1    Xu, Z.2    Weiss, A.3
  • 51
    • 0025297050 scopus 로고
    • Tyrosine phosphatase CD45 is essential for coupling T-cell antigen receptor to the phosphatidyl inositol pathway
    • Koretzky, G. A., Picus, J., Thomas, M. L. & Weiss, A. Tyrosine phosphatase CD45 is essential for coupling T-cell antigen receptor to the phosphatidyl inositol pathway. Nature 346, 66-68 (1990).
    • (1990) Nature , vol.346 , pp. 66-68
    • Koretzky, G.A.1    Picus, J.2    Thomas, M.L.3    Weiss, A.4
  • 52
    • 0026672283 scopus 로고
    • 2+ oscillations
    • 2+ oscillations. J. Exp. Med. 176, 835-844 (1992).
    • (1992) J. Exp. Med. , vol.176 , pp. 835-844
    • Volarevic, S.1
  • 53
    • 0024316870 scopus 로고
    • Expression of CD45 alters phosphorylation of the Lck-encoded tyrosine protein kinase in murine lymphoma T-cell lines
    • Ostergaard, H. L. 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 86, 8959-8963 (1989).
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 8959-8963
    • Ostergaard, H.L.1
  • 54
    • 0033049188 scopus 로고    scopus 로고
    • lck Y505F mutation in CD45-deficient mice rescues thymocyte development
    • lck Y505F mutation in CD45-deficient mice rescues thymocyte development. Mol. Cell. Biol. 19, 4200-4208 (1999).
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 4200-4208
    • Seavitt, J.1
  • 55
    • 0027263368 scopus 로고
    • Regulation of src family tyrosine kinases in lymphocytes
    • Mustelin, T. & Burn, P. Regulation of src family tyrosine kinases in lymphocytes. Trends Biochem. Sci. 18, 215-220 (1993).
    • (1993) Trends Biochem. Sci. , vol.18 , pp. 215-220
    • Mustelin, T.1    Burn, P.2
  • 56
    • 0037370491 scopus 로고    scopus 로고
    • Phosphorylation-dependent regulation of T cell actuation by PAG/Cbp, a lipid raft-associated transmembrane adaptor
    • Davidson, D., Bakinowski, M., Thomas, M. L., Horejsi, V. & Veillette, A. Phosphorylation-dependent regulation of T cell actuation by PAG/Cbp, a lipid raft-associated transmembrane adaptor. Mol. Cell. Biol. 23, 2017-2025 (2003).
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 2017-2025
    • Davidson, D.1    Bakinowski, M.2    Thomas, M.L.3    Horejsi, V.4    Veillette, A.5
  • 57
    • 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 404, 999-1003 (2000).
    • (2000) Nature , vol.404 , pp. 999-1003
    • Kawabuchi, M.1
  • 58
    • 0342313755 scopus 로고    scopus 로고
    • Phosphoprotein associated with glycosphingolipid-enriched microdomains (PAG), a novel ubiquitously expressed transmembrane adapter 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 adapter protein, binds the protein tyrosine kinase Csk and is involved in regulation of T cell activation. J. Exp. Med. 191, 1591-1604 (2000).
    • (2000) J. Exp. Med. , vol.191 , pp. 1591-1604
    • Brdicka, T.1
  • 59
    • 0035800835 scopus 로고    scopus 로고
    • Release from tonic inhibition of T cell activation through transient displacement of C-terminal Src kinase (Csk) from lipid rafts
    • Torgersen, K. M. et al. Release from tonic inhibition of T cell activation through transient displacement of C-terminal Src kinase (Csk) from lipid rafts. J. Biol. Chem. 276, 29313-29318 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 29313-29318
    • Torgersen, K.M.1
  • 60
    • 0038719674 scopus 로고    scopus 로고
    • Combined spatial and enzymatic regulation of Csk by cAMP and protein kinase A inhibits T cell receptor signaling
    • Vang, T., Abrahamsen, H., Myklebust, S., Horejsi, V. & Taskén, K. Combined spatial and enzymatic regulation of Csk by cAMP and protein kinase A inhibits T cell receptor signaling. J. Biol. Chem. 278, 17597-17604 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 17597-17604
    • Vang, T.1    Abrahamsen, H.2    Myklebust, S.3    Horejsi, V.4    Taskén, K.5
  • 61
    • 4444270866 scopus 로고    scopus 로고
    • Knockdown of C-terminal Src kinase by siRNA-mediated RNA interference augments T cell receptor signaling in mature T cells
    • Vang, T. et al. Knockdown of C-terminal Src kinase by siRNA-mediated RNA interference augments T cell receptor signaling in mature T cells. Eur. J. Immunol. 34, 2191-2199 (2004).
    • (2004) Eur. J. Immunol. , vol.34 , pp. 2191-2199
    • Vang, T.1
  • 62
    • 10744223870 scopus 로고    scopus 로고
    • Shp2 regulates Src family kinase activity and Ras/Erk activation by controlling Csk recruitment
    • Zhang, S. Q. et al. Shp2 regulates Src family kinase activity and Ras/Erk activation by controlling Csk recruitment. Mol. Cell 13, 341-351 (2004).
    • (2004) Mol. Cell , vol.13 , pp. 341-351
    • Zhang, S.Q.1
  • 63
    • 0009013817 scopus 로고
    • CD45 regulates signal transduction and lymphocyte activation by specific association with receptor molecules on T or B cells
    • Ledbetter, J. A., Tonks, N. K., Fischer, E. H. & Clark, E. A. CD45 regulates signal transduction and lymphocyte activation by specific association with receptor molecules on T or B cells. Proc. Natl Acad. Sci. USA 85, 8628-8633 (1988).
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 8628-8633
    • Ledbetter, J.A.1    Tonks, N.K.2    Fischer, E.H.3    Clark, E.A.4
  • 64
    • 0024343604 scopus 로고
    • CD45-protein tyrosine phosphatase cross-linking inhibits T cell receptor CD3-mediated activation in human T cells
    • Kiener, P. A. & Mittler, R. S. CD45-protein tyrosine phosphatase cross-linking inhibits T cell receptor CD3-mediated activation in human T cells. J. Immunol. 143, 23-28 (1989).
    • (1989) J. Immunol. , vol.143 , pp. 23-28
    • Kiener, P.A.1    Mittler, R.S.2
  • 66
    • 0027289547 scopus 로고
    • Regulation of TCR signaling by CD45 lacking transmembrane and extracellular domains
    • Volarevic, S. et al. Regulation of TCR signaling by CD45 lacking transmembrane and extracellular domains. Science 260, 541-544 (1993).
    • (1993) Science , vol.260 , pp. 541-544
    • Volarevic, S.1
  • 67
    • 0027997103 scopus 로고
    • Specific interaction of the CD45 protein-tyrosine phosphatase with tyrosine phosphorylated CD3 ζ chain
    • Furukawa, T., Itoh, M., Krueger, N. X., Streuli, M. & Saito, H. Specific interaction of the CD45 protein-tyrosine phosphatase with tyrosine phosphorylated CD3 ζ chain. Proc. Natl Acad. Sci. USA 91, 10928-10932 (1994).
    • (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
  • 68
    • 0028987733 scopus 로고
    • zap tyrosine protein kinase by the CD45 phosphotyrosine phosphatase in T cells
    • zap tyrosine protein kinase by the CD45 phosphotyrosine phosphatase in T cells. Eur. J. Immunol. 25, 942-946 (1995).
    • (1995) Eur. J. Immunol. , vol.25 , pp. 942-946
    • Mustelin, T.1
  • 69
    • 0029779003 scopus 로고    scopus 로고
    • Mutational analysis of Lck in CD45-negative T cells: Dominant role of tyrosine 394 phosphorylation in kinase activity
    • D'Oro, U., Sakaguchi, K., Appella, E. & Ashwell, J. D. Mutational analysis of Lck in CD45-negative T cells: dominant role of tyrosine 394 phosphorylation in kinase activity. Mol. Cell. Biol. 16, 4996-5003 (1996).
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 4996-5003
    • D'Oro, U.1    Sakaguchi, K.2    Appella, E.3    Ashwell, J.D.4
  • 70
    • 0033178727 scopus 로고    scopus 로고
    • CD45 negatively regulates Lyn activity by dephosphorylating both positive and negate regulatory tyrosine residues in immature B cells
    • Katagiri, T. et al. CD45 negatively regulates Lyn activity by dephosphorylating both positive and negate regulatory tyrosine residues in immature B cells. J. Immunol. 163, 1321-1330 (1999).
    • (1999) J. Immunol. , vol.163 , pp. 1321-1330
    • Katagiri, T.1
  • 71
    • 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, T. A., Johnson, K. G., Shah, D. D. & Thomas, M. L. Targeting of CD45 protein tyrosine phosphatase activity to lipid microdomains on the T cell surface inhibits TCR signaling. Eur. J. Immunol. 32, 2578-2584 (2002).
    • (2002) Eur. J. Immunol. , vol.32 , pp. 2578-2584
    • He, X.1    Woodford-Thomas, T.A.2    Johnson, K.G.3    Shah, D.D.4    Thomas, M.L.5
  • 72
    • 0032530369 scopus 로고    scopus 로고
    • Engagement of T cell receptor triggers its recruitment to low-density detergent-insoluble membrane domains
    • Montixi, C. et al. Engagement of T cell receptor triggers its recruitment to low-density detergent-insoluble membrane domains. EMBO J. 17, 5334-5340 (1998).
    • (1998) EMBO J. , vol.17 , pp. 5334-5340
    • Montixi, C.1
  • 73
    • 0036839104 scopus 로고    scopus 로고
    • Dynamic association of CD45 with detergent-insoluble microdomains in T lymphocytes
    • Edmonds, S. D. & Ostergaard, H. L. Dynamic association of CD45 with detergent-insoluble microdomains in T lymphocytes. J. Immunol. 169, 5036-5046 (2002).
    • (2002) J. Immunol. , vol.169 , pp. 5036-5046
    • Edmonds, S.D.1    Ostergaard, H.L.2
  • 74
    • 0037318863 scopus 로고    scopus 로고
    • CD45 ectodomain controls interaction with GEMs and Lck activity for optimal TCR signaling
    • Iries, C. et al. CD45 ectodomain controls interaction with GEMs and Lck activity for optimal TCR signaling. Nature Immunol. 4, 189-192 (2003).
    • (2003) Nature Immunol. , vol.4 , pp. 189-192
    • Iries, C.1
  • 75
    • 0036794399 scopus 로고    scopus 로고
    • Staging and resetting T cell activation in SMACs
    • Freiberg, B. A. et al. Staging and resetting T cell activation in SMACs. Nature Immunol. 3, 911-916 (2002).
    • (2002) Nature Immunol. , vol.3 , pp. 911-916
    • Freiberg, B.A.1
  • 76
    • 0032472226 scopus 로고    scopus 로고
    • Dimerization-induced inhibition of receptor protein tyrosine phosphatase function through an inhibitory wedge
    • Majeti, R., Bilwes, A. M., Noel, J. P., Hunter, T. & Weiss, A. Dimerization-induced inhibition of receptor protein tyrosine phosphatase function through an inhibitory wedge. Science 279, 88-91 (1998).
    • (1998) Science , vol.279 , pp. 88-91
    • Majeti, R.1    Bilwes, A.M.2    Noel, J.P.3    Hunter, T.4    Weiss, A.5
  • 77
    • 0034704180 scopus 로고    scopus 로고
    • An inactivating point mutation in the inhibitory wedge of CD45 causes lymphoproliferation and auto immunity
    • Majeti, R. et al. An inactivating point mutation in the inhibitory wedge of CD45 causes lymphoproliferation and autoimmunity. Cell 103, 1059-1069 (2000).
    • (2000) Cell , vol.103 , pp. 1059-1069
    • Majeti, R.1
  • 78
    • 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. Nature Immunol. 3, 764-770 (2002).
    • (2002) Nature Immunol. , vol.3 , pp. 764-770
    • Xu, Z.1    Weiss, A.2
  • 79
    • 0026569663 scopus 로고
    • Isoform-specific associations of CD45 with accessory molecules in human T lymphocytes
    • Dianzani, U. et al. Isoform-specific associations of CD45 with accessory molecules in human T lymphocytes. Eur. J. Immunol. 22, 365-371 (1992).
    • (1992) Eur. J. Immunol. , vol.22 , pp. 365-371
    • Dianzani, U.1
  • 80
    • 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, R. J., Bowne, D. B., Flores, E. & Thomas, M. L. 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. 12, 2396-2405 (1992).
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 2396-2405
    • Matthews, R.J.1    Bowne, D.B.2    Flores, E.3    Thomas, M.L.4
  • 81
    • 0031172446 scopus 로고    scopus 로고
    • Immunoreceptor tyrosine-based inhibition motifs
    • Vivier, E. & Daëron, M. Immunoreceptor tyrosine-based inhibition motifs. Immunol. Today 18, 286-291 (1997).
    • (1997) Immunol. Today , vol.18 , pp. 286-291
    • Vivier, E.1    Daëron, M.2
  • 82
    • 0001329440 scopus 로고    scopus 로고
    • T cell activation: The coming of the phosphatases
    • Mustelin, T. et al. T cell activation: the coming of the phosphatases. Front. Biosci. 3, D1060-D1096 (1998).
    • (1998) Front. Biosci. , vol.3
    • Mustelin, T.1
  • 83
    • 0035933771 scopus 로고    scopus 로고
    • Specific dephosphorylation of the Lck tyrosine protein kinase at Tyr-394 by the SHP-1 protein-tyrosine phosphatase
    • Chiang, G. G. & Sefton, B. M. Specific dephosphorylation of the Lck tyrosine protein kinase at Tyr-394 by the SHP-1 protein-tyrosine phosphatase. J. Biol. Chem. 276, 23173-23179 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 23173-23179
    • Chiang, G.G.1    Sefton, B.M.2
  • 84
    • 0029904324 scopus 로고    scopus 로고
    • LCK phosphorylation and ZAP-70 binding to T cell receptor ζ chain
    • LCK phosphorylation and ZAP-70 binding to T cell receptor ζ chain. Biochem. Biophys. Res. Commun. 222, 50-57 (1996).
    • (1996) Biochem. Biophys. Res. Commun. , vol.222 , pp. 50-57
    • Raab, M.1    Rudd, C.E.2
  • 85
    • 0027195626 scopus 로고
    • Motheaten and viable motheaten mice have mutations in the haematopoietic cell phosphatase gene
    • Tsui, H. W., Siminovitch, K. A., de Souza, L. & Tsui, F. W. L. Motheaten and viable motheaten mice have mutations in the haematopoietic cell phosphatase gene. Nature Genet. 4, 124-129 (1993).
    • (1993) Nature Genet. , vol.4 , pp. 124-129
    • Tsui, H.W.1    Siminovitch, K.A.2    De Souza, L.3    Tsui, F.W.L.4
  • 86
    • 0017105510 scopus 로고
    • Motheaten, an immunodeficient mutant of the mouse. II. Depressed immune competence and elevated serum immunoglobulins
    • Shultz, L. D. & Green, M. C. Motheaten, an immunodeficient mutant of the mouse. II. Depressed immune competence and elevated serum immunoglobulins. J. Immunol. 116, 936-943 (1976).
    • (1976) J. Immunol. , vol.116 , pp. 936-943
    • Shultz, L.D.1    Green, M.C.2
  • 87
    • 0029787216 scopus 로고    scopus 로고
    • Signaling capacity of the T cell antigen receptor is negatively regulated by the PTP1C tyrosine phosphatase
    • Pani, G., Fischer, K.-D., Mlinaric-Rascan, I. & Siminovitch, K. A. Signaling capacity of the T cell antigen receptor is negatively regulated by the PTP1C tyrosine phosphatase. J. Exp. Med. 184, 839-852 (1996).
    • (1996) J. Exp. Med. , vol.184 , pp. 839-852
    • Pani, G.1    Fischer, K.-D.2    Mlinaric-Rascan, I.3    Siminovitch, K.A.4
  • 88
    • 9144224359 scopus 로고    scopus 로고
    • CD22 is a functional ligand for SHP1 in primary T cells
    • Sathish, J. G. et al. CD22 is a functional ligand for SHP1 in primary T cells. J. Biol. Chem. 279, 47783-47791 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 47783-47791
    • Sathish, J.G.1
  • 90
    • 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. 15, 4909-4918 (1996).
    • (1996) EMBO J. , vol.15 , pp. 4909-4918
    • Cloutier, J.-F.1    Veillette, A.2
  • 91
    • 0033521596 scopus 로고    scopus 로고
    • Cooperative inhibition of T-cell antigen receptor signaling by a complex between a kinase and a phosphatase
    • Cloutier, J.-F. & Veillette, A, Cooperative inhibition of T-cell antigen receptor signaling by a complex between a kinase and a phosphatase. J. Exp. Med. 189, 111-121 (1999). References 90 and 91 document the high-stoichiometry association between the PEP phosphatase and the inhibitory kinase CSK. The papers conclude that the interaction between the two enzymes helps PEP reach its SRC-family PTK targets.
    • (1999) J. Exp. Med. , vol.189 , pp. 111-121
    • Cloutier, J.-F.1    Veillette, A.2
  • 92
    • 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, C. M. Cloning and characterization of a lymphoid-specific, inducible human protein tyrosine phosphatase, Lyp. Blood 93, 2013-2024 (1999).
    • (1999) Blood , vol.93 , pp. 2013-2024
    • Cohen, S.1    Dadi, H.2    Shaoul, E.3    Sharfe, N.4    Roifman, C.M.5
  • 93
    • 12144291502 scopus 로고    scopus 로고
    • A functional variant of lymphoid tyrosine phosphatase is associated with type 1 diabetes
    • Bottini, N. et al. A functional variant of lymphoid tyrosine phosphatase is associated with type 1 diabetes. Nature Genet. 36, 337-338 (2004). This paper reports that a single amino-acid substitution at position 620 of the human PTP LYP is sufficient to cause a marked increase in the incidence of type 1 diabetes. This increase correlates with a loss of association with CSK.
    • (2004) Nature Genet. , vol.36 , pp. 337-338
    • Bottini, N.1
  • 94
    • 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, A. B. 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. 75, 330-337 (2004).
    • (2004) Am. J. Hum. Genet. , vol.75 , pp. 330-337
    • Begovich, A.B.1
  • 95
    • 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. 75, 504-507 (2004).
    • (2004) Am. J. Hum. Genet. , vol.75 , pp. 504-507
    • Kyogoku, C.1
  • 96
    • 7044253358 scopus 로고    scopus 로고
    • Replication of an association between the lymphoid tyrosine phosphatase locus (LYP/PTPN22) with type 1 diabetes, and evidence for its role as a general autoimmunity locus
    • Smyth, D. et al. Replication of an association between the lymphoid tyrosine phosphatase locus (LYP/PTPN22) with type 1 diabetes, and evidence for its role as a general autoimmunity locus. Diabetes 53, 3020-3023 (2004).
    • (2004) Diabetes , vol.53 , pp. 3020-3023
    • Smyth, D.1
  • 97
    • 0942279640 scopus 로고    scopus 로고
    • PEST domain-enriched tyrosine phosphatase (PEP) regulation of effector/memory T cells
    • -/- mice.
    • (2004) Science , vol.303 , pp. 685-689
    • Hasegawa, K.1
  • 98
    • 0030796443 scopus 로고    scopus 로고
    • csk is associated with protein-tyrosine phosphatase PTP-PEST in hemopoietic and non-hemopoietic cells
    • csk is associated with protein-tyrosine phosphatase PTP-PEST in hemopoietic and non-hemopoietic cells. J. Biol. Chem. 272, 23455-23462 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 23455-23462
    • Davidson, D.1    Cloutier, J.F.2    Gregorieff, A.3    Veillette, A.4
  • 99
    • 0035141252 scopus 로고    scopus 로고
    • SH2 domain-mediated interaction of inhibitory protein tyrosine kinase Csk with protein tyrosine phosphatase-HSCF
    • Wang, B., Lemay, S., Tsai, S. & Veillette, A. SH2 domain-mediated interaction of inhibitory protein tyrosine kinase Csk with protein tyrosine phosphatase-HSCF. Mol. Cell. Biol. 21, 1077-1088 (2001).
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 1077-1088
    • Wang, B.1    Lemay, S.2    Tsai, S.3    Veillette, A.4
  • 100
    • 0040821207 scopus 로고    scopus 로고
    • Combination of gene targeting and substrate trapping to identify substrates of protein tyrosine phosphatases using PTP-PEST as a model
    • Cote, J. F., Charest, A., Wagner, J. & Tremblay, M. L. Combination of gene targeting and substrate trapping to identify substrates of protein tyrosine phosphatases using PTP-PEST as a model. Biochemistry 37, 13128-13137 (1998).
    • (1998) Biochemistry , vol.37 , pp. 13128-13137
    • Cote, J.F.1    Charest, A.2    Wagner, J.3    Tremblay, M.L.4
  • 101
    • 0029826289 scopus 로고    scopus 로고
    • cas as a substrate for the cytosolic protein tyrosine phosphatase PTP-PEST
    • cas as a substrate for the cytosolic protein tyrosine phosphatase PTP-PEST. Mol. Cell. Biol. 16, 6408-6418 (1996).
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 6408-6418
    • Garton, A.J.1    Flint, A.J.2    Tonks, N.K.3
  • 102
    • 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. 20, 3414-3426 (2001).
    • (2001) EMBO J. , vol.20 , pp. 3414-3426
    • Davidson, D.1    Veillette, A.2
  • 103
    • 0030872948 scopus 로고    scopus 로고
    • PSTPIP: A tyrosine phosphorylated cleavage furrow-associated protein that is a substrate for a PEST tyrosine phosphatase
    • Spencer, S. et al. PSTPIP: a tyrosine phosphorylated cleavage furrow-associated protein that is a substrate for a PEST tyrosine phosphatase. J. Cell Biol. 138, 845-860 (1997).
    • (1997) J. Cell Biol. , vol.138 , pp. 845-860
    • Spencer, S.1
  • 104
    • 10744226224 scopus 로고    scopus 로고
    • PTPH1 is a predominant protein-tyrosine phosphatase capable of interacting with and dephosphorylating the T cell receptor ζ subunit
    • Sozio, M. S. et al. PTPH1 is a predominant protein-tyrosine phosphatase capable of interacting with and dephosphorylating the T cell receptor ζ subunit. J. Biol. Chem. 279, 7760-7768 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 7760-7768
    • Sozio, M.S.1
  • 105
    • 0033580911 scopus 로고    scopus 로고
    • Identification of the cell cycle regulator VCP (p97/CDC48) as a substrate of the band 4.1-related protein-tyrosine phosphatase PTPH1
    • Zhang, S.-H., Liu, J., Kobayashi, R. & Tonks, N. K. Identification of the cell cycle regulator VCP (p97/CDC48) as a substrate of the band 4.1-related protein-tyrosine phosphatase PTPH1. J. Biol. Chem. 274, 17806-17812 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 17806-17812
    • Zhang, S.-H.1    Liu, J.2    Kobayashi, R.3    Tonks, N.K.4
  • 106
    • 0026660330 scopus 로고
    • VCP, the mammalian homolog of CDC48, is tyrosine phosphorylated in response to T cell antigen receptor activation
    • Egerton, M. et al. VCP, the mammalian homolog of CDC48, is tyrosine phosphorylated in response to T cell antigen receptor activation. EMBO J. 11, 3533-3540 (1992).
    • (1992) EMBO J. , vol.11 , pp. 3533-3540
    • Egerton, M.1
  • 107
    • 0034610335 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of p97 regulates transitional endoplasmic reticulum assembly in vitro
    • Lavoie, C. et al. Tyrosine phosphorylation of p97 regulates transitional endoplasmic reticulum assembly in vitro. Proc. Natl Acad. Sci. USA 97, 13637-13642 (2000).
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 13637-13642
    • Lavoie, C.1
  • 108
    • 0037044786 scopus 로고    scopus 로고
    • Evidence for regulation of the tumor necrosis factor α-convertase (TACE) by protein-tyrosine phosphatase PTPH1
    • Zheng, Y., Schlondorff, J. & Biobel, C. P. Evidence for regulation of the tumor necrosis factor α-convertase (TACE) by protein-tyrosine phosphatase PTPH1. J. Biol. Chem. 277, 42463-42470 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 42463-42470
    • Zheng, Y.1    Schlondorff, J.2    Biobel, C.P.3
  • 109
    • 0031048053 scopus 로고    scopus 로고
    • Regulation of the low molecular weight phosphotyrosine phosphatase (LMPTP) by phosphorylation at tyrosines 131 and 132
    • Tailor, P., Williams, S., Gilman, J., Couture, C, & Mustelin, T. Regulation of the low molecular weight phosphotyrosine phosphatase (LMPTP) by phosphorylation at tyrosines 131 and 132. J. Biol. Chem. 272, 5371-5376 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 5371-5376
    • Tailor, P.1    Williams, S.2    Gilman, J.3    Couture, C.4    Mustelin, T.5
  • 110
    • 0035895980 scopus 로고    scopus 로고
    • Inhibitory role for dual-specificity phosphatase VHR in T cell antigen receptor and CD28-induced Erk and Jnk activation
    • Alonso, A., Saxena, M., Williams, S. & Mustelin, T. Inhibitory role for dual-specificity phosphatase VHR in T cell antigen receptor and CD28-induced Erk and Jnk activation. J. Biol. Chem. 276, 4766-4771 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 4766-4771
    • Alonso, A.1    Saxena, M.2    Williams, S.3    Mustelin, T.4
  • 111
    • 0037232078 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of VHR phosphatase by ZAP-70
    • Alonso, A. et al. Tyrosine phosphorylation of VHR phosphatase by ZAP-70. Nature Immunol. 4, 44-48 (2003).
    • (2003) Nature Immunol. , vol.4 , pp. 44-48
    • Alonso, A.1
  • 112
    • 0033800083 scopus 로고    scopus 로고
    • Extracellular signals and scores of phosphatases: All roads lead to MAP kinase
    • Saxena, M. & Mustelin, T. Extracellular signals and scores of phosphatases: all roads lead to MAP kinase. Semin. Immunol. 12, 387-396 (2000).
    • (2000) Semin. Immunol. , vol.12 , pp. 387-396
    • Saxena, M.1    Mustelin, T.2
  • 113
    • 0032546961 scopus 로고    scopus 로고
    • Negative regulation of T cell antigen receptor signaling by hematopoietic tyrosine phosphatase (HePTP)
    • Saxena, M., Williams, S., Gilman, J. & Mustelin, T. Negative regulation of T cell antigen receptor signaling by hematopoietic tyrosine phosphatase (HePTP). J. Biol. Chem. 273, 15340-15344 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 15340-15344
    • Saxena, M.1    Williams, S.2    Gilman, J.3    Mustelin, T.4
  • 114
    • 0033597122 scopus 로고    scopus 로고
    • Inhibition of T cell signaling by MAP kinase-targeted hematopoietic tyrosine phosphatase (HePTP)
    • Saxena, M., Williams, S., Brockdorff, J., Gilman, J. & Mustelin, T. Inhibition of T cell signaling by MAP kinase-targeted hematopoietic tyrosine phosphatase (HePTP). J. Biol. Chem. 274, 11693-11700 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 11693-11700
    • Saxena, M.1    Williams, S.2    Brockdorff, J.3    Gilman, J.4    Mustelin, T.5
  • 115
    • 0033193930 scopus 로고    scopus 로고
    • Crosstalk between cAMP-dependent kinase and MAP kinase through hematopoietic protein tyrosine phosphatase (HePTP)
    • Saxena, M., Williams, S., Taskén, K. & Mustelin, T. Crosstalk between cAMP-dependent kinase and MAP kinase through hematopoietic protein tyrosine phosphatase (HePTP). Nature Cell Biol. 1, 305-311 (1999).
    • (1999) Nature Cell Biol. , vol.1 , pp. 305-311
    • Saxena, M.1    Williams, S.2    Taskén, K.3    Mustelin, T.4
  • 116
    • 1642414254 scopus 로고    scopus 로고
    • Hematopoietic protein tyrosine phosphatase (HePTP) phosphorylation by cAMP-dependent protein kinase in T cells: Dynamics and subcellular location
    • Nika, K. et al. Hematopoietic protein tyrosine phosphatase (HePTP) phosphorylation by cAMP-dependent protein kinase in T cells: dynamics and subcellular location. Biochem. J. 378, 335-342 (2004).
    • (2004) Biochem. J. , vol.378 , pp. 335-342
    • Nika, K.1
  • 117
    • 0028956353 scopus 로고
    • Specific recruitment of SH-PTP1 to the erythropoietin receptor causes inactivation of JAK2 and termination of proliferative signals
    • Klingmüller, U., Lorenz, U., Cantley, L. C., Neel, B. G. & Lodish, H. F. Specific recruitment of SH-PTP1 to the erythropoietin receptor causes inactivation of JAK2 and termination of proliferative signals. Cell 80, 729-738 (1995).
    • (1995) Cell , vol.80 , pp. 729-738
    • Klingmüller, U.1    Lorenz, U.2    Cantley, L.C.3    Neel, B.G.4    Lodish, H.F.5
  • 118
    • 0035930501 scopus 로고    scopus 로고
    • TYK2 and JAK2 are substrates of protein-tyrosine phosphatase 1B
    • Myers, M. P. et al. TYK2 and JAK2 are substrates of protein-tyrosine phosphatase 1B. J. Biol. Chem. 276, 47771-47774 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 47771-47774
    • Myers, M.P.1
  • 119
    • 0036318564 scopus 로고    scopus 로고
    • Identification of a nuclear Stat1 protein tyrosine phosphatase
    • ten Hoeve, J. et al. Identification of a nuclear Stat1 protein tyrosine phosphatase. Mol. Cell. Biol. 22, 5662-5668 (2002).
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 5662-5668
    • Ten Hoeve, J.1
  • 120
    • 0037184022 scopus 로고    scopus 로고
    • Arginine methylation of STAT1 regulates its dephosphorylation by TcPTP
    • Zhu, W., Mustelin, T. & David, M. Arginine methylation of STAT1 regulates its dephosphorylation by TcPTP. J. Biol. Chem. 277, 35787-35790 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 35787-35790
    • Zhu, W.1    Mustelin, T.2    David, M.3
  • 121
    • 0036570013 scopus 로고    scopus 로고
    • Enlargement of secretory vesicles by protein tyrosine phosphatase PTP-MEG2 in RBL mast cells and Jurkat T cells
    • Wang, X. et al. Enlargement of secretory vesicles by protein tyrosine phosphatase PTP-MEG2 in RBL mast cells and Jurkat T cells. J. Immunol. 168, 4612-4619 (2004).
    • (2004) J. Immunol. , vol.168 , pp. 4612-4619
    • Wang, X.1
  • 122
    • 0346996866 scopus 로고    scopus 로고
    • Homotypic secretory vesicle fusion induced by the protein tyrosine phosphatase MEG2 depends on polyphosphoinositides in T cells
    • Huynh, H. et al. Homotypic secretory vesicle fusion induced by the protein tyrosine phosphatase MEG2 depends on polyphosphoinositides in T cells. J. Immunol. 171, 6661-6671 (2003).
    • (2003) J. Immunol. , vol.171 , pp. 6661-6671
    • Huynh, H.1
  • 123
    • 4444247676 scopus 로고    scopus 로고
    • Control of vesicle fusion by a tyrosine phosphatase
    • Huynh, H. et al. Control of vesicle fusion by a tyrosine phosphatase. Nature Cell Biol. 6, 831-839 (2004).
    • (2004) Nature Cell Biol. , vol.6 , pp. 831-839
    • Huynh, H.1
  • 125
    • 2142710163 scopus 로고    scopus 로고
    • Altered lipid raft-associated signaling and ganglioside expression in T lymphocytes from patients with systemic lupus erythematosus
    • Jury, E. C., Kabouridis, P. S., Flores-Borja, F., Mageed, R. A. & Isenberg, D. A. Altered lipid raft-associated signaling and ganglioside expression in T lymphocytes from patients with systemic lupus erythematosus. J. Clin. Invest. 113, 1176-1187 (2004).
    • (2004) J. Clin. Invest. , vol.113 , pp. 1176-1187
    • Jury, E.C.1    Kabouridis, P.S.2    Flores-Borja, F.3    Mageed, R.A.4    Isenberg, D.A.5
  • 126
    • 0035863892 scopus 로고    scopus 로고
    • A deletion in the gene encoding the CD45 antigen in a patient with SCID
    • Tchilian, E. Z. et al. A deletion in the gene encoding the CD45 antigen in a patient with SCID. J. Immunol. 166, 1308-1313 (2001).
    • (2001) J. Immunol. , vol.166 , pp. 1308-1313
    • Tchilian, E.Z.1
  • 127
    • 0033662317 scopus 로고    scopus 로고
    • A point mutation in PTPRC is associated with the development of multiple sclerosis
    • Jacobsen, M. et al. A point mutation in PTPRC is associated with the development of multiple sclerosis. Nature Genet. 26, 495-499 (2000).
    • (2000) Nature Genet. , vol.26 , pp. 495-499
    • Jacobsen, M.1
  • 128
    • 17944365032 scopus 로고    scopus 로고
    • PTPRC (CD45) is not associated with the development of multiple sclerosis in U.S. patients
    • Barcellos, L. F. et al. PTPRC (CD45) is not associated with the development of multiple sclerosis in U.S. patients. Nature Genet. 29, 23-24 (2001).
    • (2001) Nature Genet. , vol.29 , pp. 23-24
    • Barcellos, L.F.1
  • 129
    • 0345039852 scopus 로고    scopus 로고
    • Does 77C→G in PTPRC modify autoimmune disorders linked to the major histocompatibility locus?
    • Vorechovsky, I. et al. Does 77C→G in PTPRC modify autoimmune disorders linked to the major histocompatibility locus? Nature Genet. 29, 22-23 (2001).
    • (2001) Nature Genet. , vol.29 , pp. 22-23
    • Vorechovsky, I.1
  • 130
    • 0036367267 scopus 로고    scopus 로고
    • Low-molecular-weight protein tyrosine phosphatase and human disease: In search of biochemical mechanisms
    • Bottini, N., Bottini, E., Gloria-Bottini, F. & Mustelin, T. Low-molecular-weight protein tyrosine phosphatase and human disease: in search of biochemical mechanisms. Arch. Immunol. Ther. Exp. (Warsz.) 50, 95-104 (2002).
    • (2002) Arch. Immunol. Ther. Exp. (Warsz.) , vol.50 , pp. 95-104
    • Bottini, N.1    Bottini, E.2    Gloria-Bottini, F.3    Mustelin, T.4
  • 131
    • 0043133655 scopus 로고    scopus 로고
    • Genetic control of serum IgE levels: A study of low molecular weight protein tyrosine phosphatase
    • Bottini, N. et al. Genetic control of serum IgE levels: a study of low molecular weight protein tyrosine phosphatase. Clin. Genet. 63, 228-231 (2003).
    • (2003) Clin. Genet. , vol.63 , pp. 228-231
    • Bottini, N.1
  • 132
    • 0031026828 scopus 로고    scopus 로고
    • The Yersinia Yop virulon: A bacterial system for subverting eukaryotic cells
    • Cornelis, G. R. & Wolf-Watz, H. The Yersinia Yop virulon: a bacterial system for subverting eukaryotic cells. Mol. Microbiol. 23, 861-867 (1997).
    • (1997) Mol. Microbiol. , vol.23 , pp. 861-867
    • Cornelis, G.R.1    Wolf-Watz, H.2
  • 133
    • 0029948607 scopus 로고    scopus 로고
    • YopH of Yersinia pseudotuberculosis interrupts early phosphotyrosine signalling associated with phagocytosis
    • Andersson, K. et al. YopH of Yersinia pseudotuberculosis interrupts early phosphotyrosine signalling associated with phagocytosis. Mol. Microbiol. 20, 1057-1069 (1996).
    • (1996) Mol. Microbiol. , vol.20 , pp. 1057-1069
    • Andersson, K.1
  • 134
    • 0344562930 scopus 로고    scopus 로고
    • Suppression of T and B lymphocyte activation by a Yersinia pseudotuberculosis virulence factor, YopH
    • Yao, T., Mecsas, J., Healy, J. I., Falkow, S. & Chien, Y. Suppression of T and B lymphocyte activation by a Yersinia pseudotuberculosis virulence factor, YopH. J. Exp. Med. 190, 1343-1350 (1999).
    • (1999) J. Exp. Med. , vol.190 , pp. 1343-1350
    • Yao, T.1    Mecsas, J.2    Healy, J.I.3    Falkow, S.4    Chien, Y.5
  • 135
    • 1042266623 scopus 로고    scopus 로고
    • Lck dephosphorylation at Y394 and inhibition of T cell antigen receptor signaling by Yersinia phosphatase YopH
    • Alonso, A. et al. Lck dephosphorylation at Y394 and inhibition of T cell antigen receptor signaling by Yersinia phosphatase YopH. J. Biol. Chem. 279, 4922-4928 (2004). References 134 and 135 show that the phosphatase YopH from Yersinia spp. is a potent inhibitor of T-cell activation. Reference 135 shows that the molecular mechanism of inhibition involves the dephosphorylation of Y394 of LCK, resulting in complete abrogation of signalling through the TCR.
    • (2004) J. Biol. Chem. , vol.279 , pp. 4922-4928
    • Alonso, A.1
  • 136
    • 0035214193 scopus 로고    scopus 로고
    • Role of tyrosine kinases and the tyrosine phosphatase SptP in the interaction of Salmonella with host cells
    • Murli, S., Watson, R. O. & Galan, J. E. Role of tyrosine kinases and the tyrosine phosphatase SptP in the interaction of Salmonella with host cells. Cell. Microbiol. 3, 795-810 (2001).
    • (2001) Cell. Microbiol. , vol.3 , pp. 795-810
    • Murli, S.1    Watson, R.O.2    Galan, J.E.3
  • 137
    • 10744227858 scopus 로고    scopus 로고
    • Disruption of MptpB impairs the ability of Mycobacterium tuberculosis to survive in guinea pigs
    • Singh R. et al. Disruption of MptpB impairs the ability of Mycobacterium tuberculosis to survive in guinea pigs. Mol. Microbiol. 50, 751-762 (2003).
    • (2003) Mol. Microbiol. , vol.50 , pp. 751-762
    • Singh, R.1
  • 138
    • 0038499543 scopus 로고    scopus 로고
    • Small molecule regulation of phosphatase-dependent cell signaling pathways
    • Lazo, J. S. & Wipf, P. Small molecule regulation of phosphatase-dependent cell signaling pathways. Oncol. Res. 13, 347-352 (2003).
    • (2003) Oncol. Res. , vol.13 , pp. 347-352
    • Lazo, J.S.1    Wipf, P.2
  • 139
    • 0142180154 scopus 로고    scopus 로고
    • Aurintricarboxylic acid blocks in vitro and in vivo activity of YopH, an essential virulent factor of Yersinia pestis, the agent of the plague
    • Liang, F. et al. Aurintricarboxylic acid blocks in vitro and in vivo activity of YopH, an essential virulent factor of Yersinia pestis, the agent of the plague. J. Biol. Chem. 278, 41734-41741 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 41734-41741
    • Liang, F.1


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