메뉴 건너뛰기




Volumn 162, Issue 5, 1999, Pages 2717-2724

Expression of dominant-negative Src-homology domain 2-containing protein tyrosine phosphatase-1 results in increased Syk tyrosine kinase activity and B cell activation

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN TYROSINE KINASE; PROTEIN TYROSINE PHOSPHATASE;

EID: 0033105369     PISSN: 00221767     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (93)

References (47)
  • 1
    • 0028060150 scopus 로고
    • Temporal differences in the activation of three classes of non-transmembrane protein tyrosine kinases following B-cell antigen receptor surface engagement
    • Saouaf, S. J., S. Mahajan, R. B. Rowley, S. A. Kut, J. Fargnoli, A. L. Burkhardt, S. Tsukada, O. N. Witte, and J. B. Bolen. 1994 Temporal differences in the activation of three classes of non-transmembrane protein tyrosine kinases following B-cell antigen receptor surface engagement. Proc. Natl. Acad. Sci. USA 91:9524.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 9524
    • Saouaf, S.J.1    Mahajan, S.2    Rowley, R.B.3    Kut, S.A.4    Fargnoli, J.5    Burkhardt, A.L.6    Tsukada, S.7    Witte, O.N.8    Bolen, J.B.9
  • 2
    • 0028346563 scopus 로고
    • Signal transduction by the B cell antigen receptor and its coreceptors
    • Cambier, J. C., C. M. Pleiman, and M. R. Clark. 1994. Signal transduction by the B cell antigen receptor and its coreceptors. Annu. Rev. Immunol. 12:457.
    • (1994) Annu. Rev. Immunol. , vol.12 , pp. 457
    • Cambier, J.C.1    Pleiman, C.M.2    Clark, M.R.3
  • 3
    • 0029892116 scopus 로고    scopus 로고
    • Genetic analysis of tyrosine kinase function in B cell development
    • Satterthwaite, A., and O. Witte. 1996. Genetic analysis of tyrosine kinase function in B cell development. Annu. Rev. Immunol. 14:131.
    • (1996) Annu. Rev. Immunol. , vol.14 , pp. 131
    • Satterthwaite, A.1    Witte, O.2
  • 4
    • 0029076731 scopus 로고
    • Reconstitution of syk function by the ZAP-70 protein tyrosine kinase
    • Kong, G.-H., J.-Y. Bu, T. Kurosaki, A. S. Shaw, and A. C. Chan. 1995. Reconstitution of syk function by the ZAP-70 protein tyrosine kinase. Immunity 2:485.
    • (1995) Immunity , vol.2 , pp. 485
    • Kong, G.-H.1    Bu, J.-Y.2    Kurosaki, T.3    Shaw, A.S.4    Chan, A.C.5
  • 5
    • 0029068171 scopus 로고
    • Syk protein-tyrosine kinase is regulated by tyrosine-phosphorylated Igα/ Igβ immunoreceptor tyrosine activation motif binding and autophosphorylation
    • Rowley, R. B., A. L. Burkhardt, H-G. Chao, G. R. Matsueda, and J. B. Bolen. 1995. Syk protein-tyrosine kinase is regulated by tyrosine-phosphorylated Igα/ Igβ immunoreceptor tyrosine activation motif binding and autophosphorylation. J. Biol. Chem. 270:11590.
    • (1995) J. Biol. Chem. , vol.270 , pp. 11590
    • Rowley, R.B.1    Burkhardt, A.L.2    Chao, H.-G.3    Matsueda, G.R.4    Bolen, J.B.5
  • 6
    • 0029348011 scopus 로고
    • Positive and negative regulation of leukocyte activation by protein tyrosine phosphatases
    • Thomas, M. L. 1995. Positive and negative regulation of leukocyte activation by protein tyrosine phosphatases. Semin. Immunol. 7:279.
    • (1995) Semin. Immunol. , vol.7 , pp. 279
    • Thomas, M.L.1
  • 7
    • 0028961264 scopus 로고
    • Protein tyrosine phosphatase 1C negatively regulates antigen receptor signaling in B lymphocytes and determines thresholds for negative selection
    • Cyster, J. G., and C. C. Goodnow. 1995. Protein tyrosine phosphatase 1C negatively regulates antigen receptor signaling in B lymphocytes and determines thresholds for negative selection. Immunity 2:13.
    • (1995) Immunity , vol.2 , pp. 13
    • Cyster, J.G.1    Goodnow, C.C.2
  • 8
    • 0027710741 scopus 로고
    • The leukocyte common antigen, CD45 and other protein tyrosine phosphatases in hematopoietic cells
    • Woodford-Thomas, T., and M. L. Thomas. 1994. The leukocyte common antigen, CD45 and other protein tyrosine phosphatases in hematopoietic cells. Semin. Cell Biol. 4:409.
    • (1994) Semin. Cell Biol. , vol.4 , pp. 409
    • Woodford-Thomas, T.1    Thomas, M.L.2
  • 9
    • 0016836299 scopus 로고
    • Motheaten, an immunodeficient mutant of the mouse
    • Green, M. C., and L. D. Shultz. 1975. Motheaten, an immunodeficient mutant of the mouse. J. Hered. 66:250.
    • (1975) J. Hered. , vol.66 , pp. 250
    • Green, M.C.1    Shultz, L.D.2
  • 11
    • 0027197067 scopus 로고
    • Mutations at the murine motheaten locus are within the hematopoietic cell protein-tyrosine phosphatase (Hcph) gene
    • Shultz, L. D., P. A. Schweitzer, T. V. Rajan, T. Yi, J. N. Ihle, R. J. Matthews, M. L. Thomas, and D. R. Beier 1993. Mutations at the murine motheaten locus are within the hematopoietic cell protein-tyrosine phosphatase (Hcph) gene. Cell 73:1445.
    • (1993) Cell , vol.73 , pp. 1445
    • Shultz, L.D.1    Schweitzer, P.A.2    Rajan, T.V.3    Yi, T.4    Ihle, J.N.5    Matthews, R.J.6    Thomas, M.L.7    Beier, D.R.8
  • 12
    • 0027359495 scopus 로고
    • Expression and catalytic activity of the tyrosine phosphatase PTP1C is severely impaired in motheaten and viable motheaten mice
    • Kozlowski, M., I. Mlinaric-Rascan, G.-S. Feng, R. Shen, T. Pawson, and K. A. Siminovitch. 1993. Expression and catalytic activity of the tyrosine phosphatase PTP1C is severely impaired in motheaten and viable motheaten mice. J. Exp. Med. 178:2157.
    • (1993) J. Exp. Med. , vol.178 , pp. 2157
    • Kozlowski, M.1    Mlinaric-Rascan, I.2    Feng, G.-S.3    Shen, R.4    Pawson, T.5    Siminovitch, K.A.6
  • 13
    • 0027195626 scopus 로고
    • Motheaten and viable motheaten mice have mutations in the haematopoietic cell phosphatase gene
    • Tsui, H. W., K. A. Siminovitch, L. de Souza, and F. W. L. Tsui. 1993. Motheaten and viable motheaten mice have mutations in the haematopoietic cell phosphatase gene. Nat. Genet. 4:124.
    • (1993) Nat. Genet. , vol.4 , pp. 124
    • Tsui, H.W.1    Siminovitch, K.A.2    De Souza, L.3    Tsui, F.W.L.4
  • 14
    • 0030710537 scopus 로고    scopus 로고
    • Down-regulated expression of SHP-1 in Burkitt lymphomas and germinal center B lymphocytes
    • Delibrias, C. C., J. E. Floettmann, M. Rowe, and D. T. Fearon. 1997. Down-regulated expression of SHP-1 in Burkitt lymphomas and germinal center B lymphocytes. J. Exp. Med. 186:1575.
    • (1997) J. Exp. Med. , vol.186 , pp. 1575
    • Delibrias, C.C.1    Floettmann, J.E.2    Rowe, M.3    Fearon, D.T.4
  • 15
    • 0028989144 scopus 로고
    • Identification of the tyrosine phosphatase PTP1C as a B cell antigen receptor-associated protein involved in the regulation of B cell signalling
    • Pani, G., M. Kozlowski, J. C. Cambier, G. B. Mills, and K. A. Siminovitch. 1995. Identification of the tyrosine phosphatase PTP1C as a B cell antigen receptor-associated protein involved in the regulation of B cell signalling. J. Exp. Med. 181:2077.
    • (1995) J. Exp. Med. , vol.181 , pp. 2077
    • Pani, G.1    Kozlowski, M.2    Cambier, J.C.3    Mills, G.B.4    Siminovitch, K.A.5
  • 16
    • 0029048060 scopus 로고
    • Phosphotyrosine-dependent association between CD22 and protein tyrosine phosphatase IC
    • Campbell, M., and N. Klinman. 1995. Phosphotyrosine-dependent association between CD22 and protein tyrosine phosphatase IC. Eur. J. Immunol. 25:1573.
    • (1995) Eur. J. Immunol. , vol.25 , pp. 1573
    • Campbell, M.1    Klinman, N.2
  • 18
    • 0029103298 scopus 로고
    • Hematopoietic cell phosphatase is recruited to CD22 following B cell antigen receptor ligation
    • Lankester, A. C., G. M. W. van Schijndel, and R. A. W. van Lier. 1995. Hematopoietic cell phosphatase is recruited to CD22 following B cell antigen receptor ligation. J. Biol. Chem. 270:20305.
    • (1995) J. Biol. Chem. , vol.270 , pp. 20305
    • Lankester, A.C.1    Van Schijndel, G.M.W.2    Van Lier, R.A.W.3
  • 20
    • 0030022278 scopus 로고    scopus 로고
    • The tyrosine phosphatase PTP1C associates with Vav, Grb2, and mSos1 in hematopoietic cells
    • Kon-Kozlowski, M., G. Pani, T. Pawson, and K. A. Siminovitch. 1996. The tyrosine phosphatase PTP1C associates with Vav, Grb2, and mSos1 in hematopoietic cells. J. Biol. Chem. 271:3856.
    • (1996) J. Biol. Chem. , vol.271 , pp. 3856
    • Kon-Kozlowski, M.1    Pani, G.2    Pawson, T.3    Siminovitch, K.A.4
  • 21
    • 0029829894 scopus 로고    scopus 로고
    • Hematopoietic cell phosphatase, SHP-1, is constitutively associated with the SH2 domain-containing leukocyte protein, SLP-76, in B cells
    • Mizuno, K., T. Katagiri, K. Hasegawa, M. Ogimoto, and H. Yakura. 1996. Hematopoietic cell phosphatase, SHP-1, is constitutively associated with the SH2 domain-containing leukocyte protein, SLP-76, in B cells. J. Exp. Med. 184:457.
    • (1996) J. Exp. Med. , vol.184 , pp. 457
    • Mizuno, K.1    Katagiri, T.2    Hasegawa, K.3    Ogimoto, M.4    Yakura, H.5
  • 22
    • 0028997875 scopus 로고
    • Of ITAMs and ITIMs: Turning on and off the B cell antigen receptor
    • Thomas, M. L. 1995. Of ITAMs and ITIMs: turning on and off the B cell antigen receptor. J. Exp. Med. 181:1953.
    • (1995) J. Exp. Med. , vol.181 , pp. 1953
    • Thomas, M.L.1
  • 24
    • 0028956353 scopus 로고
    • Specific recruitment of SH-PTP1 to the erythropoietin receptor causes inactivation of JAK2 and termination of proliferative signals
    • Klingmüller, U., U. Lorenz, L. Cantley, B. Neel, and H. Lodish. 1995. Specific recruitment of SH-PTP1 to the erythropoietin receptor causes inactivation of JAK2 and termination of proliferative signals. Cell 80:729.
    • (1995) Cell , vol.80 , pp. 729
    • Klingmüller, U.1    Lorenz, U.2    Cantley, L.3    Neel, B.4    Lodish, H.5
  • 25
    • 0029973560 scopus 로고    scopus 로고
    • Direct association with and dephosphorylation of Jak2 kinase by the SH2-domain-containing protein tyrosine phosphatase SHP-1
    • Jiao, H., K. Berrada, W. Yang, M. Tabrizi, L. C. Platanias, and T. Yi. 1996. Direct association with and dephosphorylation of Jak2 kinase by the SH2-domain-containing protein tyrosine phosphatase SHP-1. Mol. Cell. Biol. 16:6985.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 6985
    • Jiao, H.1    Berrada, K.2    Yang, W.3    Tabrizi, M.4    Platanias, L.C.5    Yi, T.6
  • 26
    • 0028972719 scopus 로고
    • Differential regulation of the α/β interferon-stimulated Jak/Stat pathway by the SH2 domain-containing tyrosine phosphatase SHPTP1
    • David, M., H. E. Chen, S. Goelz, A. C. Larner, and B. G. Neel. 1995. Differential regulation of the α/β interferon-stimulated Jak/Stat pathway by the SH2 domain-containing tyrosine phosphatase SHPTP1. Mol. Cell. Biol. 15:7050.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 7050
    • David, M.1    Chen, H.E.2    Goelz, S.3    Larner, A.C.4    Neel, B.G.5
  • 30
    • 0343307005 scopus 로고    scopus 로고
    • Deletion of SHIP or SHP-1 reveals two distinct pathways for inhibitory signaling
    • Ono, M., H. Okada, S. Bolland, S. Yanagi, T. Kurosaki, and J. V. Ravetch. 1997. Deletion of SHIP or SHP-1 reveals two distinct pathways for inhibitory signaling. Cell 90:293.
    • (1997) Cell , vol.90 , pp. 293
    • Ono, M.1    Okada, H.2    Bolland, S.3    Yanagi, S.4    Kurosaki, T.5    Ravetch, J.V.6
  • 31
    • 0027536588 scopus 로고
    • Differential signaling through the Ig-α and Ig-β components of the B cell antigen receptor
    • Kim, K.-M., G. Alber, P. Weiser, and M. Reth. 1993. Differential signaling through the Ig-α and Ig-β components of the B cell antigen receptor. Eur. J. Immunol. 23:911.
    • (1993) Eur. J. Immunol. , vol.23 , pp. 911
    • Kim, K.-M.1    Alber, G.2    Weiser, P.3    Reth, M.4
  • 32
    • 0026324171 scopus 로고
    • Protein tyrosine phosphatases: A diverse family of intracellular and transmembrane enzymes
    • Fischer, E. H., H. Charbonneau, and N. K. Tonks. 1991. Protein tyrosine phosphatases: a diverse family of intracellular and transmembrane enzymes. Science 253:401.
    • (1991) Science , vol.253 , pp. 401
    • Fischer, E.H.1    Charbonneau, H.2    Tonks, N.K.3
  • 34
    • 0028064781 scopus 로고
    • Temporal regulation of non-transmembrane protein tyrosine kinase enzyme activity following T cell antigen receptor engagement
    • Burkhardt, A. L., B. Stealey, R. B. Rowley, S. Mahajan, M. Prendergast, J. Fargnoli, and J. B. Bolen. 1994. Temporal regulation of non-transmembrane protein tyrosine kinase enzyme activity following T cell antigen receptor engagement. J. Biol. Chem. 269:23642.
    • (1994) J. Biol. Chem. , vol.269 , pp. 23642
    • Burkhardt, A.L.1    Stealey, B.2    Rowley, R.B.3    Mahajan, S.4    Prendergast, M.5    Fargnoli, J.6    Bolen, J.B.7
  • 35
    • 0028090058 scopus 로고
    • Interactions of Lyn with the antigen receptor during B cell activation
    • Burg, D. L., M. T. Furlong, M. L. Harrison, and R. L. Geahlen. 1994. Interactions of Lyn with the antigen receptor during B cell activation. J. Biol. Chem. 269: 28136.
    • (1994) J. Biol. Chem. , vol.269 , pp. 28136
    • Burg, D.L.1    Furlong, M.T.2    Harrison, M.L.3    Geahlen, R.L.4
  • 36
    • 0025292741 scopus 로고
    • Protein tyrosine phosphorylation is induced in murine B lymphocytes in response to stimulation with anti-immunoglobulin
    • Campbell, M.-A., and B. M. Sefton. 1990. Protein tyrosine phosphorylation is induced in murine B lymphocytes in response to stimulation with anti-immunoglobulin. EMBO J. 9:2125.
    • (1990) EMBO J. , vol.9 , pp. 2125
    • Campbell, M.-A.1    Sefton, B.M.2
  • 37
    • 0030834178 scopus 로고    scopus 로고
    • Counterregulation by the coreceptors CD19 and CD22 of MAP kinase activation by membrane immunoglobulin
    • Tooze, R. M., G. M. Doody, and D. T. Fearon. 1997. Counterregulation by the coreceptors CD19 and CD22 of MAP kinase activation by membrane immunoglobulin. Immunity 7:59.
    • (1997) Immunity , vol.7 , pp. 59
    • Tooze, R.M.1    Doody, G.M.2    Fearon, D.T.3
  • 38
    • 0030740148 scopus 로고    scopus 로고
    • Characterization of the B lymphocyte populations in Lyn-deficient mice and the role of Lyn in signal initiation and down-regulation
    • Chan, V. W. F., F. Meng, P. Soriano, A. L. DeFranco, and C. A. Lowell. 1997. Characterization of the B lymphocyte populations in Lyn-deficient mice and the role of Lyn in signal initiation and down-regulation. Immunity 7:69.
    • (1997) Immunity , vol.7 , pp. 69
    • Chan, V.W.F.1    Meng, F.2    Soriano, P.3    DeFranco, A.L.4    Lowell, C.A.5
  • 39
    • 0029071585 scopus 로고
    • Activation of ZAP-70 kinase activity by phosphorylation of tyrosine 493 is required for lymphocyte antigen receptor function
    • Chan, A., M. Dalton, R. Johnson, G.-h. Kong, T. Wang, R. Thoma, and T. Kurosaki. 1995. Activation of ZAP-70 kinase activity by phosphorylation of tyrosine 493 is required for lymphocyte antigen receptor function. EMBO J. 14:2499.
    • (1995) EMBO J. , vol.14 , pp. 2499
    • Chan, A.1    Dalton, M.2    Johnson, R.3    Kong, G.-H.4    Wang, T.5    Thoma, R.6    Kurosaki, T.7
  • 40
    • 0028905060 scopus 로고
    • Syk is activated by phosphotyrosine-containing peptides representing the tyrosine-based activation motifs of the high affinity receptor for IgE
    • Shiue, L., M. J. Zoller, and J. S. Brugge 1995. Syk is activated by phosphotyrosine-containing peptides representing the tyrosine-based activation motifs of the high affinity receptor for IgE. J. Biol. Chem. 270:10498.
    • (1995) J. Biol. Chem. , vol.270 , pp. 10498
    • Shiue, L.1    Zoller, M.J.2    Brugge, J.S.3
  • 41
    • 0028693794 scopus 로고    scopus 로고
    • Intracellular ionized calcium
    • Z. Darzynkiewicz, J. P. Robinson and H. A. Crissman, eds. Academic Press, San Diego, CA
    • June, C. H., and P. S. Rabinovitch. 1998. Intracellular ionized calcium. In Methods in Cell Biology. Vol. 41. Z. Darzynkiewicz, J. P. Robinson and H. A. Crissman, eds. Academic Press, San Diego, CA, p. 149.
    • (1998) Methods in Cell Biology , vol.41 , pp. 149
    • June, C.H.1    Rabinovitch, P.S.2
  • 42
    • 0030047811 scopus 로고    scopus 로고
    • CD22 associates with protein tyrosine phosphatase 1C, Syk, and phospholipase Cγ1 upon B cell activation
    • Law, C.-L., S. P. Sidorenko, K. A. Chandran, Z. Zhao, S. H. Shen, E. H. Fischer, and E. A. Clark. 1996. CD22 associates with protein tyrosine phosphatase 1C, Syk, and phospholipase Cγ1 upon B cell activation. J. Exp. Med. 183:547.
    • (1996) J. Exp. Med. , vol.183 , pp. 547
    • Law, C.-L.1    Sidorenko, S.P.2    Chandran, K.A.3    Zhao, Z.4    Shen, S.H.5    Fischer, E.H.6    Clark, E.A.7
  • 43
    • 0027936858 scopus 로고
    • Induction of tyrosine phosphorylation during ICAM-3 and LFA-1-mediated intercellular adhesion, and its regulation by the CD45 phosphatase
    • Arroyo, A., M. Campanero, P. Sanchez-Mateos, J. Zapata, M. Ursa, M. Angel del Pozo, and F. Sanchez-Madrid. 1994. Induction of tyrosine phosphorylation during ICAM-3 and LFA-1-mediated intercellular adhesion, and its regulation by the CD45 phosphatase. J. Cell Biol. 126:1277.
    • (1994) J. Cell Biol. , vol.126 , pp. 1277
    • Arroyo, A.1    Campanero, M.2    Sanchez-Mateos, P.3    Zapata, J.4    Ursa, M.5    Angel Del Pozo, M.6    Sanchez-Madrid, F.7
  • 44
    • 0029118777 scopus 로고
    • B-cell homotypic adhesion through exon-A restricted epitopes of CD45 involves LFA-1/ICAM-1, ICAM-3 interactions, and induces coclustering of CD45 and LFA-1
    • Zapata, J. M., M. R. Campanero, M. Marazuela, F. Sanchez-Madrid, and M. O. De Landazuri. 1995. B-cell homotypic adhesion through exon-A restricted epitopes of CD45 involves LFA-1/ICAM-1, ICAM-3 interactions, and induces coclustering of CD45 and LFA-1. Blood 86:1861.
    • (1995) Blood , vol.86 , pp. 1861
    • Zapata, J.M.1    Campanero, M.R.2    Marazuela, M.3    Sanchez-Madrid, F.4    De Landazuri, M.O.5
  • 46
    • 0026043267 scopus 로고
    • Identification of novel protein tyrosine phosphatases of hematopoietic cells by polymerase chain reaction amplification
    • Yi, T., J. L. Cleveland, and J. N. Ihle. 1991. Identification of novel protein tyrosine phosphatases of hematopoietic cells by polymerase chain reaction amplification. Blood 78:2222.
    • (1991) Blood , vol.78 , pp. 2222
    • Yi, T.1    Cleveland, J.L.2    Ihle, J.N.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.