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Volumn 91, Issue 3, 1999, Pages 243-253

Bruton's tyrosine kinase controls a sustained calcium signal essential for B lineage development and function

Author keywords

B cell antigen receptor (BCR); IP3; PLC ; XID; XLA

Indexed keywords

LYMPHOCYTE ANTIGEN RECEPTOR; PROTEIN TYROSINE KINASE;

EID: 0033013019     PISSN: 15216616     EISSN: None     Source Type: Journal    
DOI: 10.1006/clim.1999.4732     Document Type: Review
Times cited : (89)

References (116)
  • 1
    • 0000419304 scopus 로고
    • Agammaglobulinemia
    • Bruton O. C. Agammaglobulinemia. Pediatrics. 9:1952;722-727.
    • (1952) Pediatrics , vol.9 , pp. 722-727
    • Bruton, O.C.1
  • 4
    • 0025027433 scopus 로고
    • Phenotypic features and proliferative activity of B cell progenitors in X-linked agammaglobulinemia
    • Campana D., Farrant J., Inamdar N., Webster A. D. B., Janossy G. Phenotypic features and proliferative activity of B cell progenitors in X-linked agammaglobulinemia. J. Immunol. 145:1990;1675-1680.
    • (1990) J. Immunol. , vol.145 , pp. 1675-1680
    • Campana, D.1    Farrant, J.2    Inamdar, N.3    Webster, A.D.B.4    Janossy, G.5
  • 5
    • 0018102013 scopus 로고
    • B lymphocyte precursors in human bone marrow: An analysis of normal individuals and patients with antibody-deficiency states
    • Pearl E. R., Vogler L. B., Okos A. J., Crist W. M., Lawton A. R. III, Cooper M. D. B lymphocyte precursors in human bone marrow: An analysis of normal individuals and patients with antibody-deficiency states. Immunol. 120:1978;1169-1175.
    • (1978) Immunol. , vol.120 , pp. 1169-1175
    • Pearl, E.R.1    Vogler, L.B.2    Okos, A.J.3    Crist, W.M.4    Lawton A.R. III5    Cooper, M.D.6
  • 6
  • 7
    • 0027329865 scopus 로고
    • IL-5 receptor positive B cells, but not eosinophils, are functionally and numerically influenced in mice carrying the X-linked immune defect
    • Hitoshi Y., Sonoda E., Kikuchi Y., Yonehara S., Nakauchi H., Takatsu K. IL-5 receptor positive B cells, but not eosinophils, are functionally and numerically influenced in mice carrying the X-linked immune defect. Int. Immunol. 5:1993;1183-1190.
    • (1993) Int. Immunol. , vol.5 , pp. 1183-1190
    • Hitoshi, Y.1    Sonoda, E.2    Kikuchi, Y.3    Yonehara, S.4    Nakauchi, H.5    Takatsu, K.6
  • 8
    • 0025673971 scopus 로고
    • Interleukin 10, a novel B cell stimulatory factor: Unresponsiveness of X chromosome-linked immunodeficiency B cells
    • Go N. F., Castle B. E., Barret R., Kastelein R., Dang W., Mosmann T. R., Moore K. W., Howard M. Interleukin 10, a novel B cell stimulatory factor: Unresponsiveness of X chromosome-linked immunodeficiency B cells. J. Exp. Med. 172:1990;1625-1631.
    • (1990) J. Exp. Med. , vol.172 , pp. 1625-1631
    • Go, N.F.1    Castle, B.E.2    Barret, R.3    Kastelein, R.4    Dang, W.5    Mosmann, T.R.6    Moore, K.W.7    Howard, M.8
  • 10
    • 0028071612 scopus 로고
    • Murine B cell proliferation and protection from apoptosis with an antibody against a 105-kD molecule: Unresponsiveness of X-linked immunodeficient B cells
    • Miyake K., Yamashita Y., Hitoshi Y., Takatsu K., Kimoto M. Murine B cell proliferation and protection from apoptosis with an antibody against a 105-kD molecule: Unresponsiveness of X-linked immunodeficient B cells. J. Exp. Med. 180:1994;1217-1224.
    • (1994) J. Exp. Med. , vol.180 , pp. 1217-1224
    • Miyake, K.1    Yamashita, Y.2    Hitoshi, Y.3    Takatsu, K.4    Kimoto, M.5
  • 11
    • 0028158091 scopus 로고
    • B cells from CBA/N mice do not proliferate following ligation of CD40
    • Hasbold J., Klaus G. G. B cells from CBA/N mice do not proliferate following ligation of CD40. Eur. J. Immunol. 24:1994;152-157.
    • (1994) Eur. J. Immunol. , vol.24 , pp. 152-157
    • Hasbold, J.1    Klaus, G.G.2
  • 12
    • 0029348814 scopus 로고
    • The Btk subfamily of cytoplasmic tyrosine kinases: Structure, regulation, and function
    • Rawlings D. J., Witte O. N. The Btk subfamily of cytoplasmic tyrosine kinases: Structure, regulation, and function. Semin. Immunol. 7:1995;237-246.
    • (1995) Semin. Immunol. , vol.7 , pp. 237-246
    • Rawlings, D.J.1    Witte, O.N.2
  • 16
    • 0027261447 scopus 로고
    • Colocalization of X-linked agammaglobulinemia and X-linked immunodeficiency genes
    • Thomas J. D., Sideras P., Smith C. I., Vorechovsky I., Chapman V., Paul W. E. Colocalization of X-linked agammaglobulinemia and X-linked immunodeficiency genes. Science. 261:1993;355-358.
    • (1993) Science , vol.261 , pp. 355-358
    • Thomas, J.D.1    Sideras, P.2    Smith, C.I.3    Vorechovsky, I.4    Chapman, V.5    Paul, W.E.6
  • 18
    • 0029146219 scopus 로고
    • Molecular and Cellular Aspects of X-linked agammaglobulinemia
    • Sideras P., Smith C. I. E. Molecular and Cellular Aspects of X-linked agammaglobulinemia. Adv. Immunol. 59:1995;135-223.
    • (1995) Adv. Immunol. , vol.59 , pp. 135-223
    • Sideras, P.1    Smith, C.I.E.2
  • 19
    • 0032146708 scopus 로고    scopus 로고
    • Genetic basis of abnormal B cell development
    • Conley M. E., Cooper M. D. Genetic basis of abnormal B cell development. Curr. Opin. Immunol. 10:1998;399-406.
    • (1998) Curr. Opin. Immunol. , vol.10 , pp. 399-406
    • Conley, M.E.1    Cooper, M.D.2
  • 21
    • 0032511228 scopus 로고    scopus 로고
    • Drosophila ring canal growth requires Src and Tec kinases
    • Cooley L. Drosophila ring canal growth requires Src and Tec kinases. Cell. 93:1998;913-915.
    • (1998) Cell , vol.93 , pp. 913-915
    • Cooley, L.1
  • 22
    • 0027358430 scopus 로고
    • The Bruton's tyrosine kinase gene is expressed throughout B cell differentiation, from early precursor B cell stages preceding immunoglobulin gene rearrangement up to mature B cell stages
    • de Weers M., Verschuren M. C. M., Kraakman M. E. M., Mensink R. G. J., Schuurman R. K. B., van Dongen J. J. M., Hendriks R. W. The Bruton's tyrosine kinase gene is expressed throughout B cell differentiation, from early precursor B cell stages preceding immunoglobulin gene rearrangement up to mature B cell stages. Eur. J. Immunol. 23:1993;3109-3114.
    • (1993) Eur. J. Immunol. , vol.23 , pp. 3109-3114
    • De Weers, M.1    Verschuren, M.C.M.2    Kraakman, M.E.M.3    Mensink, R.G.J.4    Schuurman, R.K.B.5    Van Dongen, J.J.M.6    Hendriks, R.W.7
  • 24
    • 0027267532 scopus 로고
    • Nonreceptor tyrosine protein kinases
    • Bolen J. B. Nonreceptor tyrosine protein kinases. Oncogene. 8:1993;2025-2031.
    • (1993) Oncogene , vol.8 , pp. 2025-2031
    • Bolen, J.B.1
  • 25
    • 0028859279 scopus 로고
    • Protein modules and signalling networks
    • Pawson T. Protein modules and signalling networks. Nature. 373:1995;573-580.
    • (1995) Nature , vol.373 , pp. 573-580
    • Pawson, T.1
  • 26
    • 0030983422 scopus 로고    scopus 로고
    • The SH3 domain of Bruton's tyrosine kinase interacts with Vav, Sam68 and EWS
    • Guinamard R., Fougereau M., Seckinger P. The SH3 domain of Bruton's tyrosine kinase interacts with Vav, Sam68 and EWS. Scand. J. Immunol. 45:1997;587-595.
    • (1997) Scand. J. Immunol. , vol.45 , pp. 587-595
    • Guinamard, R.1    Fougereau, M.2    Seckinger, P.3
  • 29
    • 0028173679 scopus 로고
    • Myristylation and palmitylation of Src family members: The fats of the matter
    • Resh M. D. Myristylation and palmitylation of Src family members: The fats of the matter. Cell. 76:1994;411-413.
    • (1994) Cell , vol.76 , pp. 411-413
    • Resh, M.D.1
  • 30
    • 0027300619 scopus 로고
    • The when and how of src regulation
    • Cooper J. A., Howell B. The when and how of src regulation. Cell. 63:1993;1051-1054.
    • (1993) Cell , vol.63 , pp. 1051-1054
    • Cooper, J.A.1    Howell, B.2
  • 31
    • 0027941128 scopus 로고
    • Tec homology (TH) adjacent to the PH domain
    • Vihinen M., Nilsson L., Smith C. I. E. Tec homology (TH) adjacent to the PH domain. FEBS Lett. 350:1994;263-265.
    • (1994) FEBS Lett. , vol.350 , pp. 263-265
    • Vihinen, M.1    Nilsson, L.2    Smith, C.I.E.3
  • 33
    • 0029939448 scopus 로고    scopus 로고
    • PH domains: Diverse sequences with a common fold recruit signaling molecules to the cell surface
    • Lemmon M. A., Ferguson K. M., Schlessinger J. PH domains: Diverse sequences with a common fold recruit signaling molecules to the cell surface. Cell. 85:1996;621-624.
    • (1996) Cell , vol.85 , pp. 621-624
    • Lemmon, M.A.1    Ferguson, K.M.2    Schlessinger, J.3
  • 34
    • 0039710379 scopus 로고    scopus 로고
    • Structure of the PH domain and Btk motif from Bruton's tyrosine kinase: Molecular explanations for X-linked agammaglobulinaemia
    • Hyvönen M., Saraste M. Structure of the PH domain and Btk motif from Bruton's tyrosine kinase: Molecular explanations for X-linked agammaglobulinaemia. EMBO J. 16:1997;3396-3404.
    • (1997) EMBO J. , vol.16 , pp. 3396-3404
    • Hyvönen, M.1    Saraste, M.2
  • 35
    • 0028173394 scopus 로고
    • Binding of the βγ subunits of heterotrimeric G-proteins to the PH domain of Bruton's tyrosine kinase
    • Tsukada S., Simon M., Witte O., Katz A. Binding of the βγ subunits of heterotrimeric G-proteins to the PH domain of Bruton's tyrosine kinase. Proc. Natl. Acad. Sci. USA. 91:1994;11256-11260.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 11256-11260
    • Tsukada, S.1    Simon, M.2    Witte, O.3    Katz, A.4
  • 36
    • 0031038046 scopus 로고    scopus 로고
    • BAP-135, a target for Bruton's tyrosine kinase in response to B cell receptor engagement
    • Yang W., Desiderio S. BAP-135, a target for Bruton's tyrosine kinase in response to B cell receptor engagement. Proc. Natl. Acad. Sci. USA. 94:1997;604-609.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 604-609
    • Yang, W.1    Desiderio, S.2
  • 37
    • 0032509536 scopus 로고    scopus 로고
    • Regulation of TFII-I activity by phosphorylation
    • Novina C. D., Cheriyath V., Roy A. L. Regulation of TFII-I activity by phosphorylation. J. Biol. Chem. 273:1998;33443-33448.
    • (1998) J. Biol. Chem. , vol.273 , pp. 33443-33448
    • Novina, C.D.1    Cheriyath, V.2    Roy, A.L.3
  • 38
    • 0032558834 scopus 로고    scopus 로고
    • The G protein G alpha12 stimulates Bruton's tyrosine kinase and a rasGAP through a conserved PH/BM domain
    • Jiang Y., Ma W., Wan Y., Kozasa T., Hattori S., Huang X. Y. The G protein G alpha12 stimulates Bruton's tyrosine kinase and a rasGAP through a conserved PH/BM domain. Nature. 395:1998;808-813.
    • (1998) Nature , vol.395 , pp. 808-813
    • Jiang, Y.1    Ma, W.2    Wan, Y.3    Kozasa, T.4    Hattori, S.5    Huang, X.Y.6
  • 39
    • 0027980301 scopus 로고
    • Binding of Bruton's tyrosine kinase to Fyn, Lyn, or Hck through a Src homology 3 domain-mediated interaction
    • Cheng G., Ye Z.-S., Baltimore D. Binding of Bruton's tyrosine kinase to Fyn, Lyn, or Hck through a Src homology 3 domain-mediated interaction. Proc. Natl. Acad. Sci. USA. 91:1994;8152-8155.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 8152-8155
    • Cheng, G.1    Ye, Z.-S.2    Baltimore, D.3
  • 40
    • 0031029781 scopus 로고    scopus 로고
    • Regulatory intramolecular association in a tyrosine kinase of the Tec family
    • Andreotti A. H., Bunnell S. C., Feng S., Berg L. J., Schreiber S. L. Regulatory intramolecular association in a tyrosine kinase of the Tec family. Nature. 385:1997;93-97.
    • (1997) Nature , vol.385 , pp. 93-97
    • Andreotti, A.H.1    Bunnell, S.C.2    Feng, S.3    Berg, L.J.4    Schreiber, S.L.5
  • 46
    • 0029824848 scopus 로고    scopus 로고
    • Mutation of the pleckstrin homology domain of Bruton's tyrosine kinase in immunodeficiency impaired inositol 1,3,4,5-tetrakisphosphate binding capacity
    • Fukuda M., Kojima T., Kabayama H., Mikoshiba K. Mutation of the pleckstrin homology domain of Bruton's tyrosine kinase in immunodeficiency impaired inositol 1,3,4,5-tetrakisphosphate binding capacity. J. Biol. Chem. 271:1996;30303-30306.
    • (1996) J. Biol. Chem. , vol.271 , pp. 30303-30306
    • Fukuda, M.1    Kojima, T.2    Kabayama, H.3    Mikoshiba, K.4
  • 47
    • 0020036442 scopus 로고
    • Lack of mature B cells in nude mice with X-linked immune deficiency
    • Wortis H. H., Burkly L., Hughes D., Roschelle S., Waneck G. Lack of mature B cells in nude mice with X-linked immune deficiency. J. Exp. Med. 155:1982;903-913.
    • (1982) J. Exp. Med. , vol.155 , pp. 903-913
    • Wortis, H.H.1    Burkly, L.2    Hughes, D.3    Roschelle, S.4    Waneck, G.5
  • 48
    • 0026446910 scopus 로고
    • B cell deficiency progresses with lineage maturation in nude X-linked immunodeficient mice
    • Chung H. Y., Dong Z., Wortis H. H. B cell deficiency progresses with lineage maturation in nude X-linked immunodeficient mice. J. Immunol. 149:1992;3456-3462.
    • (1992) J. Immunol. , vol.149 , pp. 3456-3462
    • Chung, H.Y.1    Dong, Z.2    Wortis, H.H.3
  • 49
    • 0028033527 scopus 로고
    • B-cell antigen receptor stimulation activates the human Bruton's tyrosine kinase, which is deficient in X-linked agammaglobulinemia
    • de Weers M., Brouns G. S., Hinshelwood S., Kinnon C., Schuurman R. K. B., Hendriks R. W., Borst J. B-cell antigen receptor stimulation activates the human Bruton's tyrosine kinase, which is deficient in X-linked agammaglobulinemia. J. Biol. Chem. 269:1994;23857-23860.
    • (1994) J. Biol. Chem. , vol.269 , pp. 23857-23860
    • De Weers, M.1    Brouns, G.S.2    Hinshelwood, S.3    Kinnon, C.4    Schuurman, R.K.B.5    Hendriks, R.W.6    Borst, J.7
  • 52
    • 0029792213 scopus 로고    scopus 로고
    • Inactivation of Btk by insertion of lacZ reveals defects in B cell development only past the pre-B cell stage
    • Hendriks R. W., de Bruijn M. F. T. R., Maas A., Dingjan G. M., Karis A., Grosveld F. Inactivation of Btk by insertion of lacZ reveals defects in B cell development only past the pre-B cell stage. EMBO J. 15:1996;4862-4872.
    • (1996) EMBO J. , vol.15 , pp. 4862-4872
    • Hendriks, R.W.1    De Bruijn, M.F.T.R.2    Maas, A.3    Dingjan, G.M.4    Karis, A.5    Grosveld, F.6
  • 54
    • 0028915948 scopus 로고
    • Defective signalling through the T- And B-cell antigen receptors in lymphoid cells lacking the vav proto-oncogene
    • Zhang R., Alt F. W., Davidson L., Orkin S. H., Swat W. Defective signalling through the T- and B-cell antigen receptors in lymphoid cells lacking the vav proto-oncogene. Nature. 374:1995;470-473.
    • (1995) Nature , vol.374 , pp. 470-473
    • Zhang, R.1    Alt, F.W.2    Davidson, L.3    Orkin, S.H.4    Swat, W.5
  • 55
    • 0033556333 scopus 로고    scopus 로고
    • Impaired B cell development and proliferation in absence of phosphoinositide 3-kinase p85alpha
    • Fruman D. A., Snapper S. B., Yballe C. M., Davidson L., Yu J. Y., Alt F. W., Cantley L. C. Impaired B cell development and proliferation in absence of phosphoinositide 3-kinase p85alpha. Science. 283:1999;393-397.
    • (1999) Science , vol.283 , pp. 393-397
    • Fruman, D.A.1    Snapper, S.B.2    Yballe, C.M.3    Davidson, L.4    Yu, J.Y.5    Alt, F.W.6    Cantley, L.C.7
  • 56
    • 0033555829 scopus 로고    scopus 로고
    • Xid-like immunodeficiency in mice with disruption of the p85alpha subunit of phosphoinositide 3-kinase
    • Suzuki H., Terauchi Y., Fujiwara M., Aizawa S., Yazaki Y., Kadowaki T., Koyasu S. Xid-like immunodeficiency in mice with disruption of the p85alpha subunit of phosphoinositide 3-kinase. Science. 283:1999;390-392.
    • (1999) Science , vol.283 , pp. 390-392
    • Suzuki, H.1    Terauchi, Y.2    Fujiwara, M.3    Aizawa, S.4    Yazaki, Y.5    Kadowaki, T.6    Koyasu, S.7
  • 58
    • 0029588608 scopus 로고
    • CD38 ligation induces tyrosine phosphorylation of Bruton tyrosine kinase and enhanced expression of interleukin 5-receptor α chain: Synergistic effects with interleukin 5
    • Kikuchi Y., Yasue T., Miyake K., Kimoto M., Takatsu K. CD38 ligation induces tyrosine phosphorylation of Bruton tyrosine kinase and enhanced expression of interleukin 5-receptor α chain: Synergistic effects with interleukin 5. Proc. Natl. Acad. Sci. USA. 92:1995;11814-11818.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 11814-11818
    • Kikuchi, Y.1    Yasue, T.2    Miyake, K.3    Kimoto, M.4    Takatsu, K.5
  • 60
    • 0028049537 scopus 로고
    • Tyrosine phosphorylation and activation of Bruton tyrosine kinase upon Fc epsilon RI cross-linking
    • Kawakami Y., Yao L., Miura T., Tsukada S., Witte O. N., Kawakami T. Tyrosine phosphorylation and activation of Bruton tyrosine kinase upon Fc epsilon RI cross-linking. Mol. Cell. Biol. 14:1994;5108-5113.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 5108-5113
    • Kawakami, Y.1    Yao, L.2    Miura, T.3    Tsukada, S.4    Witte, O.N.5    Kawakami, T.6
  • 61
    • 0032514660 scopus 로고    scopus 로고
    • Identification of the binding site for Gqalpha on its effector Bruton's tyrosine kinase
    • Ma Y. C., Huang X. Y. Identification of the binding site for Gqalpha on its effector Bruton's tyrosine kinase. Proc. Natl. Acad. Sci. USA. 95:1998;12197-12201.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 12197-12201
    • Ma, Y.C.1    Huang, X.Y.2
  • 62
    • 0032497629 scopus 로고    scopus 로고
    • A role for Bruton's tyrosine kinase (Btk) in platelet activation by collagen
    • Quek L. S., Bolen J., Watson S. P. A role for Bruton's tyrosine kinase (Btk) in platelet activation by collagen. Curr. Biol. 8:1998;1137-1140.
    • (1998) Curr. Biol. , vol.8 , pp. 1137-1140
    • Quek, L.S.1    Bolen, J.2    Watson, S.P.3
  • 64
    • 0025766890 scopus 로고
    • Molecular and cellular origins of B lymphocyte diversity
    • Rolink A., Melchers F. Molecular and cellular origins of B lymphocyte diversity. Cell. 66:1991;1081-1094.
    • (1991) Cell , vol.66 , pp. 1081-1094
    • Rolink, A.1    Melchers, F.2
  • 66
    • 0028060150 scopus 로고
    • Temporal differences in the activation of three classes of non-transmembrane protein tyrosine kinase following B cell antigen receptor surface engagement
    • Saouaf S. J., Mahajan S., Rowley R. B., Kut S., Fargnoli J., Burkhardt A. L., Tsukada S., Witte O. N., Bolen J. B. Temporal differences in the activation of three classes of non-transmembrane protein tyrosine kinase following B cell antigen receptor surface engagement. Proc. Natl. Acad. Sci. USA. 91:1994;9524-9528.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 9524-9528
    • Saouaf, S.J.1    Mahajan, S.2    Rowley, R.B.3    Kut, S.4    Fargnoli, J.5    Burkhardt, A.L.6    Tsukada, S.7    Witte, O.N.8    Bolen, J.B.9
  • 67
    • 0028346563 scopus 로고
    • Signal transduction by the B cell antigen receptor and its coreceptors
    • Cambier J. C., Pleiman C. M., Clark M. R. Signal transduction by the B cell antigen receptor and its coreceptors. Annu. Rev. Immunol. 12:1994;457-486.
    • (1994) Annu. Rev. Immunol. , vol.12 , pp. 457-486
    • Cambier, J.C.1    Pleiman, C.M.2    Clark, M.R.3
  • 68
    • 0028014460 scopus 로고
    • Signal transduction by lymphocyte antigen receptors
    • Weiss A., Littman D. R. Signal transduction by lymphocyte antigen receptors. Cell. 76:1994;263-274.
    • (1994) Cell , vol.76 , pp. 263-274
    • Weiss, A.1    Littman, D.R.2
  • 69
    • 0030831199 scopus 로고    scopus 로고
    • The complexity of signaling pathways activated by the BCR
    • DeFranco A. L. The complexity of signaling pathways activated by the BCR. Curr. Opin. Immunol. 9:1997;296-308.
    • (1997) Curr. Opin. Immunol. , vol.9 , pp. 296-308
    • DeFranco, A.L.1
  • 70
    • 0032010114 scopus 로고    scopus 로고
    • Molecular dissection of B cell antigen receptor signaling (review)
    • Kurosaki T. Molecular dissection of B cell antigen receptor signaling (review). Int. J. Mol. Med. 1:1998;515-527.
    • (1998) Int. J. Mol. Med. , vol.1 , pp. 515-527
    • Kurosaki, T.1
  • 73
    • 0030822605 scopus 로고    scopus 로고
    • Phosphorylation of two regulatory tyrosine residues in the activation of Bruton's tyrosine kinase via alternative receptors
    • Wahl M. I., Fluckiger A.-C., Kato R. M., Park H., Witte O. N., Rawlings D. J. Phosphorylation of two regulatory tyrosine residues in the activation of Bruton's tyrosine kinase via alternative receptors. Proc. Natl. Acad. Sci. USA. 94:1997;11526-11533.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 11526-11533
    • Wahl, M.I.1    Fluckiger, A.-C.2    Kato, R.M.3    Park, H.4    Witte, O.N.5    Rawlings, D.J.6
  • 74
    • 0033515021 scopus 로고    scopus 로고
    • In situ detection of activated Bruton's tyrosine kinase in the Ig signaling complex by phosphopeptide-specific monoclonal antibodies
    • Nisitani S., Kato R. M., Rawlings D. J., Witte O. N., Wahl M. I. In situ detection of activated Bruton's tyrosine kinase in the Ig signaling complex by phosphopeptide-specific monoclonal antibodies. Proc. Natl. Acad. Sci. USA. 96:1999;2221-2226.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 2221-2226
    • Nisitani, S.1    Kato, R.M.2    Rawlings, D.J.3    Witte, O.N.4    Wahl, M.I.5
  • 75
    • 0024849618 scopus 로고
    • Analysis of signaling via surface immunoglobulin receptors on B cells from CBA/N mice
    • Rigley K. P., Harnett M. M., Phillips R. J., Klaus G. G. B. Analysis of signaling via surface immunoglobulin receptors on B cells from CBA/N mice. Eur. J. Immunol. 19:1989;2081-2086.
    • (1989) Eur. J. Immunol. , vol.19 , pp. 2081-2086
    • Rigley, K.P.1    Harnett, M.M.2    Phillips, R.J.3    Klaus, G.G.B.4
  • 76
    • 0027397544 scopus 로고
    • Inositol trisphosphate and calcium signalling
    • Berridge M. J. Inositol trisphosphate and calcium signalling. Nature. 361:1993;315-325.
    • (1993) Nature , vol.361 , pp. 315-325
    • Berridge, M.J.1
  • 77
    • 0032127159 scopus 로고    scopus 로고
    • BLNK: A central linker protein in B cell activation
    • Fu C., Turck C. W., Kurosaki T., Chan A. C. BLNK: A central linker protein in B cell activation. Immunity. 9:1998;93-103.
    • (1998) Immunity , vol.9 , pp. 93-103
    • Fu, C.1    Turck, C.W.2    Kurosaki, T.3    Chan, A.C.4
  • 79
    • 0032055484 scopus 로고    scopus 로고
    • Phosphatidylinositol-3,4,5-trisphosphate (PtdIns-3,4,5-P3)/Tec kinase-dependent calcium signaling pathway: A target for SHIP-mediated inhibitory signals
    • Scharenberg A. M., El-Hillal O., Fruman D. A., Beitz L. O., Li Z., Lin S., Gout I., Cantley L. C., Rawlings D. J., Kinet J. P. Phosphatidylinositol-3,4,5-trisphosphate (PtdIns-3,4,5-P3)/Tec kinase-dependent calcium signaling pathway: A target for SHIP-mediated inhibitory signals. EMBO J. 17:1998;1961-1972.
    • (1998) EMBO J. , vol.17 , pp. 1961-1972
    • Scharenberg, A.M.1    El-Hillal, O.2    Fruman, D.A.3    Beitz, L.O.4    Li, Z.5    Lin, S.6    Gout, I.7    Cantley, L.C.8    Rawlings, D.J.9    Kinet, J.P.10
  • 81
    • 0032543221 scopus 로고    scopus 로고
    • T cell receptor-initiated calcium release is uncoupled from capacitative calcium entry in Itk-deficient T cells
    • Liu K. Q., Bunnell S. C., Gurniak C. B., Berg L. J. T cell receptor-initiated calcium release is uncoupled from capacitative calcium entry in Itk-deficient T cells. J. Exp. Med. 187:1998;1721-1727.
    • (1998) J. Exp. Med. , vol.187 , pp. 1721-1727
    • Liu, K.Q.1    Bunnell, S.C.2    Gurniak, C.B.3    Berg, L.J.4
  • 82
    • 0030018304 scopus 로고    scopus 로고
    • A role for Bruton's tyrosine kinase in B cell antigen receptor-mediated activation of phospholipase C-gamma2
    • Takata M., Kurosaki T. A role for Bruton's tyrosine kinase in B cell antigen receptor-mediated activation of phospholipase C-gamma2. J. Exp. Med. 184:1996;31-40.
    • (1996) J. Exp. Med. , vol.184 , pp. 31-40
    • Takata, M.1    Kurosaki, T.2
  • 83
    • 0030610361 scopus 로고    scopus 로고
    • Fc gammaRIIB1 inhibition of BCR-mediated phosphoinositide hydrolysis and Ca2+ mobilization is integrated by CD19 dephosphorylation
    • Hippen K. L., Buhl A. M., D'Ambrosio D., Nakamura K., Persin C., Cambier J. C. Fc gammaRIIB1 inhibition of BCR-mediated phosphoinositide hydrolysis and Ca2+ mobilization is integrated by CD19 dephosphorylation. Immunity. 7:1997;49-58.
    • (1997) Immunity , vol.7 , pp. 49-58
    • Hippen, K.L.1    Buhl, A.M.2    D'Ambrosio, D.3    Nakamura, K.4    Persin, C.5    Cambier, J.C.6
  • 84
    • 0027422088 scopus 로고
    • The signal for capacitative calcium entry
    • Putney J. W. Jr., Bird G. S. J. The signal for capacitative calcium entry. Cell. 75:1993;199-201.
    • (1993) Cell , vol.75 , pp. 199-201
    • Putney J.W., Jr.1    Bird, G.S.J.2
  • 85
    • 0030883269 scopus 로고    scopus 로고
    • Function follows form: The role of store-operated calcium channels in T-cell activation
    • Fanger C. M., Zweifach A., Dolmetsch R. E., Hoth M., Lewis R. S. Function follows form: The role of store-operated calcium channels in T-cell activation. Cell. Physiol. Biochem. 7:1997;203-218.
    • (1997) Cell. Physiol. Biochem. , vol.7 , pp. 203-218
    • Fanger, C.M.1    Zweifach, A.2    Dolmetsch, R.E.3    Hoth, M.4    Lewis, R.S.5
  • 86
    • 0030731130 scopus 로고    scopus 로고
    • The store-operated calcium current I(CRAC): Nonlinear activation by InsP3 and dissociation from calcium release
    • Parekh A. B., Fleig A., Penner R. The store-operated calcium current I(CRAC): Nonlinear activation by InsP3 and dissociation from calcium release. Cell. 89:1997;973-980.
    • (1997) Cell , vol.89 , pp. 973-980
    • Parekh, A.B.1    Fleig, A.2    Penner, R.3
  • 87
    • 0032584584 scopus 로고    scopus 로고
    • Relationship between intracellular calcium store depletion and calcium release-activated calcium current in a mast cell line (RBL-1)
    • Huang Y., Putney J. W. Jr. Relationship between intracellular calcium store depletion and calcium release-activated calcium current in a mast cell line (RBL-1). J. Biol. Chem. 273:1998;19554-19559.
    • (1998) J. Biol. Chem. , vol.273 , pp. 19554-19559
    • Huang, Y.1    Putney J.W., Jr.2
  • 88
    • 0032503687 scopus 로고    scopus 로고
    • PtdIns-3,4,5-P3: A regulatory nexus between tyrosine kinases and sustained calcium signals
    • Scharenberg A. M., Kinet J. P. PtdIns-3,4,5-P3: A regulatory nexus between tyrosine kinases and sustained calcium signals. Cell. 94:1998;5-8.
    • (1998) Cell , vol.94 , pp. 5-8
    • Scharenberg, A.M.1    Kinet, J.P.2
  • 89
    • 0028347321 scopus 로고
    • A 13-amino-acid motif in the cytoplasmic domain of FcgammaRIIB modulates B-cell receptor signalling
    • Muta T., Kurosaki T., Misulovin Z., Sanchez M., Nussenzweig M. C., Ravetch J. V. A 13-amino-acid motif in the cytoplasmic domain of FcgammaRIIB modulates B-cell receptor signalling. Nature. 368:1994;70-73.
    • (1994) Nature , vol.368 , pp. 70-73
    • Muta, T.1    Kurosaki, T.2    Misulovin, Z.3    Sanchez, M.4    Nussenzweig, M.C.5    Ravetch, J.V.6
  • 90
    • 0028851582 scopus 로고
    • The same tyrosine-based inhibition motif, in the intracytoplasmic domain of FccRIIB, regulates negatively BCR-, TCR-, and FcR-dependent cell activation
    • Daeron M., Latour S., Malbec O., Espinosa E., Pina P., Pasmans S., Fridman W. H. The same tyrosine-based inhibition motif, in the intracytoplasmic domain of FccRIIB, regulates negatively BCR-, TCR-, and FcR-dependent cell activation. Immunity. 3:1995;635-646.
    • (1995) Immunity , vol.3 , pp. 635-646
    • Daeron, M.1    Latour, S.2    Malbec, O.3    Espinosa, E.4    Pina, P.5    Pasmans, S.6    Fridman, W.H.7
  • 91
    • 0030582671 scopus 로고    scopus 로고
    • The emerging field of receptor-mediated inhibitory signaling: SHP or SHIP?
    • Scharenberg A. M., Kinet J.-P. The emerging field of receptor-mediated inhibitory signaling: SHP or SHIP? Cell. 87:1996;961-964.
    • (1996) Cell , vol.87 , pp. 961-964
    • Scharenberg, A.M.1    Kinet, J.-P.2
  • 92
    • 0022319106 scopus 로고
    • Crosslinking of surface immunoglobulin and Fc receptors on B lymphocytes inhibits stimulation of inositol phospholipid breakdown via the antigen receptors
    • Bijsterbosch M. K., Klaus G. G. B. Crosslinking of surface immunoglobulin and Fc receptors on B lymphocytes inhibits stimulation of inositol phospholipid breakdown via the antigen receptors. J. Exp. Med. 162:1985;1825-1836.
    • (1985) J. Exp. Med. , vol.162 , pp. 1825-1836
    • Bijsterbosch, M.K.1    Klaus, G.G.B.2
  • 93
    • 0027418367 scopus 로고
    • Cross-linking of IgG receptors inhibits membrane immunoglobulin-stimulated calcium influx in B lymphocytes
    • Choquet D., Partisetti M., Amigorena S., Bonnerot C., Fridman W. H., Korn H. Cross-linking of IgG receptors inhibits membrane immunoglobulin-stimulated calcium influx in B lymphocytes. J. Cell Biol. 121:1993;355-363.
    • (1993) J. Cell Biol. , vol.121 , pp. 355-363
    • Choquet, D.1    Partisetti, M.2    Amigorena, S.3    Bonnerot, C.4    Fridman, W.H.5    Korn, H.6
  • 94
    • 0028179403 scopus 로고
    • Cross-linking of Fc gamma receptor to surface immunoglobulin on B cells provides an inhibitory signal that closes the plasma membrane calcium channel
    • Diegel M. L., Rankin B. M., Bolen J. B., Dubois P. M., Kiener P. A. Cross-linking of Fc gamma receptor to surface immunoglobulin on B cells provides an inhibitory signal that closes the plasma membrane calcium channel. J. Biol. Chem. 269:1994;11409-11416.
    • (1994) J. Biol. Chem. , vol.269 , pp. 11409-11416
    • Diegel, M.L.1    Rankin, B.M.2    Bolen, J.B.3    Dubois, P.M.4    Kiener, P.A.5
  • 95
    • 0343307005 scopus 로고    scopus 로고
    • Deletion of SHIP-1 reveals two distinct pathways for inhibitory signaling
    • Ono M., Okada H., Bolland S., Yanagi S., Kurosaki T., Ravetch J. B. Deletion of SHIP-1 reveals two distinct pathways for inhibitory signaling. Cell. 90:1997;293-301.
    • (1997) Cell , vol.90 , pp. 293-301
    • Ono, M.1    Okada, H.2    Bolland, S.3    Yanagi, S.4    Kurosaki, T.5    Ravetch, J.B.6
  • 96
    • 0032055485 scopus 로고    scopus 로고
    • SHIP modulates immune receptor responses by regulating membrane association of Btk
    • Bolland S., Pearse R. N., Kurosaki T., Ravetch J. V. SHIP modulates immune receptor responses by regulating membrane association of Btk. Immunity. 8:1998;509-516.
    • (1998) Immunity , vol.8 , pp. 509-516
    • Bolland, S.1    Pearse, R.N.2    Kurosaki, T.3    Ravetch, J.V.4
  • 99
    • 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 C. J. Immunoglobulin-mediated signal transduction in B cells from CD45-deficient mice. J. Exp. Med. 183:1996;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
  • 100
    • 0029835940 scopus 로고    scopus 로고
    • Role of the inositol phosphatase SHIP in negative regulation of the immune system by the receptor Fc(gamma)RIIB
    • Ono M., Bolland S., Tempst P., Ravetch J. V. Role of the inositol phosphatase SHIP in negative regulation of the immune system by the receptor Fc(gamma)RIIB. Nature. 383:1996;263-266.
    • (1996) Nature , vol.383 , pp. 263-266
    • Ono, M.1    Bolland, S.2    Tempst, P.3    Ravetch, J.V.4
  • 102
    • 0029965138 scopus 로고    scopus 로고
    • Balancing immunity and tolerance: Deleting and tuning lymphocyte repertoires
    • Goodnow C. C. Balancing immunity and tolerance: Deleting and tuning lymphocyte repertoires. Proc. Natl. Acad. Sci. USA. 93:1996;2264-2271.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 2264-2271
    • Goodnow, C.C.1
  • 103
    • 0030888186 scopus 로고    scopus 로고
    • Differential activation of transcription factors induced by Ca2+ response amplitude and duration
    • Dolmetsch R. E., Lewis R. S., Goodnow C. C., Healy J. I. Differential activation of transcription factors induced by Ca2+ response amplitude and duration. Nature. 386:1997;855-858.
    • (1997) Nature , vol.386 , pp. 855-858
    • Dolmetsch, R.E.1    Lewis, R.S.2    Goodnow, C.C.3    Healy, J.I.4
  • 104
    • 0028834424 scopus 로고
    • The elemental principles of calcium signaling
    • Bootman M. D., Berridge M. J. The elemental principles of calcium signaling. Cell. 83:1995;675-678.
    • (1995) Cell , vol.83 , pp. 675-678
    • Bootman, M.D.1    Berridge, M.J.2
  • 105
  • 106
    • 0025954474 scopus 로고
    • The immunoglobulin light chain related protein lambda 5 is expressed on the surface of mouse pre-B cell lines and can function as a signal transducing molecule
    • Misener V., Downey G. P., Jongstra J. The immunoglobulin light chain related protein lambda 5 is expressed on the surface of mouse pre-B cell lines and can function as a signal transducing molecule. Int. Immunol. 3:1991;1129-1136.
    • (1991) Int. Immunol. , vol.3 , pp. 1129-1136
    • Misener, V.1    Downey, G.P.2    Jongstra, J.3
  • 107
    • 0026096955 scopus 로고
    • Signal transmission through the B cell-specific MB-1 molecule at the pre-B cell stage
    • Nomura J., Matsuo T., Kubota E., Kimoto M., Sakaguchi N. Signal transmission through the B cell-specific MB-1 molecule at the pre-B cell stage. Int. Immunol. 3:1991;117-126.
    • (1991) Int. Immunol. , vol.3 , pp. 117-126
    • Nomura, J.1    Matsuo, T.2    Kubota, E.3    Kimoto, M.4    Sakaguchi, N.5
  • 108
    • 0027505014 scopus 로고
    • Signal transduction in human B cells initiated via Ig beta ligation
    • Nakamura T., Sekar M. C., Kubagawa H., Cooper M. D. Signal transduction in human B cells initiated via Ig beta ligation. Int. Immunol. 5:1993;1309-1315.
    • (1993) Int. Immunol. , vol.5 , pp. 1309-1315
    • Nakamura, T.1    Sekar, M.C.2    Kubagawa, H.3    Cooper, M.D.4
  • 109
    • 0030611753 scopus 로고    scopus 로고
    • The Ig alpha/Igbeta heterodimer on mu-negative proB cells is competent for transducing signals to induce early B cell differentiation
    • Nagata K., Nakamura T., Kitamura F., Kuramochi S., Taki S., Campbell K. S., Karasuyama H. The Ig alpha/Igbeta heterodimer on mu-negative proB cells is competent for transducing signals to induce early B cell differentiation. Immunity. 7:1997;559-570.
    • (1997) Immunity , vol.7 , pp. 559-570
    • Nagata, K.1    Nakamura, T.2    Kitamura, F.3    Kuramochi, S.4    Taki, S.5    Campbell, K.S.6    Karasuyama, H.7
  • 110
    • 0030886340 scopus 로고    scopus 로고
    • Antigen receptor signaling gives lymphocytes a long life
    • Neuberger M. S. Antigen receptor signaling gives lymphocytes a long life. Cell. 90:1997;971-973.
    • (1997) Cell , vol.90 , pp. 971-973
    • Neuberger, M.S.1
  • 111
    • 0030662472 scopus 로고    scopus 로고
    • A reevaluation of the effects of X-linked immunodeficiency (xid) mutation on B cell differentiation and function in the mouse
    • Klaus G. G., Johnson-Leger C., Elgueta-Karstegl C., Atkins C. A reevaluation of the effects of X-linked immunodeficiency (xid) mutation on B cell differentiation and function in the mouse. Eur. J. Immunol. 27:1997;2749-2756.
    • (1997) Eur. J. Immunol. , vol.27 , pp. 2749-2756
    • Klaus, G.G.1    Johnson-Leger, C.2    Elgueta-Karstegl, C.3    Atkins, C.4
  • 112
    • 0029804461 scopus 로고    scopus 로고
    • Profound reduction of mature B cell numbers, reactivities and serum Ig levels in mice which simultaneously carry the XID and CD40 deficiency genes
    • Oka Y., Rolink A. G., Andersson J., Kamanaka M., Uchida J., Yasui T., Kishimoto T., Kikutani H., Melchers F. Profound reduction of mature B cell numbers, reactivities and serum Ig levels in mice which simultaneously carry the XID and CD40 deficiency genes. Int. Immunol. 8:1996;1675-1685.
    • (1996) Int. Immunol. , vol.8 , pp. 1675-1685
    • Oka, Y.1    Rolink, A.G.2    Andersson, J.3    Kamanaka, M.4    Uchida, J.5    Yasui, T.6    Kishimoto, T.7    Kikutani, H.8    Melchers, F.9
  • 114
    • 0029871737 scopus 로고    scopus 로고
    • Regulation of B cell survival in xid mice by the proto-oncogene bcl-2
    • Woodland R. T., Schmidt M. R., Korsmeyer S. J., Gravel K. A. Regulation of B cell survival in xid mice by the proto-oncogene bcl-2. J. Immunol. 156:1996;2143-2154.
    • (1996) J. Immunol. , vol.156 , pp. 2143-2154
    • Woodland, R.T.1    Schmidt, M.R.2    Korsmeyer, S.J.3    Gravel, K.A.4
  • 116
    • 0030267068 scopus 로고    scopus 로고
    • An essential role for tyrosine kinase in the regulation of Bruton's B-cell apoptosis
    • Anderson J. S., Teutsch M., Dong Z., Wortis H. H. An essential role for tyrosine kinase in the regulation of Bruton's B-cell apoptosis. Proc. Natl. Acad. Sci. USA. 93:1996;10966-10971.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 10966-10971
    • Anderson, J.S.1    Teutsch, M.2    Dong, Z.3    Wortis, H.H.4


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