10
Views
4
CrossRef citations to date
0
Altmetric
Cell Growth and Development

Functional Analysis of Csk in Signal Transduction through the B-Cell Antigen Receptor

, , , &
Pages 7306-7313 | Received 07 Jul 1994, Accepted 22 Aug 1994, Published online: 30 Mar 2023

References

  • Autero, M., J. Saharinen, T. Pessa-Morikawa, M. Soula-Rothhut, C. Oetken, M. Gassmann, M. Bergman, K. Alitalo, P. Burn, C. G. Gahmberg, and T. Mustelin. 1994. Tyrosine phosphorylation of CD45 phosphotyrosine phosphatase by p50csk kinase creates a binding site for p56lck tyrosine kinase and activates the phosphatase. Mol. Cell. Biol. 14:1308–1321.
  • Bagrodia, S., I. Chackalaparampil, T. E. Kmiecik, and D. Shalloway. 1991. Altered tyrosine 527 phosphorylation and mitotic activation of p60c-src. Nature (London) 349:172–175.
  • Bergman, M., T. Mustelin, C. Oetkin, J. Partanen, N. F. Flint, K. E. Amerin, M. Autero, P. Burn, and K. Alitalo. 1992. The human p50csk tyrosine kinase phosphorylates p56lck at Tyr-505 and down regulates its catalytic activity. EMBO J. 11:2919–2924.
  • Bijsterbosch, M. K., C. J. Meade, G. A. Turner, and G. G. B. Klaus. 1985. B lymphocyte receptors and polyphosphoinositide degradation. Cell 41:999–1006.
  • Brunswick, M., L. E. Samelson, and J. J. Mond. 1991. Surface immunoglobulin crosslinking activates a tyrosine kinase pathway in B cells is independent of protein kinase C. Proc. Natl. Acad. Sci. USA 88:1311–1314.
  • Buerstedde, J., and S. Takeda. 1991. Increased ratio of targeted to random integration after transfection of chicken B cell lines. Cell 67:179–188.
  • Burkhardt, A. L., M. Brunswick, J. B. Bolen, and J. J. Mond. 1991. Anti-immunoglobulin stimulation of B lymphocytes activates src-related protein-tyrosine kinases. Proc. Natl. Acad. Sci. USA 88:7410–7414.
  • Cambier, J. C., and J. T. Ransom. 1987. Molecular mechanisms of transmembrane signaling in B lymphocytes. Annu. Rev. Immunol. 5:175–199.
  • Campbell, K. S., E. J. Hager, R. J. Freidrich, and J. C. Cambier. 1991. IgM antigen receptor complex contains phosphoprotein products of B29 and mb-1 genes. Proc. Natl. Acad. Sci. USA 88:3982–3986.
  • Campbell, M.-A., and B. M. Sefton. 1992. Association between B-lymphocyte membrane immunoglobulin and multiple members of the Src family of protein tyrosine kinases. Mol. Cell. Biol. 12:2315–2321.
  • 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. 9:2125–2131.
  • Carter, R. H., D. J. Park, S. G. Rhee, and D. T. Fearon. 1991. Tyrosine phosphorylation of phospholipase C induced by membrane immunoglobulin in B lymphocytes. Proc. Natl. Acad. Sci. USA 88:2745–2749.
  • Chan, A. C., M. Iwashima, C. W. Turck, and A. Weiss. 1992. ZAP-70: a 70 kd protein-tyrosine kinase that associates with the TCRz chain. Cell 71:649–662.
  • Chen, C., J. E. Lehmeyer, and M. D. Cooper. 1982. Evidence for an IgD homologue on chicken lymphocytes. J. Immunol. 129:2580–2585.
  • Chow, L. L., M. Fournel, D. Davidson, and A. Villette. 1993. Negative regulation of T-cell receptor signalling by tyrosine protein kinase p50csk. Nature (London) 365:156–160.
  • Clark, M. R., K. S. Campbell, A. Kazlauskas, S. A. Johnson, M. Hertz, T. A. Potter, C. Pleiman, and J. C. Cambier. 1992. The B cell antigen receptor complex: association of Ig-α and Ig-β with distinct cytoplasmic effectors. Science 258:123–126.
  • Cooper, J. A., K. L. Gould, C. A. Cartwright, and T. Hunter. 1986. Tyrosine 527 is phosphorylated in pp60c-src: implication for regulation. Science 231:1431–1434.
  • Couture, C., G. Baier, A. Altman, and T. Mustelin. 1994. p56lck-independent activation and tyrosine phosphorylation of p72syk by T-cell antigen receptor/CD3 stimulation. Proc. Natl. Acad. Sci. USA 91:5301–5305.
  • Gold, M. R., D. A. Law, and A. L. DeFranco. 1990. Stimulation of protein tyrosine phosphorylation by the B-lymphocyte antigen receptor. Nature (London) 345:810–4813.
  • Gold, M. R., L. Matsuuchi, R. B. Kelly, and A. L. DeFranco. 1991. Tyrosine phosphorylation of components of the B-cell antigen receptors following receptor crosslinking. Proc. Natl. Acad. Sci. USA 88:3436–3440.
  • Grynkiewicz, G., M. Poenie, and R. Y. Tsien. 1985. A new generation of Ca2+ indicators with greatly improved fluorescence properties. J. Biol. Chem. 260:3440–3450.
  • Hata, A., H. Sabe, and H. Hanafusa. Unpublished data.
  • Hermanson, G. G., D. Eisenberg, P. W. Kincaid, and R. Wall. 1988. B29: a member of the immunoglobulin gene superfamily exclusively expressed on B-lineage cells. Proc. Natl. Acad. Sci. USA 85:6890–6894.
  • Hombach, J., L. Leclercq, A. Radbruch, K. Rajewsky, and M. Reth. 1988. A novel 34-kd protein co-isolated with the IgM molecule in surface IgM-expressing cells. EMBO J. 7:3451–3456.
  • Hurley, T. R., R. Hyman, and B. M. Sefton. 1993. Differential effects of expression of the CD45 tyrosine protein phosphatase on the tyrosine phosphorylation of the lck, fyn, and c-src tyrosine protein kinases. Mol. Cell. Biol. 13:1651–1656.
  • Hutchcroft, J. E., M. L. Harrison, and R. L. Geahlen. 1991. B lymphocyte activation is accompanied by phosphorylation of a 72-kDa protein-tyrosine kinase. J. Biol. Chem. 266:14846–14849.
  • Iba, H., F. R. Cross, E. A. Garber, and H. Hanafusa. 1985. Low level of cellular protein phosphorylation by nontransforming overproduced p60c-src. Mol. Cell. Biol. 5:1058–1066.
  • Imamoto, A., and P. Soriano. 1993. Disruption of the csk gene, encoding a negative regulator of Src family tyrosine kinases, leads to neural tube defects and embryonic lethality in mice. Cell 73:1117–1124.
  • Jove, R., and H. Hanafusa. 1987. Cell transformation by the viral src oncogene. Annu. Rev. Cell Biol. 3:31–56.
  • Justement, L. B., K. S. Campbell, N. C. Chien, and J. C. Cambier. 1991. Regulation of B cell antigen receptor signal transduction and phosphorylation by CD45. Science 252:1839–1842.
  • Kishihara, K., J. Penninger, V. A. Wallace, T. M. Kundig, K. Kawai, A. Wakeham, E. Timms, K. Pfeifer, P. S. Ohashi, M. L. Thomas, C. Furlonger, C. J. Paige, and T. W. Mak. 1993. Normal B lymphocyte development but impaired T cell maturation in CD45-exon 6 protein tyrosine phosphatase-deficient mice. Cell 74:143–156.
  • Kurosaki, T., M. Takata, Y. Yamanashi, T. Inazu, T. Taniguchi, Y. Yamamoto, and H. Yamamura. 1994. Syk activation by the Src-family tyrosine kinase in the B cell receptor signaling. J. Exp. Med. 179:1725–1729.
  • Lane, P. J. L., J. A. Ledbetter, F. M. McConnel, K. Draves, J. Deans, G. L. Schieven, and E. A. Clark. 1991. The role of tyrosine phosphorylation in signal transduction through surface Ig in human B cells. J. Immunol. 146:715–722.
  • Mayer, B., M. Hamaguchi, and H. Hanafusa. 1988. A novel viral oncogene product with structural similarity to phospholipase C. Nature (London) 332:272–275.
  • McFarland, E. D. C., T. R. Hurley, J. T. Pingel, B. M. Sefton, A. Shaw, and M. L. Thomas. 1993. Correlation between Src family member regulation by the protein-tyrosine-phosphatase CD45 and transmembrane signaling through the T-cell receptor. Proc. Natl. Acad. Sci. USA 90:1402–1406.
  • Nada, S., M. Okada, A. MacAuley, J. A. Cooper, and H. Nakagawa. 1991. Cloning of a complementary DNA for a protein-tyrosine kinase that specifically phosphorylates a negative regulatory site of p60c-src. Nature (London) 351:69–72.
  • Nada, S., T. Yagi, H. Takeda, T. Tokunaga, H. Nakagawa, Y. Ikawa, M. Okada, and S. Aizawa. 1993. Constitutive activation of Src family kinases in mouse embryos that lack Csk. Cell 73:1125–1135.
  • Okada, M., S. Nada, Y. Yamanashi, T. Yamamoto, and H. Nakagawa. 1991. CSK: a protein-tyrosine kinase involved in regulation of src family kinases. J. Biol. Chem. 266:24249–24252.
  • Okada, M., and H. Nakagawa. 1989. A protein tyrosine kinase involved in regulation of pp60c-src function. J. Biol. Chem. 264:20886–20893.
  • Reth, M. 1989. Antigen receptor tail clue. Nature (London) 338:383–384.
  • Sabe, Η., B. Knudsen, M. Okada, S. Nada, H. Nakagawa, and H. Hanafusa. 1992. Molecular cloning and expression of chicken C-terminal Src kinase: lack of stable association with c-Src protein. Proc. Natl. Acad. Sci. USA 89:2190–2194.
  • Sabe, Η., M. Okada, H. Nakagawa, and H. Hanafusa. 1992. Activation of c-Src in cells bearing v-Crk and its suppression by Csk. Mol. Cell. Biol. 12:4706–4713.
  • Sambrook, J., E. F. Fritsch, and T. Maniatis. 1989. Molecular cloning: a laboratory manual, 2nd ed. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
  • Sanchez, M., Z. Misulovin, A. L. Burkhardt, S. Mahajan, T. Costa, R. Franke, J. B. Bolen, and M. Nussenzweig. 1993. Signal transduction by immunoglobulin is mediated through Igα and Igβ. J. Exp. Med. 178:1049–1055.
  • Takata, M., H. Sabe, A. Hata, T. Inazu, Y. Homma, T. Nukada, H. Yamamura, and T. Kurosaki. 1994. Tyrosine kinases Lyn and Syk regulate B cell receptor-coupled Ca2+ mobilization through distinct pathways. EMBO J. 13:1341–1349.
  • Taniguchi, T., T. Kobayahi, J. Kondo, K. Takahashi, H. Nakamura, J. Suzuki, K. Nagai, T. Yamada, S.-I. Nakamura, and H. Yamamura. 1991. Molecular cloning of a porcine gene syk that encodes a 72-kDa protein-tyrosine kinase showing high susceptibility to proteolysis. J. Biol. Chem. 266:15790–15796.
  • Trowbridge, I. S. 1991. CD45. J. Biol. Chem. 266:23517–23520.
  • Weiss, A. 1993. T cell antigen receptor signal transduction: a tale of tails and cytoplasmic protein-tyrosine kinases. Cell 73:209–212.
  • Weiss, A., and D. R. Littman. 1994. Signal transduction by lymphocyte antigen receptors. Cell 76:263–274.
  • Yamanashi, Y., T. Kakiuchi, J. Mizuguchi, T. Yamamoto, and K. Toyoshima. 1991. Association of B cell antigen receptor with protein tyrosine kinase Lyn. Science 251:192–194.

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.