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Volumn 29, Issue 10, 1999, Pages 3179-3187

Tyrosine kinase-dependent ubiquitination of CD16 ζ subunit in human NK cells following receptor engagement

Author keywords

Fc receptor; NK cell; Phosphorylation; Signal transduction; Ubiquitination

Indexed keywords

CD16 ANTIGEN; GENISTEIN; IMMUNOGLOBULIN G; IMMUNOGLOBULIN RECEPTOR; LIGAND; LYMPHOCYTE RECEPTOR; PHOSPHOTRANSFERASE; PROTEIN TYROSINE KINASE; RECEPTOR SUBUNIT; UBIQUITIN;

EID: 0032843891     PISSN: 00142980     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1521-4141(199910)29:10<3179::AID-IMMU3179>3.0.CO;2-9     Document Type: Article
Times cited : (19)

References (43)
  • 2
    • 0029162583 scopus 로고
    • Selective protein degradation: A journey's end within the proteasome
    • Jentsch, S. and Schlenker, S., Selective protein degradation: a journey's end within the proteasome. Cell 1995. 82: 881-884.
    • (1995) Cell , vol.82 , pp. 881-884
    • Jentsch, S.1    Schlenker, S.2
  • 3
    • 0030457014 scopus 로고    scopus 로고
    • Ubiquitin-dependent protein degradation
    • Hochstrasser, M., Ubiquitin-dependent protein degradation. Annu. Rev. Genet. 1996. 4: 405-439.
    • (1996) Annu. Rev. Genet. , vol.4 , pp. 405-439
    • Hochstrasser, M.1
  • 4
    • 0029861143 scopus 로고    scopus 로고
    • The N-end rule: Functions, mysteries, uses
    • Varshavsky, A., The N-end rule: functions, mysteries, uses. Proc. Natl. Acad. Sci. USA 1996. 93: 12142-12149.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 12142-12149
    • Varshavsky, A.1
  • 5
    • 0030997067 scopus 로고    scopus 로고
    • Regulating protein degradation by ubiquitination
    • Weissman, A. M., Regulating protein degradation by ubiquitination. Immunol. Today 1997. 18: 189-198.
    • (1997) Immunol. Today , vol.18 , pp. 189-198
    • Weissman, A.M.1
  • 6
    • 0026664626 scopus 로고
    • Ligand-induced polyubiquitination of the platelet-derived growth factor β-receptor
    • Mori, S., Heldin, C. H. and Claesson-Welsh, L., Ligand-induced polyubiquitination of the platelet-derived growth factor β-receptor. J. Biol. Chem. 1992. 267: 6429-6434.
    • (1992) J. Biol. Chem. , vol.267 , pp. 6429-6434
    • Mori, S.1    Heldin, C.H.2    Claesson-Welsh, L.3
  • 7
    • 0028840915 scopus 로고
    • Degradation of CFTR by the ubiquitin-proteasome pathway
    • Ward, C. L., Omura, S. and Kopito, R. R., Degradation of CFTR by the ubiquitin-proteasome pathway. Cell 1995. 83: 121-127.
    • (1995) Cell , vol.83 , pp. 121-127
    • Ward, C.L.1    Omura, S.2    Kopito, R.R.3
  • 8
    • 0029008487 scopus 로고
    • Herbymicin A induces the 20 S proteasome- and ubiquitin-dependent degradation of receptor tyrosine kinases
    • Sepp-Lorenzino, L., Ma, Z., Lebwohl, D. E., Vinitsky, A. and Rosen, N., Herbymicin A induces the 20 S proteasome- and ubiquitin-dependent degradation of receptor tyrosine kinases. J. Biol. Chem. 1995. 270: 16580-16587.
    • (1995) J. Biol. Chem. , vol.270 , pp. 16580-16587
    • Sepp-Lorenzino, L.1    Ma, Z.2    Lebwohl, D.E.3    Vinitsky, A.4    Rosen, N.5
  • 9
    • 0030054178 scopus 로고    scopus 로고
    • Ubiquitination of a yeast plasma membrane receptor signals its ligand-stimulated endocytosis
    • Hicke, L. and Riezman, H., Ubiquitination of a yeast plasma membrane receptor signals its ligand-stimulated endocytosis. Cell 1996. 84: 277-286.
    • (1996) Cell , vol.84 , pp. 277-286
    • Hicke, L.1    Riezman, H.2
  • 10
    • 0029765099 scopus 로고    scopus 로고
    • The ubiquitin conjugation system is required for ligand-induced endocytosis and degradation of the growth hormone receptor
    • Strous, G. J., van Kerkhof, P., Govers, R., Ciechanover, A. and Schwartz, A., The ubiquitin conjugation system is required for ligand-induced endocytosis and degradation of the growth hormone receptor. EMBO J. 1996. 15: 3806-3812.
    • (1996) EMBO J. , vol.15 , pp. 3806-3812
    • Strous, G.J.1    Van Kerkhof, P.2    Govers, R.3    Ciechanover, A.4    Schwartz, A.5
  • 11
    • 0030797998 scopus 로고    scopus 로고
    • Linkage of the ubiquitin-conjugating system and the endocytic pathway in ligand-induced internalization of the growth hormone receptor
    • Govers, R., van Kerkhof, P., Schwartz, A. L. and Strous, G. J., Linkage of the ubiquitin-conjugating system and the endocytic pathway in ligand-induced internalization of the growth hormone receptor. EMBO J. 1997. 16: 4851-4858.
    • (1997) EMBO J. , vol.16 , pp. 4851-4858
    • Govers, R.1    Van Kerkhof, P.2    Schwartz, A.L.3    Strous, G.J.4
  • 13
    • 0027458572 scopus 로고
    • Cell surface control of the multiubiquitination and deubiquitination of high-affinity immunoglobulin E receptor
    • Paolini, R. and Kinet, J.-P., Cell surface control of the multiubiquitination and deubiquitination of high-affinity immunoglobulin E receptor. EMBO J. 1993. 12: 779-786.
    • (1993) EMBO J. , vol.12 , pp. 779-786
    • Paolini, R.1    Kinet, J.-P.2
  • 14
    • 0028158499 scopus 로고
    • Ligand-dependent polyubiquitination of c-kit gene product: A possible mechanism of receptor down modulation in M07e cells
    • Miyazaka, K., Toyama, K., Gotoh, A., Hendrie, P. C., Mantel, C. and Broxmeyer, H. E., Ligand-dependent polyubiquitination of c-kit gene product: a possible mechanism of receptor down modulation in M07e cells. Blood 1994. 83: 137-145.
    • (1994) Blood , vol.83 , pp. 137-145
    • Miyazaka, K.1    Toyama, K.2    Gotoh, A.3    Hendrie, P.C.4    Mantel, C.5    Broxmeyer, H.E.6
  • 15
    • 0024451644 scopus 로고
    • CD3-negative natural killer cells express ζ TCR as part of a novel molecular complex
    • Anderson, P., Caligiuri, M., Ritz, J. and Schlossman, S. F., CD3-negative natural killer cells express ζ TCR as part of a novel molecular complex. Nature 1989. 341: 159-162.
    • (1989) Nature , vol.341 , pp. 159-162
    • Anderson, P.1    Caligiuri, M.2    Ritz, J.3    Schlossman, S.F.4
  • 16
    • 0024822508 scopus 로고
    • Co-association of CD3ζ with a receptor (CD16) for IgG Fc on human natural killer cells
    • Lanier, L. L., Yu, G. and Phillips, J. H., Co-association of CD3ζ with a receptor (CD16) for IgG Fc on human natural killer cells. Nature 1989. 342: 803-805.
    • (1989) Nature , vol.342 , pp. 803-805
    • Lanier, L.L.1    Yu, G.2    Phillips, J.H.3
  • 17
    • 0026015285 scopus 로고
    • Characterization of the family of dimer associated with Fc receptors (FcεRI and FcγRIII)
    • Letourneur, O., Kennedy, I. C. S., Brini, A. T., Ortaldo, J. R., O'Shea, J. and Kinet, J.-P., Characterization of the family of dimer associated with Fc receptors (FcεRI and FcγRIII). J. Immunol. 1991. 147: 2652-2656.
    • (1991) J. Immunol. , vol.147 , pp. 2652-2656
    • Letourneur, O.1    Kennedy, I.C.S.2    Brini, A.T.3    Ortaldo, J.R.4    O'Shea, J.5    Kinet, J.-P.6
  • 19
    • 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 1993. 73: 209-212.
    • (1993) Cell , vol.73 , pp. 209-212
    • Weiss, A.1
  • 20
    • 0029082078 scopus 로고
    • Antigen and Fc receptor signaling. The awesome power of the immunoreceptor tyrosine-based activation motif (ITAM)
    • Cambier, J. C., Antigen and Fc receptor signaling. The awesome power of the immunoreceptor tyrosine-based activation motif (ITAM). J. Immunol. 1995. 155: 3281-3285.
    • (1995) J. Immunol. , vol.155 , pp. 3281-3285
    • Cambier, J.C.1
  • 21
    • 0028130057 scopus 로고
    • Fc receptors: Rubor redux
    • Ravetch, J. V., Fc receptors: rubor redux. Cell 1994. 78: 553-560.
    • (1994) Cell , vol.78 , pp. 553-560
    • Ravetch, J.V.1
  • 22
    • 0028859279 scopus 로고
    • Protein modules and signalling networks
    • Pawson, T., Protein modules and signalling networks. Nature 1995. 373: 573-580.
    • (1995) Nature , vol.373 , pp. 573-580
    • Pawson, T.1
  • 25
    • 0029057410 scopus 로고
    • Interaction between lck and syk family tyrosine kinases in Fcγ receptor-initiated activation of natural killer cells
    • Ting, A. T., Dick, C. J., Schoon, R. A., Karnitz, L. M., Abraham, R. T. and Leibson, P. J., Interaction between lck and syk family tyrosine kinases in Fcγ receptor-initiated activation of natural killer cells. J. Biol. Chem. 1995. 270: 16415-16421.
    • (1995) J. Biol. Chem. , vol.270 , pp. 16415-16421
    • Ting, A.T.1    Dick, C.J.2    Schoon, R.A.3    Karnitz, L.M.4    Abraham, R.T.5    Leibson, P.J.6
  • 26
    • 0026008159 scopus 로고
    • Engagement of the natural killer cell IgG Fc receptor results in tyrosine phosphorylation of the ζ chain
    • O'Shea, J. J., Weissman, A. M., Kennedy, I. C. S. and Ortaldo, J. R., Engagement of the natural killer cell IgG Fc receptor results in tyrosine phosphorylation of the ζ chain. Proc. Natl. Acad. Sci. USA 1991. 88: 350-354.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 350-354
    • O'Shea, J.J.1    Weissman, A.M.2    Kennedy, I.C.S.3    Ortaldo, J.R.4
  • 27
    • 0026021836 scopus 로고
    • Tyrosine phosphorylation of the FcγRIII (CD16): ζ complex in human natural killer cells
    • Vivier, E., Morin, P., O'Brien, C., Druker, B., Schlossman, S. F. and Anderson, P., Tyrosine phosphorylation of the FcγRIII (CD16): ζ complex in human natural killer cells. J. Immunol. 1991. 146: 206-210.
    • (1991) J. Immunol. , vol.146 , pp. 206-210
    • Vivier, E.1    Morin, P.2    O'Brien, C.3    Druker, B.4    Schlossman, S.F.5    Anderson, P.6
  • 28
    • 0031572521 scopus 로고    scopus 로고
    • Selective binding of shc-SH2 domain to tyrosine-phosphorylated ζ- but not γ-chain upon CD16 ligation on human NK cells
    • Galandrini, R., Palmieri, G., Paolini, R., Piccoli, M., Frati, L. and Santoni, A., Selective binding of shc-SH2 domain to tyrosine-phosphorylated ζ- but not γ-chain upon CD16 ligation on human NK cells. J. Immunol. 1997. 159: 3767-3773.
    • (1997) J. Immunol. , vol.159 , pp. 3767-3773
    • Galandrini, R.1    Palmieri, G.2    Paolini, R.3    Piccoli, M.4    Frati, L.5    Santoni, A.6
  • 29
    • 0027444588 scopus 로고
    • Receptors for the Fc fragment of IgG on natural killer cells
    • Trinchieri, G. and Valiante, N., Receptors for the Fc fragment of IgG on natural killer cells. Nat. Immun. 1993. 12: 218-234.
    • (1993) Nat. Immun. , vol.12 , pp. 218-234
    • Trinchieri, G.1    Valiante, N.2
  • 30
    • 0030848994 scopus 로고    scopus 로고
    • Signal transduction during natural killer cell activation: Inside the mind of a killer
    • Leibson, P. J., Signal transduction during natural killer cell activation: inside the mind of a killer. Immunity 1997. 6: 655-661.
    • (1997) Immunity , vol.6 , pp. 655-661
    • Leibson, P.J.1
  • 31
    • 0027228369 scopus 로고
    • Constitutive tyrosine phosphorylation of the T-cell receptor (TCR) ζ subunit: Regulation of TCR-associated protein tyrosine kinase activity by TCR ζ
    • van Oers, N. S. C., Tao, W., Watts, J. D., Johnson, P., Aebersold, R. and Teh, H.-S., Constitutive tyrosine phosphorylation of the T-cell receptor (TCR) ζ subunit: regulation of TCR-associated protein tyrosine kinase activity by TCR ζ. Mol. Cell. Biol. 1993. 13: 5771-5780.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 5771-5780
    • Van Oers, N.S.C.1    Tao, W.2    Watts, J.D.3    Johnson, P.4    Aebersold, R.5    Teh, H.-S.6
  • 32
    • 0021099710 scopus 로고
    • Components of ubiquitin-protein ligase system. Resolution, affinity purification, and role in protein breakdown
    • Hershko, A., Heller, H., Elias, S. and Ciechanover, A., Components of ubiquitin-protein ligase system. Resolution, affinity purification, and role in protein breakdown. J. Biol. Chem. 1983. 258: 8206-8214.
    • (1983) J. Biol. Chem. , vol.258 , pp. 8206-8214
    • Hershko, A.1    Heller, H.2    Elias, S.3    Ciechanover, A.4
  • 33
    • 0033525589 scopus 로고    scopus 로고
    • A novel ubiquitination factor, E4, is involved in multiubiquitin chain assembly
    • Koegl, M., Hoppe, T., Schlenker, S., Ulrich, H. D., Mayer, T. U. and Jentsch, S., A novel ubiquitination factor, E4, is involved in multiubiquitin chain assembly. Cell 1999. 96: 635-644.
    • (1999) Cell , vol.96 , pp. 635-644
    • Koegl, M.1    Hoppe, T.2    Schlenker, S.3    Ulrich, H.D.4    Mayer, T.U.5    Jentsch, S.6
  • 34
    • 0031448209 scopus 로고    scopus 로고
    • Activation of the Lck tyrosine kinase targets cell surface T cell antigen receptors for lysosomal degradation
    • D'Oro, U., Vacchio, M. S., Weissman, A. M. and Ashwell, J. D., Activation of the Lck tyrosine kinase targets cell surface T cell antigen receptors for lysosomal degradation. Immunity 1997. 7: 619-628.
    • (1997) Immunity , vol.7 , pp. 619-628
    • D'Oro, U.1    Vacchio, M.S.2    Weissman, A.M.3    Ashwell, J.D.4
  • 35
    • 0032550179 scopus 로고    scopus 로고
    • Cytoplasmic tail phosphorylation of the alpha-factor receptor is required for its ubiquitination and internalization
    • Hicke, L., Zanolari, B. and Riezman, H., Cytoplasmic tail phosphorylation of the alpha-factor receptor is required for its ubiquitination and internalization. J. Cell Biol. 1998. 141: 349-358.
    • (1998) J. Cell Biol. , vol.141 , pp. 349-358
    • Hicke, L.1    Zanolari, B.2    Riezman, H.3
  • 36
    • 0028970734 scopus 로고
    • Stimulation-dependent I(Greek small letter script kappa)Bα phosphorylation marks the NF-(Greek small letter script kappa)B inhibitor for degradation via the ubiquitin-proteasome pathway
    • Alkalay, I., Yaron, A., Hatzubai, A., Orian, A., Ciechanover, A. and Ben-Neriah, Y., Stimulation-dependent I(Greek small letter script kappa)Bα phosphorylation marks the NF-(Greek small letter script kappa)B inhibitor for degradation via the ubiquitin-proteasome pathway. Proc. Natl. Acad. Sci. USA 1995. 92: 10599-10603.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 10599-10603
    • Alkalay, I.1    Yaron, A.2    Hatzubai, A.3    Orian, A.4    Ciechanover, A.5    Ben-Neriah, Y.6
  • 37
    • 0029916504 scopus 로고    scopus 로고
    • T cell antigen receptor ubiquitination is a consequence of receptor-mediated tyrosine kinase activation
    • Cenciarelli, C., Wilhelm, K., Guo, A. and Weissman, A. M., T cell antigen receptor ubiquitination is a consequence of receptor-mediated tyrosine kinase activation. J. Biol. Chem. 1996. 271: 8709-8713.
    • (1996) J. Biol. Chem. , vol.271 , pp. 8709-8713
    • Cenciarelli, C.1    Wilhelm, K.2    Guo, A.3    Weissman, A.M.4
  • 38
    • 0027402689 scopus 로고
    • Ligand-induced ubiquitination of the platelet-derived growth factor beta-receptor plays a negative regulatory role in its mitogenic signaling
    • Mori, S., Heldin, C. H. and Claesson-Welsh, L., Ligand-induced ubiquitination of the platelet-derived growth factor beta-receptor plays a negative regulatory role in its mitogenic signaling. J. Biol. Chem. 1993. 268: 577-583.
    • (1993) J. Biol. Chem. , vol.268 , pp. 577-583
    • Mori, S.1    Heldin, C.H.2    Claesson-Welsh, L.3
  • 39
    • 0030004897 scopus 로고    scopus 로고
    • Site-specific phosphorylation of I(Greek small letter script kappa)Bα by a novel ubiquitination-dependent protein kinase activity
    • Chen, Z. J., Parent, L. and Maniatis, T., Site-specific phosphorylation of I(Greek small letter script kappa) Bα by a novel ubiquitination-dependent protein kinase activity. Cell 1996. 84: 853-862.
    • (1996) Cell , vol.84 , pp. 853-862
    • Chen, Z.J.1    Parent, L.2    Maniatis, T.3
  • 40
    • 0026772564 scopus 로고
    • Protein ubiquitination is regulated by phosphorylation. An in vitro study
    • Kong, S.-K. and Chock, P. B., Protein ubiquitination is regulated by phosphorylation. An in vitro study. J. Biol. Chem. 1992. 267: 14189-14192.
    • (1992) J. Biol. Chem. , vol.267 , pp. 14189-14192
    • Kong, S.-K.1    Chock, P.B.2
  • 41
    • 0022379602 scopus 로고
    • The immunochemical detection and quantitation of intracellular ubiquitin-protein conjugates
    • Haas, A. L. and Bright, P. M., The immunochemical detection and quantitation of intracellular ubiquitin-protein conjugates. J. Biol. Chem. 1985. 260: 12464-12473.
    • (1985) J. Biol. Chem. , vol.260 , pp. 12464-12473
    • Haas, A.L.1    Bright, P.M.2
  • 42
    • 0000828765 scopus 로고
    • Preferential proliferation of natural killer cells among peripheral blood mononuclear cells cocultured with B lymphoblastoid cell lines
    • Perussia, B., Ramoni, C., Anegon, I., Cuturi, C., Faust, J. and Trinchieri, G., Preferential proliferation of natural killer cells among peripheral blood mononuclear cells cocultured with B lymphoblastoid cell lines. Nat. Immun. Cell Growth Regul. 1987. 6: 171-188.
    • (1987) Nat. Immun. Cell Growth Regul. , vol.6 , pp. 171-188
    • Perussia, B.1    Ramoni, C.2    Anegon, I.3    Cuturi, C.4    Faust, J.5    Trinchieri, G.6
  • 43
    • 0000498346 scopus 로고
    • Expression of proteins in mammalian cells using vaccinia viral vectors
    • Ausubel, F. M., Brent, R., Kingston, R. E., Moore, D. D., Seidman, J. G., Smith, J. A. and Struhl, K. (Eds.). Green Publishing and Wiley-Interscience, New York
    • Earl, P. L., Cooper, N. and Moss, B., Expression of proteins in mammalian cells using vaccinia viral vectors. In Ausubel, F. M., Brent, R., Kingston, R. E., Moore, D. D., Seidman, J. G., Smith, J. A. and Struhl, K. (Eds.). Current Protocols in Molecular Biology. Green Publishing and Wiley-Interscience, New York 1991, pp 16.16-16.18.
    • (1991) Current Protocols in Molecular Biology , pp. 1616-1618
    • Earl, P.L.1    Cooper, N.2    Moss, B.3


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