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Volumn 163, Issue 11, 1999, Pages 5827-5835

Inhibition of signaling through the B cell antigen receptor by the protooncogene product, c-Cbl, requires Syk tyrosine 317 and the c-Cbl phosphotyrosine-binding domain

Author keywords

[No Author keywords available]

Indexed keywords

COMPLEMENTARY DNA; GENE PRODUCT; IONOMYCIN; LYMPHOCYTE RECEPTOR; PHORBOL 13 ACETATE 12 MYRISTATE; PHOSPHOTYROSINE; PROTEIN TYROSINE KINASE; TRANSCRIPTION FACTOR;

EID: 0033485914     PISSN: 00221767     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (63)

References (32)
  • 1
    • 0030175744 scopus 로고
    • Regulation of antigen receptor signal transduction by protein tyrosine kinases
    • Chan, A. C., and A. S. Shaw. 1995. Regulation of antigen receptor signal transduction by protein tyrosine kinases. Curr. Opin. Immunol. 8:394.
    • (1995) Curr. Opin. Immunol. , vol.8 , pp. 394
    • Chan, A.C.1    Shaw, A.S.2
  • 2
    • 0028014460 scopus 로고
    • Signal transduction by lymphocyte antigen receptors
    • Weiss, A., and D. R. Littman. 1994. Signal transduction by lymphocyte antigen receptors. Cell 76:263.
    • (1994) Cell , vol.76 , pp. 263
    • Weiss, A.1    Littman, D.R.2
  • 3
    • 0000722327 scopus 로고
    • New nomenclature for the Reth motif (or ARHi/TAM/ ARAM/YXXL)
    • Cambier, J. C. 1995. New nomenclature for the Reth motif (or ARHi/TAM/ ARAM/YXXL). Immunol. Today 16:110.
    • (1995) Immunol. Today , vol.16 , pp. 110
    • Cambier, J.C.1
  • 4
    • 0024980981 scopus 로고
    • Antigen receptor tail clue
    • Reth, M. 1989. Antigen receptor tail clue. Nature 338:383.
    • (1989) Nature , vol.338 , pp. 383
    • Reth, M.1
  • 5
    • 0028125752 scopus 로고
    • Dual role of the tyrosine activation motif of the Ig-α protein during signal transduction via the B cell antigen receptor
    • Flaswinkel, H., and M. Reth. 1994. Dual role of the tyrosine activation motif of the Ig-α protein during signal transduction via the B cell antigen receptor. EMBO J. 13:83.
    • (1994) EMBO J. , vol.13 , pp. 83
    • Flaswinkel, H.1    Reth, M.2
  • 6
    • 0000387536 scopus 로고
    • B cell antigen receptor motifs have redundant signaling capabilities and bind the tyrosine kinases PTK72, Lyn and Fyn
    • Law, D. A., V. W.-F. Chan, S. K. Datta, and A. L. DeFranco. 1993. B cell antigen receptor motifs have redundant signaling capabilities and bind the tyrosine kinases PTK72, Lyn and Fyn. Curr. Biol. 3:645.
    • (1993) Curr. Biol. , vol.3 , pp. 645
    • Law, D.A.1    Chan, V.W.-F.2    Datta, S.K.3    DeFranco, A.L.4
  • 9
    • 0030968306 scopus 로고    scopus 로고
    • Syk activation and dissociation from the B-cell antigen receptor is mediated by phosphorylation of tyrosine 130
    • Keshvara, L.M., C. Isaacson, M. L. Harrison, and R. L. Geahlen. 1997. Syk activation and dissociation from the B-cell antigen receptor is mediated by phosphorylation of tyrosine 130. J. Biol. Chem. 272:10377.
    • (1997) J. Biol. Chem. , vol.272 , pp. 10377
    • Keshvara, L.M.1    Isaacson, C.2    Harrison, M.L.3    Geahlen, R.L.4
  • 10
    • 0028783396 scopus 로고
    • Role of the Syk autophosphorylation site and SH2 domains in B cell antigen receptor signaling
    • Kurosaki, T., S. A. Johnson, L. Pao, K. Sada, H. Yamamura, and J. C. Cambier. 1995. Role of the Syk autophosphorylation site and SH2 domains in B cell antigen receptor signaling. J. Exp. Med. 182:1815.
    • (1995) J. Exp. Med. , vol.182 , pp. 1815
    • Kurosaki, T.1    Johnson, S.A.2    Pao, L.3    Sada, K.4    Yamamura, H.5    Cambier, J.C.6
  • 12
    • 0032534071 scopus 로고    scopus 로고
    • Syk- and Lyn-dependent phosphorylation of Syk on multiple tyrosines following B-cell activation includes a site that negatively regulates signaling
    • Keshvara, L. M., C. C. Isaacson, T. M. Yankee, R. Sarac, M. L. Harrison, and R. L. Geahlen. 1998. Syk- and Lyn-dependent phosphorylation of Syk on multiple tyrosines following B-cell activation includes a site that negatively regulates signaling. J. Immunol. 161:5276.
    • (1998) J. Immunol. , vol.161 , pp. 5276
    • Keshvara, L.M.1    Isaacson, C.C.2    Yankee, T.M.3    Sarac, R.4    Harrison, M.L.5    Geahlen, R.L.6
  • 13
    • 0032502734 scopus 로고    scopus 로고
    • Coordinated regulation of the tyrosine phosphorylation of Cbl by Fyn and Syk tyrosine kinases
    • Deckert, M., C. Elly, A. Altman, and Y.-C. Liu. 1998. Coordinated regulation of the tyrosine phosphorylation of Cbl by Fyn and Syk tyrosine kinases. J. Biol. Chem. 273:8867.
    • (1998) J. Biol. Chem. , vol.273 , pp. 8867
    • Deckert, M.1    Elly, C.2    Altman, A.3    Liu, Y.-C.4
  • 14
    • 0030499383 scopus 로고    scopus 로고
    • Functional and physical interactions of Syk family kinases with the Vav proto-oncogene product
    • Deckert, M., S. Tartare-Deckert, C. Couture, T. Mustelin, and A. Altman. 1996. Functional and physical interactions of Syk family kinases with the Vav proto-oncogene product. Immunity 5:591.
    • (1996) Immunity , vol.5 , pp. 591
    • Deckert, M.1    Tartare-Deckert, S.2    Couture, C.3    Mustelin, T.4    Altman, A.5
  • 15
    • 0029670081 scopus 로고    scopus 로고
    • Phospholipase C-γ interacts with conserved phosphotyrosyl residues in the linker region of Syk and is a substrate for Syk
    • Law, C.-L., K. A. Chandran, S. P. Sidorenko, and E. A. Clark. 1996. Phospholipase C-γ interacts with conserved phosphotyrosyl residues in the linker region of Syk and is a substrate for Syk. Mol. Cell. Biol. 16:1305.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 1305
    • Law, C.-L.1    Chandran, K.A.2    Sidorenko, S.P.3    Clark, E.A.4
  • 16
    • 0029671073 scopus 로고    scopus 로고
    • cbl is a major substrate of tyrosine phosphorylation upon B cell antigen receptor stimulation and interacts in vivo with Fyn and Syk tyrosine kinases, Grb2 and Shc adaptors, and the p85 subunit of phosphatidylinositol 3-kinase
    • cbl is a major substrate of tyrosine phosphorylation upon B cell antigen receptor stimulation and interacts in vivo with Fyn and Syk tyrosine kinases, Grb2 and Shc adaptors, and the p85 subunit of phosphatidylinositol 3-kinase. J. Biol. Chem. 271:3187.
    • (1996) J. Biol. Chem. , vol.271 , pp. 3187
    • Panchamoorthy, G.1    Fukazawa, T.2    Jiyake, S.3    Soltoff, S.4    Reedquist, K.5    Druker, B.6    Shoelson, S.7    Cantley, L.8    Band, H.9
  • 19
    • 0030889218 scopus 로고    scopus 로고
    • The product of the proto-oncogene c-cbl: A negative regulator of the Syk tyrosine kinase
    • Ota, Y., and L. E. Samelson. 1997. The product of the proto-oncogene c-cbl: a negative regulator of the Syk tyrosine kinase. Science 276:418.
    • (1997) Science , vol.276 , pp. 418
    • Ota, Y.1    Samelson, L.E.2
  • 21
    • 14444276991 scopus 로고    scopus 로고
    • The Cbl phosphotyrosine-binding domain selects a D(N/D)XpY motif and binds to the Tyr292 negative regulatory phosphorylation site of ZAP-70
    • Lupher, M. L., Jr., Z. Songyang, S. E. Shoelson, L. C. Cantley, and H. Band. 1997. The Cbl phosphotyrosine-binding domain selects a D(N/D)XpY motif and binds to the Tyr292 negative regulatory phosphorylation site of ZAP-70. J. Biol. Chem. 272:33140.
    • (1997) J. Biol. Chem. , vol.272 , pp. 33140
    • Lupher M.L., Jr.1    Songyang, Z.2    Shoelson, S.E.3    Cantley, L.C.4    Band, H.5
  • 23
    • 0029867911 scopus 로고    scopus 로고
    • Syk, activated by cross-linking the B-cell antigen receptor, localizes to the cytosol where it interacts with and phosphorylates α-tubulin on tyrosine
    • Peters, J. D., M. T. Furlong, D. J. Asai, M. L. Harrison, and R. L. Geahlen. 1996. Syk, activated by cross-linking the B-cell antigen receptor, localizes to the cytosol where it interacts with and phosphorylates α-tubulin on tyrosine. J. Biol. Chem. 271:4755.
    • (1996) J. Biol. Chem. , vol.271 , pp. 4755
    • Peters, J.D.1    Furlong, M.T.2    Asai, D.J.3    Harrison, M.L.4    Geahlen, R.L.5
  • 24
    • 0024456610 scopus 로고
    • IgH enhancer-mediated deregulation of N-myc gene expression in transgenic mice: Generation of lymphoid neoplasias that lack c-myc expression
    • Dildrop, R., A. Ma, K. Zimmerman, E. Hsu, A. Tesfaye, R. DePinho, and F. W. Alt. 1989. IgH enhancer-mediated deregulation of N-myc gene expression in transgenic mice: generation of lymphoid neoplasias that lack c-myc expression. EMBO J. 8:1121.
    • (1989) EMBO J. , vol.8 , pp. 1121
    • Dildrop, R.1    Ma, A.2    Zimmerman, K.3    Hsu, E.4    Tesfaye, A.5    DePinho, R.6    Alt, F.W.7
  • 25
    • 0025884056 scopus 로고
    • Efficient selection for high-expression transfectants with a novel eukaryotic vector
    • Niwa, H., K. Yamamura, and J. Miyazaki. 1991. Efficient selection for high-expression transfectants with a novel eukaryotic vector. Gene 108:193.
    • (1991) Gene , vol.108 , pp. 193
    • Niwa, H.1    Yamamura, K.2    Miyazaki, J.3
  • 26
    • 0025819499 scopus 로고
    • The sequences of the human and mouse c-cbl proto-oncogenes show v-cbl was generated by a large tuncation encompassing a proline-rich domain and a leucine zipper-like motif
    • Blake, T. J., M. Shapiro, H. C. Morse III, and W. Y. Langdon. 1991. The sequences of the human and mouse c-cbl proto-oncogenes show v-cbl was generated by a large tuncation encompassing a proline-rich domain and a leucine zipper-like motif. Oncogene 6:653.
    • (1991) Oncogene , vol.6 , pp. 653
    • Blake, T.J.1    Shapiro, M.2    Morse H.C. III3    Langdon, W.Y.4
  • 27
    • 0032103332 scopus 로고    scopus 로고
    • Ets transcription factors: Nuclear effectors of the ras-map-kinase signaling pathway
    • Wasylyk, B., J. Hagman, and A. Gutierrez-Hartmann. 1998. Ets transcription factors: nuclear effectors of the ras-map-kinase signaling pathway. Trends Biochem. Sci. 23:213.
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 213
    • Wasylyk, B.1    Hagman, J.2    Gutierrez-Hartmann, A.3
  • 28
    • 0027337880 scopus 로고
    • p72Syk tyrosine kinase is activated by oxidizing conditions that induce lymphocyte tyrosine phosphorylation and calcium signals
    • Schieven, G. L., J. M. Kirihara, D. Burg, R. L. Geahlen, and J. A. Ledbetter. 1993. p72Syk tyrosine kinase is activated by oxidizing conditions that induce lymphocyte tyrosine phosphorylation and calcium signals. J. Biol. Chem. 268: 16688.
    • (1993) J. Biol. Chem. , vol.268 , pp. 16688
    • Schieven, G.L.1    Kirihara, J.M.2    Burg, D.3    Geahlen, R.L.4    Ledbetter, J.A.5
  • 29
    • 0029968995 scopus 로고    scopus 로고
    • Enhancement of lymphocyte responsiveness by a gain-of-function mutation of ZAP-70
    • Zhao, Q., and A. Weiss. 1996. Enhancement of lymphocyte responsiveness by a gain-of-function mutation of ZAP-70. Mol. Cell. Biol 16:6765.
    • (1996) Mol. Cell. Biol , vol.16 , pp. 6765
    • Zhao, Q.1    Weiss, A.2
  • 30
    • 0028920694 scopus 로고
    • sli-1, a negative regulator of let-23-mediated signaling in C. elegans
    • Jongeward, G. D., T. R. Clandinin, and P. W. Sternberg. 1995. sli-1, a negative regulator of let-23-mediated signaling in C. elegans. Genetics 139:1553.
    • (1995) Genetics , vol.139 , pp. 1553
    • Jongeward, G.D.1    Clandinin, T.R.2    Sternberg, P.W.3
  • 31
    • 10144243337 scopus 로고    scopus 로고
    • A novel phosphotyrosine-binding domain in the N-terminal transforming region of Cbl interacts directly and selectively with ZAP-70 in T cells
    • Lupher, M. L., K. A. Reedquist, S. Miyake, W. Y. Langdon, and H. Band. 1996. A novel phosphotyrosine-binding domain in the N-terminal transforming region of Cbl interacts directly and selectively with ZAP-70 in T cells. J. Biol. Chem. 271:24063.
    • (1996) J. Biol. Chem. , vol.271 , pp. 24063
    • Lupher, M.L.1    Reedquist, K.A.2    Miyake, S.3    Langdon, W.Y.4    Band, H.5
  • 32
    • 0033555527 scopus 로고    scopus 로고
    • Phosphorylation- and activation-independent association of the tyrosine kinase Syk and the tyrosine kinase substrates Cbl and Vav with tubulin in B-cells
    • Fernandez, J. A., L. M. Keshvara, J. D. Peters, M. T. Furlong, M. L. Harrison, and R. L. Geahlen. 1999. Phosphorylation- and activation-independent association of the tyrosine kinase Syk and the tyrosine kinase substrates Cbl and Vav with tubulin in B-cells. J. Biol. Chem. 274:1401.
    • (1999) J. Biol. Chem. , vol.274 , pp. 1401
    • Fernandez, J.A.1    Keshvara, L.M.2    Peters, J.D.3    Furlong, M.T.4    Harrison, M.L.5    Geahlen, R.L.6


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