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Volumn 19, Issue 10, 1999, Pages 6652-6664

The oncogenic 70Z Cbl mutation blocks the phosphotyrosine binding domain-dependent negative regulation of ZAP-70 by c-Cbl in Jurkat T cells

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN TYROSINE KINASE;

EID: 0032873651     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.19.10.6652     Document Type: Article
Times cited : (25)

References (72)
  • 1
    • 12044256844 scopus 로고
    • Tumour induction by activated abl involves tyrosine phosphorylation of the product of the cbl oncogene
    • Andoniou, C. E., C. B. Thien, and W. Y. Langdon. 1994. Tumour induction by activated abl involves tyrosine phosphorylation of the product of the cbl oncogene. EMBO J. 13:4515-4523.
    • (1994) EMBO J. , vol.13 , pp. 4515-4523
    • Andoniou, C.E.1    Thien, C.B.2    Langdon, W.Y.3
  • 2
    • 0029912203 scopus 로고    scopus 로고
    • All ErbB receptors other than the epidermal growth factor receptor are endocytosis impaired
    • Baulida, J., M. H. Kraus, M. Alimandi, P. P. Di Fiore, and G. Carpenter. 1996. All ErbB receptors other than the epidermal growth factor receptor are endocytosis impaired. J. Biol. Chem. 271:5251-5257.
    • (1996) J. Biol. Chem. , vol.271 , pp. 5251-5257
    • Baulida, J.1    Kraus, M.H.2    Alimandi, M.3    Di Fiore, P.P.4    Carpenter, G.5
  • 3
    • 0025819499 scopus 로고
    • The sequences of the human and mouse c-cbl proto-oncogenes show v-cbl was generated by a large truncation encompassing a proline-rich domain and a leucine zipper-like motif
    • Blake, T. J., M. Shapiro, H. C. Morse, and W. Y. Langdon. 1991. The sequences of the human and mouse c-cbl proto-oncogenes show v-cbl was generated by a large truncation encompassing a proline-rich domain and a leucine zipper-like motif. Oncogene 6:653-657.
    • (1991) Oncogene , vol.6 , pp. 653-657
    • Blake, T.J.1    Shapiro, M.2    Morse, H.C.3    Langdon, W.Y.4
  • 4
    • 0032441479 scopus 로고    scopus 로고
    • Ubiquitin and the control of protein fate in the secretory and endocytic pathways
    • Bonifacino, J. S., and A. M. Weissman. 1998. Ubiquitin and the control of protein fate in the secretory and endocytic pathways. Annu. Rev. Cell Biol. 14:19-57.
    • (1998) Annu. Rev. Cell Biol. , vol.14 , pp. 19-57
    • Bonifacino, J.S.1    Weissman, A.M.2
  • 5
    • 0030872395 scopus 로고    scopus 로고
    • Phosphotyrosine binding domain-dependent upregulation of the platelet-derived growth factor receptor alpha signaling cascade by transforming mutants of Cbl: Implications for Cbl's function and oncogenicity
    • Bonita, D. P., S. Miyake, M. L. Lupher, Jr., W. Y. Langdon, and H. Band. 1997. Phosphotyrosine binding domain-dependent upregulation of the platelet-derived growth factor receptor alpha signaling cascade by transforming mutants of Cbl: implications for Cbl's function and oncogenicity. Mol. Cell. Biol. 17:4597-4610.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 4597-4610
    • Bonita, D.P.1    Miyake, S.2    Lupher M.L., Jr.3    Langdon, W.Y.4    Band, H.5
  • 6
    • 0032541404 scopus 로고    scopus 로고
    • Syk protein tyrosine kinase regulates Fc receptor gamma-chain-mediated transport to lysosomes
    • Bonnerot, C., V. Briken, V. Brachet, D. Lankar, S. Cassard, B. Jabri, and S. Amigorena. 1998. syk protein tyrosine kinase regulates Fc receptor gamma-chain-mediated transport to lysosomes. EMBO J. 17:4606-4616.
    • (1998) EMBO J. , vol.17 , pp. 4606-4616
    • Bonnerot, C.1    Briken, V.2    Brachet, V.3    Lankar, D.4    Cassard, S.5    Jabri, B.6    Amigorena, S.7
  • 7
    • 0029977716 scopus 로고    scopus 로고
    • The RING finger domain: A recent example of a sequence-structure family
    • Borden, K. L., and P. S. Freemont. 1996. The RING finger domain: a recent example of a sequence-structure family. Curr. Opin. Struct. Biol. 6:395-401.
    • (1996) Curr. Opin. Struct. Biol. , vol.6 , pp. 395-401
    • Borden, K.L.1    Freemont, P.S.2
  • 8
    • 0029071585 scopus 로고
    • Activation of ZAP-70 kinase activity by phosphorylation of tyrosine 493 is required for lymphocyte antigen receptor function
    • Chan, A. C., 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. 14:2499-2508.
    • (1995) EMBO J. , vol.14 , pp. 2499-2508
    • Chan, A.C.1    Dalton, M.2    Johnson, R.3    Kong, G.H.4    Wang, T.5    Thoma, R.6    Kurosaki, T.7
  • 10
    • 0029779003 scopus 로고    scopus 로고
    • Mutational analysis of Lck in CD45-negative T cells: Dominant role of tyrosine 394 phosphorylation in kinase activity
    • D'Oro, U., K. Sakaguchi, E. Appella, and J. D. Ashwell. 1996. Mutational analysis of Lck in CD45-negative T cells: dominant role of tyrosine 394 phosphorylation in kinase activity. Mol. Cell. Biol. 16:4996-5003.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 4996-5003
    • D'Oro, U.1    Sakaguchi, K.2    Appella, E.3    Ashwell, J.D.4
  • 11
    • 0031448209 scopus 로고    scopus 로고
    • Activation of the Lck tyrosine kinase targets cell surface T cell antigen receptors for lysosomal degradation
    • D'Oro, U., M. S. Vacchio, A. M. Weissman, and J. D. Ashwell. 1997. Activation of the Lck tyrosine kinase targets cell surface T cell antigen receptors for lysosomal degradation. Immunity 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
  • 12
    • 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. 273:8867-8874.
    • (1998) J. Biol. Chem. , vol.273 , pp. 8867-8874
    • Deckert, M.1    Elly, C.2    Altman, A.3    Liu, Y.C.4
  • 13
    • 0029662222 scopus 로고    scopus 로고
    • Regulation of the association of p120cbl with Grb2 in Jurkat T cells
    • Donovan, J. A., Y. Ota, W. Y. Langdon, and L. E. Samelson. 1996. Regulation of the association of p120cbl with Grb2 in Jurkat T cells. J. Biol. Chem. 271:26369-26374.
    • (1996) J. Biol. Chem. , vol.271 , pp. 26369-26374
    • Donovan, J.A.1    Ota, Y.2    Langdon, W.Y.3    Samelson, L.E.4
  • 14
    • 0028027169 scopus 로고
    • The protein product of the c-cbl protooncogene is the 120-kDa tyrosine-phosphorylated protein in Jurkat cells activated via the T cell antigen receptor
    • Donovan, J. A., R. L. Wange, W. Y. Langdon, and L. E. Samelson. 1994. The protein product of the c-cbl protooncogene is the 120-kDa tyrosine-phosphorylated protein in Jurkat cells activated via the T cell antigen receptor. J. Biol. Chem. 269:22921-22924.
    • (1994) J. Biol. Chem. , vol.269 , pp. 22921-22924
    • Donovan, J.A.1    Wange, R.L.2    Langdon, W.Y.3    Samelson, L.E.4
  • 15
    • 0032478805 scopus 로고    scopus 로고
    • Fyn, Yes, and Syk phosphorylation sites in c-Cbl map to the same tyrosine residues that become phosphorylated in activated T cells
    • Feshchenko, E. A., W. Y. Langdon, and A. Y. Tsygankov. 1998. Fyn, Yes, and Syk phosphorylation sites in c-Cbl map to the same tyrosine residues that become phosphorylated in activated T cells. J. Biol. Chem. 273:8323-8331.
    • (1998) J. Biol. Chem. , vol.273 , pp. 8323-8331
    • Feshchenko, E.A.1    Langdon, W.Y.2    Tsygankov, A.Y.3
  • 17
    • 0030944455 scopus 로고    scopus 로고
    • ErbB-2, the preferred heterodimerization partner of all ErbB receptors, is a mediator of lateral signaling
    • Graus-Porta, D., R. R. Beerli, J. M. Daly, and N. E. Hynes. 1997. ErbB-2, the preferred heterodimerization partner of all ErbB receptors, is a mediator of lateral signaling. EMBO J. 16:1647-1655.
    • (1997) EMBO J. , vol.16 , pp. 1647-1655
    • Graus-Porta, D.1    Beerli, R.R.2    Daly, J.M.3    Hynes, N.E.4
  • 18
    • 0030700220 scopus 로고    scopus 로고
    • Ubiquitin-dependent internalization and down-regulation of plasma membrane proteins
    • Hicke, L. 1999. Ubiquitin-dependent internalization and down-regulation of plasma membrane proteins. FASEB J. 11:1215-1226.
    • (1999) FASEB J. , vol.11 , pp. 1215-1226
    • Hicke, L.1
  • 19
    • 0030790509 scopus 로고    scopus 로고
    • D-Cbl, the drosophila homologue of the c-Cbl proto-oncogene, interacts with the Drosophila EGF receptor in vivo, despite lacking C-terminal adaptor binding sites
    • Hime, G. R., M. P. Dhungat, A. Ng, and D. D. Bowtell. 1997. D-Cbl, the Drosophila homologue of the c-Cbl proto-oncogene, interacts with the Drosophila EGF receptor in vivo, despite lacking C-terminal adaptor binding sites. Oncogene 14:2709-2719.
    • (1997) Oncogene , vol.14 , pp. 2709-2719
    • Hime, G.R.1    Dhungat, M.P.2    Ng, A.3    Bowtell, D.D.4
  • 20
    • 0028209548 scopus 로고
    • Sequential interactions of the TCR with two distinct cytoplasmic tyrosine kinases
    • Iwashima, M., B. A. Irving, N. S. van Oers, A. C. Chan, and A. Weiss. 1994. Sequential interactions of the TCR with two distinct cytoplasmic tyrosine kinases. Science 263:1136-1139.
    • (1994) Science , vol.263 , pp. 1136-1139
    • Iwashima, M.1    Irving, B.A.2    Van Oers, N.S.3    Chan, A.C.4    Weiss, A.5
  • 21
    • 0029006745 scopus 로고
    • Cloning and characterization of cbl-b: A SH3 binding protein with homology to the c-cbl proto-oncogene
    • Keane, M. M., O. M. Rivero-Lezcano, J. A. Mitchell, K. C. Robbins, and S. Lipkowitz. 1995. Cloning and characterization of cbl-b: a SH3 binding protein with homology to the c-cbl proto-oncogene. Oncogene 10:2367-2377.
    • (1995) Oncogene , vol.10 , pp. 2367-2377
    • Keane, M.M.1    Rivero-Lezcano, O.M.2    Mitchell, J.A.3    Robbins, K.C.4    Lipkowitz, S.5
  • 22
    • 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. 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. 161:5276-5283.
    • (1998) J. Immunol. , vol.161 , pp. 5276-5283
    • Keshvara, L.M.1    Isaacson, C.2    Yankee, T.M.3    Sarac, R.4    Harrison, M.L.5    Geahlen, R.L.6
  • 24
    • 0029783430 scopus 로고    scopus 로고
    • Distinct tyrosine phosphorylation sites in ZAP-70 mediate activation and negative regulation of antigen receptor function
    • Kong, G., M. Dalton, J. B. Wardenburg, D. Straus, T. Kurosaki, and A. C. Chan. 1996. Distinct tyrosine phosphorylation sites in ZAP-70 mediate activation and negative regulation of antigen receptor function. Mol. Cell. Biol. 16:5026-5035.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 5026-5035
    • Kong, G.1    Dalton, M.2    Wardenburg, J.B.3    Straus, D.4    Kurosaki, T.5    Chan, A.C.6
  • 27
    • 0029917264 scopus 로고    scopus 로고
    • Coupling of the c-Cbl protooncogene product to ErbB-1/ EGF-receptor but not to other ErbB proteins
    • Levkowitz, G., L. N. Klapper, E. Tzahar, A. Freywald, M. Sela, and Y. Yarden. 1996. Coupling of the c-Cbl protooncogene product to ErbB-1/ EGF-receptor but not to other ErbB proteins. Oncogene 12:1117-1125.
    • (1996) Oncogene , vol.12 , pp. 1117-1125
    • Levkowitz, G.1    Klapper, L.N.2    Tzahar, E.3    Freywald, A.4    Sela, M.5    Yarden, Y.6
  • 29
    • 0030614453 scopus 로고    scopus 로고
    • Ras-dependent, Ca2+-stimulated activation of nuclear factor of activated T cells by a constitutively active Cbl mutant in T cells
    • Liu, Y. C., C. Elly, W. Y. Langdon, and A. Altman. 1997. Ras-dependent, Ca2+-stimulated activation of nuclear factor of activated T cells by a constitutively active Cbl mutant in T cells. J. Biol. Chem. 272:168-173.
    • (1997) J. Biol. Chem. , vol.272 , pp. 168-173
    • Liu, Y.C.1    Elly, C.2    Langdon, W.Y.3    Altman, A.4
  • 30
    • 0032567438 scopus 로고    scopus 로고
    • Cbl-mediated negative regulation of the Syk tyrosine kinase. A critical role for Cbl phosphotyrosine-binding domain binding to Syk phosphotyrosine 323
    • Lupher, M. L., Jr., N. Rao, N. L. Lill, C. E. Andoniou, S. Miyake, E. A. Clark, B. Druker, and H. Band. 1998. Cbl-mediated negative regulation of the Syk tyrosine kinase. A critical role for Cbl phosphotyrosine-binding domain binding to Syk phosphotyrosine 323. J. Biol. Chem. 273:35273-35281.
    • (1998) J. Biol. Chem. , vol.273 , pp. 35273-35281
    • Lupher M.L., Jr.1    Rao, N.2    Lill, N.L.3    Andoniou, C.E.4    Miyake, S.5    Clark, E.A.6    Druker, B.7    Band, H.8
  • 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., Jr., 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. 271:24063-24068.
    • (1996) J. Biol. Chem. , vol.271 , pp. 24063-24068
    • Lupher M.L., Jr.1    Reedquist, K.A.2    Miyake, S.3    Langdon, W.Y.4    Band, H.5
  • 32
    • 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. 272:33140-33144.
    • (1997) J. Biol. Chem. , vol.272 , pp. 33140-33144
    • Lupher M.L., Jr.1    Songyang, Z.2    Shoelson, S.E.3    Cantley, L.C.4    Band, H.5
  • 33
    • 0031114123 scopus 로고    scopus 로고
    • Tyrosine and serine protein kinase activities associated with ligand-induced internalized TCR/CD3 complexes
    • Luton, F., V. Legendre, J. P. Gorvel, A. M. Schmitt-Verhulst, and C. Boyer. 1997. Tyrosine and serine protein kinase activities associated with ligand-induced internalized TCR/CD3 complexes. J. Immunol. 158:3140-3147.
    • (1997) J. Immunol. , vol.158 , pp. 3140-3147
    • Luton, F.1    Legendre, V.2    Gorvel, J.P.3    Schmitt-Verhulst, A.M.4    Boyer, C.5
  • 35
    • 0030978136 scopus 로고    scopus 로고
    • Interactions of Drosophila Cbl with epidermal growth factor receptors and role of Cbl in R7 photoreceptor cell development
    • Meisner, H., A. Daga, J. Buxton, B. Fernandez, A. Chawla, U. Banerjee, and M. P. Czech. 1997. Interactions of Drosophila Cbl with epidermal growth factor receptors and role of Cbl in R7 photoreceptor cell development. Mol. Cell. Biol. 17:2217-2225.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 2217-2225
    • Meisner, H.1    Daga, A.2    Buxton, J.3    Fernandez, B.4    Chawla, A.5    Banerjee, U.6    Czech, M.P.7
  • 36
    • 0033522219 scopus 로고    scopus 로고
    • Structure of the amino-terminal domain of Cbl completed to its binding site on ZAP-70 kinase
    • Meng, W., S. Sawasdikosol, S. J. Burakoff, and M. J. Eck. 1999. Structure of the amino-terminal domain of Cbl completed to its binding site on ZAP-70 kinase. Nature 398:84-90.
    • (1999) Nature , vol.398 , pp. 84-90
    • Meng, W.1    Sawasdikosol, S.2    Burakoff, S.J.3    Eck, M.J.4
  • 37
    • 0032493444 scopus 로고    scopus 로고
    • The tyrosine kinase regulator Cbl enhances the ubiquitination and degradation of the platelet-derived growth factor receptor alpha
    • Miyake, S., M. L. Lupher, Jr., B. Druker, and H. Band. 1998. The tyrosine kinase regulator Cbl enhances the ubiquitination and degradation of the platelet-derived growth factor receptor alpha. Proc. Natl. Acad. Sci. USA 95:7927-7932.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 7927-7932
    • Miyake, S.1    Lupher M.L., Jr.2    Druker, B.3    Band, H.4
  • 39
    • 0032438114 scopus 로고    scopus 로고
    • Altered thymic positive selection and intracellular signals in Cbl-deficient mice
    • Naramura, M., H. K. Kole, R.-J. Hu, and H. Gu. 1998. Altered thymic positive selection and intracellular signals in Cbl-deficient mice. Proc. Natl. Acad. Sci. USA 95:15547-15552.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 15547-15552
    • Naramura, M.1    Kole, H.K.2    Hu, R.-J.3    Gu, H.4
  • 40
    • 0030002817 scopus 로고    scopus 로고
    • Characterization of the roles of SH2 domain-containing proteins in T-lymphocyte activation by using dominant negative SH2 domains
    • Northrop, J. P., M. J. Pustelnik, A. T. Lu, and J. R. Grove. 1996. Characterization of the roles of SH2 domain-containing proteins in T-lymphocyte activation by using dominant negative SH2 domains. Mol. Cell. Biol. 16: 2255-2263.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 2255-2263
    • Northrop, J.P.1    Pustelnik, M.J.2    Lu, A.T.3    Grove, J.R.4
  • 41
    • 0032543778 scopus 로고    scopus 로고
    • Oncogenic forms of CW abrogate the anchorage requirement but not the growth factor requirement for proliferation
    • Ojaniemi, M., W. Y. Langdon, and K. Vuori. 1998. Oncogenic forms of CW abrogate the anchorage requirement but not the growth factor requirement for proliferation. Oncogene 16:3159-3167.
    • (1998) Oncogene , vol.16 , pp. 3159-3167
    • Ojaniemi, M.1    Langdon, W.Y.2    Vuori, K.3
  • 43
    • 0029852837 scopus 로고    scopus 로고
    • Characterization of Cbl tyrosine phosphorylation and a Cbl-Syk complex in RBL-2H3 cells
    • Ota, Y., L. O. Beitz, A. M. Scharenberg, J. A. Donovan, J. P. Kinet, and L. E. Samelson. 1996. Characterization of Cbl tyrosine phosphorylation and a Cbl-Syk complex in RBL-2H3 cells. J. Exp. Med. 184:1713-1723.
    • (1996) J. Exp. Med. , vol.184 , pp. 1713-1723
    • Ota, Y.1    Beitz, L.O.2    Scharenberg, A.M.3    Donovan, J.A.4    Kinet, J.P.5    Samelson, L.E.6
  • 44
    • 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 276:418-420.
    • (1997) Science , vol.276 , pp. 418-420
    • Ota, Y.1    Samelson, L.E.2
  • 46
    • 0028246501 scopus 로고
    • Association of Rap1a and Rap1b proteins with late endocytic/phagocytic compartments and Rap2a with the Golgi complex
    • Pizon, V., M. Desjardins, C. Bucci, R. G. Parton, and M. Zerial. 1994. Association of Rap1a and Rap1b proteins with late endocytic/phagocytic compartments and Rap2a with the Golgi complex. J. Cell Sci. 107:1661-1670.
    • (1994) J. Cell Sci. , vol.107 , pp. 1661-1670
    • Pizon, V.1    Desjardins, M.2    Bucci, C.3    Parton, R.G.4    Zerial, M.5
  • 48
    • 0030046923 scopus 로고    scopus 로고
    • Dominant-negative zeta-associated protein 70 inhibits T cell antigen receptor signaling
    • Qian, D., M. N. Mollenauer, and A. Weiss. 1996. Dominant-negative zeta-associated protein 70 inhibits T cell antigen receptor signaling. J. Exp. Med. 183:611-620.
    • (1996) J. Exp. Med. , vol.183 , pp. 611-620
    • Qian, D.1    Mollenauer, M.N.2    Weiss, A.3
  • 49
    • 0030973579 scopus 로고    scopus 로고
    • Transcription factors of the NFAT family: Regulation and function
    • Rao, A., C. Luo, and P. G. Hogan. 1997. Transcription factors of the NFAT family: regulation and function. Annu. Rev. Immunol. 15:707-747.
    • (1997) Annu. Rev. Immunol. , vol.15 , pp. 707-747
    • Rao, A.1    Luo, C.2    Hogan, P.G.3
  • 50
    • 0030712944 scopus 로고    scopus 로고
    • Cbl-mediated regulation of T cell receptor-induced AP1 activation. Implications for activation via the Ras signaling pathway
    • Rellahan, B. L., L. J. Graham, B. Stoica, K. E. DeBell, and E. Bonvini. 1997. Cbl-mediated regulation of T cell receptor-induced AP1 activation. Implications for activation via the Ras signaling pathway. J. Biol. Chem. 272: 30806-30811.
    • (1997) J. Biol. Chem. , vol.272 , pp. 30806-30811
    • Rellahan, B.L.1    Graham, L.J.2    Stoica, B.3    Debell, K.E.4    Bonvini, E.5
  • 51
    • 0027417482 scopus 로고
    • Stimulatory effects of the protein tyrosine phosphatase inhibitor, pervanadate, on T-cell activation events
    • Secrist, J. P., L. A. Burns, L. Karnitz, G. A. Koretzky, and R. T. Abraham. 1993. Stimulatory effects of the protein tyrosine phosphatase inhibitor, pervanadate, on T-cell activation events. J. Biol. Chem. 268:5886-5893.
    • (1993) J. Biol. Chem. , vol.268 , pp. 5886-5893
    • Secrist, J.P.1    Burns, L.A.2    Karnitz, L.3    Koretzky, G.A.4    Abraham, R.T.5
  • 52
    • 0030027394 scopus 로고    scopus 로고
    • Potential sites of PI-3 kinase function in the endocytic pathway revealed by the PI-3 kinase inhibitor, wortmannin
    • Shpetner, H., M. Joly, D. Hartley, and S. Corvera. 1996. Potential sites of PI-3 kinase function in the endocytic pathway revealed by the PI-3 kinase inhibitor, wortmannin. J. Cell Biol. 132:595-605.
    • (1996) J. Cell Biol. , vol.132 , pp. 595-605
    • Shpetner, H.1    Joly, M.2    Hartley, D.3    Corvera, S.4
  • 53
    • 0031394111 scopus 로고    scopus 로고
    • The Cbl family of signal transduction molecules
    • Smit, L., and J. Borst 1998. The Cbl family of signal transduction molecules. Crit. Rev. Oncogenesis 8:359-379.
    • (1998) Crit. Rev. Oncogenesis , vol.8 , pp. 359-379
    • Smit, L.1    Borst, J.2
  • 54
    • 0032494080 scopus 로고    scopus 로고
    • ZAP-70 tyrosine kinase is required for LFA-1-dependent T cell migration
    • Soede, R. D. M., V. M. Wijnands, I. Van Kouteren-Cobzaru, and E. Roos. 1998. ZAP-70 tyrosine kinase is required for LFA-1-dependent T cell migration. J. Cell Biol. 142:1371-1379.
    • (1998) J. Cell Biol. , vol.142 , pp. 1371-1379
    • Soede, R.D.M.1    Wijnands, V.M.2    Van Kouteren-Cobzaru, I.3    Roos, E.4
  • 56
    • 2142713199 scopus 로고    scopus 로고
    • Endocytosis and intracellular sorting of receptor tyrosine kinases
    • Sorkin, A. 1998. Endocytosis and intracellular sorting of receptor tyrosine kinases. Front. Biosci. 3:729-738.
    • (1998) Front. Biosci. , vol.3 , pp. 729-738
    • Sorkin, A.1
  • 57
    • 0027756895 scopus 로고
    • Controlling signal transduction with synthetic ligands
    • Spencer, D. M., T. J. Wandless, S. L. Schreiber, and G. R. Crabtree. 1993. Controlling signal transduction with synthetic ligands. Science 262:1019-1024.
    • (1993) Science , vol.262 , pp. 1019-1024
    • Spencer, D.M.1    Wandless, T.J.2    Schreiber, S.L.3    Crabtree, G.R.4
  • 58
    • 0028180858 scopus 로고
    • Tyrosine kinases Lyn and Syk regulate B cell receptor-coupled Ca2+ mobilization through distinct pathways
    • Takata, M., H. Sabe, A. Hata, T. Inazu, Y. Momma, 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.
    • (1994) EMBO J. , vol.13 , pp. 1341-1349
    • Takata, M.1    Sabe, H.2    Hata, A.3    Inazu, T.4    Momma, Y.5    Nukada, T.6    Yamamura, H.7    Kurosaki, T.8
  • 59
    • 0031011155 scopus 로고    scopus 로고
    • EGF receptor binding and transformation by v-Cbl is ablated by the introduction of a loss-of-function mutation from the Caenorhabditis elegans Sli-1 gene
    • Thien, C. B., and W. Y. Langdon. 1997. EGF receptor binding and transformation by v-Cbl is ablated by the introduction of a loss-of-function mutation from the Caenorhabditis elegans Sli-1 gene. Oncogene 14:2239-2249.
    • (1997) Oncogene , vol.14 , pp. 2239-2249
    • Thien, C.B.1    Langdon, W.Y.2
  • 60
    • 0031455765 scopus 로고    scopus 로고
    • Tyrosine kinase activity of the EGF receptor is enhanced by the expression of oncogenic 70Z-Cbl
    • Thien, C. B., and W. Y. Langdon. 1997. Tyrosine kinase activity of the EGF receptor is enhanced by the expression of oncogenic 70Z-Cbl. Oncogene 15:2909-2919.
    • (1997) Oncogene , vol.15 , pp. 2909-2919
    • Thien, C.B.1    Langdon, W.Y.2
  • 61
    • 0032053760 scopus 로고    scopus 로고
    • Analysis of antigen receptor signalling using mouse gene targeting
    • Tybulewicz, V. L. 1998. Analysis of antigen receptor signalling using mouse gene targeting. Curr. Opin. Cell Biol. 10:195-204.
    • (1998) Curr. Opin. Cell Biol. , vol.10 , pp. 195-204
    • Tybulewicz, V.L.1
  • 62
    • 0030935791 scopus 로고    scopus 로고
    • Antisense repression of proto-oncogene c-Cbl enhances activation of the JAK-STAT pathway but not the ras pathway in epidermal growth factor receptor signaling
    • Ueno, H., K. Sasaki, K. Miyagawa, H. Honda, K. Mitani, Y. Yazaki, and H. Hirai. 1997. Antisense repression of proto-oncogene c-Cbl enhances activation of the JAK-STAT pathway but not the ras pathway in epidermal growth factor receptor signaling. J. Biol. Chem. 272:8739-8743.
    • (1997) J. Biol. Chem. , vol.272 , pp. 8739-8743
    • Ueno, H.1    Sasaki, K.2    Miyagawa, K.3    Honda, H.4    Mitani, K.5    Yazaki, Y.6    Hirai, H.7
  • 63
    • 0033582458 scopus 로고    scopus 로고
    • Activation of NFAT and AP1 by oncogenic 70Z Cbl requires an intact PTB domain but not Crk(L) or p85 PI3K association
    • van Leeuwen, J. E. M., P. K. Paik, and L. E. Samelson. 1999. Activation of NFAT and AP1 by oncogenic 70Z Cbl requires an intact PTB domain but not Crk(L) or p85 PI3K association. J. Biol. Chem. 274:5153-5162.
    • (1999) J. Biol. Chem. , vol.274 , pp. 5153-5162
    • Van Leeuwen, J.E.M.1    Paik, P.K.2    Samelson, L.E.3
  • 64
  • 66
    • 0030058105 scopus 로고    scopus 로고
    • c-Cbl is transiently tyrosine-phosphorylated, ubiquitinated, and membrane-targeted following CSF-1 stimulation of macrophages
    • Wang, Y., Y. G. Yeung, W. Y. Langdon, and R. J. Stanley. 1996. c-Cbl is transiently tyrosine-phosphorylated, ubiquitinated, and membrane-targeted following CSF-1 stimulation of macrophages. J. Biol. Chem. 271:17-20.
    • (1996) J. Biol. Chem. , vol.271 , pp. 17-20
    • Wang, Y.1    Yeung, Y.G.2    Langdon, W.Y.3    Stanley, R.J.4
  • 67
    • 0032890156 scopus 로고    scopus 로고
    • CSF-1 stimulated multi-ubiquitination of the CSF-1 receptor and of Cbl follows their tyrosine phosphorylation and association with other signaling proteins
    • Wang, Y., Y. G. Yeung, and R. J. Stanley. 1999. CSF-1 stimulated multi-ubiquitination of the CSF-1 receptor and of Cbl follows their tyrosine phosphorylation and association with other signaling proteins. J. Cell. Biochem. 72:119-134.
    • (1999) J. Cell. Biochem. , vol.72 , pp. 119-134
    • Wang, Y.1    Yeung, Y.G.2    Stanley, R.J.3
  • 68
    • 0029151944 scopus 로고
    • Activating and inhibitory mutations in adjacent tyrosines in the kinase domain of ZAP-70
    • Wange, R. L., R. Guitian, N. Isakov, J. D. Watts, R. Aebersold, and L. E. Samelson. 1995. Activating and inhibitory mutations in adjacent tyrosines in the kinase domain of ZAP-70. J. Biol. Chem. 270:18730-18733.
    • (1995) J. Biol. Chem. , vol.270 , pp. 18730-18733
    • Wange, R.L.1    Guitian, R.2    Isakov, N.3    Watts, J.D.4    Aebersold, R.5    Samelson, L.E.6
  • 69
    • 0031912097 scopus 로고    scopus 로고
    • Genetic evidence for differential coupling of Syk family kinases to the T-cell receptor: Reconstitution studies in a ZAP-70-deficient Jurkat T-cell line
    • Williams, B. L., K. L. Schreiber, W. Zhang, R. L. Wange, L. E. Samelson, P. J. Leibson, and R. T. Abraham. 1998. Genetic evidence for differential coupling of Syk family kinases to the T-cell receptor: reconstitution studies in a ZAP-70-deficient Jurkat T-cell line. Mol. Cell. Biol. 18:1388-1399.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 1388-1399
    • Williams, B.L.1    Schreiber, K.L.2    Zhang, W.3    Wange, R.L.4    Samelson, L.E.5    Leibson, P.J.6    Abraham, R.T.7
  • 70
    • 0029124883 scopus 로고
    • Similarity of sli-1, a regulator of vulval development in C. elegans, to the mammalian proto-oncogene c-cbl
    • Yoon, C. H., J. Lee, G. D. Jongeward, and P. W. Sternberg. 1995. Similarity of sli-1, a regulator of vulval development in C. elegans, to the mammalian proto-oncogene c-cbl. Science 269:1102-1105.
    • (1995) Science , vol.269 , pp. 1102-1105
    • Yoon, C.H.1    Lee, J.2    Jongeward, G.D.3    Sternberg, P.W.4
  • 71
    • 0033582462 scopus 로고    scopus 로고
    • Dual regulation of T cell receptor-mediated signaling by oncogenic Cbl mutant 70z
    • Zhang, Z., C. Elly, A. Altman, and Y. C. Liu. 1999. Dual regulation of T cell receptor-mediated signaling by oncogenic Cbl mutant 70Z. J. Biol. Chem. 274:4883-4889.
    • (1999) J. Biol. Chem. , vol.274 , pp. 4883-4889
    • Zhang, Z.1    Elly, C.2    Altman, A.3    Liu, Y.C.4
  • 72
    • 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. 16:6765-6774.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 6765-6774
    • Zhao, Q.1    Weiss, A.2


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