메뉴 건너뛰기




Volumn 162, Issue 12, 1999, Pages 7133-7139

Perturbed regulation of ZAP-70 and sustained tyrosine phosphorylation of LAT and SLP-76 in c-CBL-deficient thymocytes

Author keywords

[No Author keywords available]

Indexed keywords

TYROSINE;

EID: 0033564933     PISSN: 00221767     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (87)

References (48)
  • 1
    • 0029874657 scopus 로고    scopus 로고
    • T cell antigen receptor signal transduction pathways
    • Cantrell, D. 1996. T cell antigen receptor signal transduction pathways. Annu. Rev. Immunol. 14:259.
    • (1996) Annu. Rev. Immunol. , vol.14 , pp. 259
    • Cantrell, D.1
  • 2
    • 0030250114 scopus 로고    scopus 로고
    • Complex complexes: Signaling at the TCR
    • Wange, R. L., and L. E. Samelson. 1996. Complex complexes: signaling at the TCR. Immunity 5:1.
    • (1996) Immunity , vol.5 , pp. 1
    • Wange, R.L.1    Samelson, L.E.2
  • 5
    • 0029866039 scopus 로고    scopus 로고
    • Lck regulates the tyrosine phosphorylation of the T cell receptor subunits and ZAP-70 in murine thymocytes
    • van Oers, N. S. C., N. Killeen, and A. Weiss. 1996. Lck regulates the tyrosine phosphorylation of the T cell receptor subunits and ZAP-70 in murine thymocytes. J. Exp. Med. 183:1053. .
    • (1996) J. Exp. Med. , vol.183 , pp. 1053
    • Van Oers, N.S.C.1    Killeen, N.2    Weiss, A.3
  • 7
    • 0030802186 scopus 로고    scopus 로고
    • A spontaneously arising mutation in the DLAARN motif of murine ZAP-70 abrogates kinase activity and arrests thymocyte development
    • Wiest, D. O., J. M. Ahse, T. K. Howcroft, H.-M. Lee, D. M. Kemper, I. Negishi, D. S. Singer, A. Singer, and R. Abe. 1997. A spontaneously arising mutation in the DLAARN motif of murine ZAP-70 abrogates kinase activity and arrests thymocyte development. Immunity 6:663.
    • (1997) Immunity , vol.6 , pp. 663
    • Wiest, D.O.1    Ahse, J.M.2    Howcroft, T.K.3    Lee, H.-M.4    Kemper, D.M.5    Negishi, I.6    Singer, D.S.7    Singer, A.8    Abe, R.9
  • 9
    • 0026483786 scopus 로고
    • ZAP-70: A 70-kDa protein-tyrosine kinase that associates with the TCRζ chain
    • Chan, A. C., M. Iwashima, C. W. Turck, and A. Weiss. 1992. ZAP-70: a 70-kDa protein-tyrosine kinase that associates with the TCRζ chain. Cell 71:649.
    • (1992) Cell , vol.71 , pp. 649
    • Chan, A.C.1    Iwashima, M.2    Turck, C.W.3    Weiss, A.4
  • 11
    • 0030906543 scopus 로고    scopus 로고
    • Regulation of Vav-SLP-76 binding by ZAP-70 and its relevance to TCRζ/CD3 induction of interleukin-2
    • Raab M., A. J. da Silva, P. R. Findell, and C. E. Rudd. 1997. Regulation of Vav-SLP-76 binding by ZAP-70 and its relevance to TCRζ/CD3 induction of interleukin-2. Immunity 6:155.
    • (1997) Immunity , vol.6 , pp. 155
    • Raab, M.1    Da Silva, A.J.2    Findell, P.R.3    Rudd, C.E.4
  • 12
    • 0032541062 scopus 로고    scopus 로고
    • Uncoupling of nonreceptor tyrosine kinases from PLC-γl in an SLP-76-deficient T cell
    • Yablonski, D., M. R. Kuhne, T. Kadlecek, and A. Weiss. 1998. Uncoupling of nonreceptor tyrosine kinases from PLC-γl in an SLP-76-deficient T cell. Science 281:413.
    • (1998) Science , vol.281 , pp. 413
    • Yablonski, D.1    Kuhne, M.R.2    Kadlecek, T.3    Weiss, A.4
  • 14
    • 0032563256 scopus 로고    scopus 로고
    • Impaired viability and profound block in thymocyte development in mice lacking the adaptor protein SLP-76
    • Pivniouk V., E. Tsitsikov, P. Swinton, G. Rathbun, F. W. Alt, and R. S. Geha. 1998. Impaired viability and profound block in thymocyte development in mice lacking the adaptor protein SLP-76. Cell 94:229.
    • (1998) Cell , vol.94 , pp. 229
    • Pivniouk, V.1    Tsitsikov, E.2    Swinton, P.3    Rathbun, G.4    Alt, F.W.5    Geha, R.S.6
  • 15
    • 0032498231 scopus 로고    scopus 로고
    • LAT: The ZAP-70 tyrosine kinase substrate that links T cell receptor to cellular activation
    • Zhang, W., J. Sloan-Lancaster, J. Kitchen, R. P. Trible, and L. E. Samelson. 1998. LAT: the ZAP-70 tyrosine kinase substrate that links T cell receptor to cellular activation. Cell 92:83.
    • (1998) Cell , vol.92 , pp. 83
    • Zhang, W.1    Sloan-Lancaster, J.2    Kitchen, J.3    Trible, R.P.4    Samelson, L.E.5
  • 16
    • 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. M. 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
    • (1995) EMBO J. , vol.14 , pp. 2499
    • Chan, A.C.1    Dalton, M.2    Johnson, R.3    Kong, G.M.4    Wang, T.5    Thoma, R.6    Kurosaki, T.7
  • 17
    • 0029151944 scopus 로고
    • Activating and inhibitory mutations in adjacent tyrosines in the kinase domain of ZAP-70
    • Wange, R. L., R. Gultian, 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.
    • (1995) J. Biol. Chem. , vol.270 , pp. 18730
    • Wange, R.L.1    Gultian, R.2    Isakov, N.3    Watts, J.D.4    Aebersold, R.5    Samelson, L.E.6
  • 18
    • 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.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 5026
    • Kong, G.1    Dalton, M.2    Wardenburg, J.B.3    Straus, D.4    Kurosaki, T.5    Chan, A.C.6
  • 19
    • 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
  • 20
    • 0032546910 scopus 로고    scopus 로고
    • T cell activation induced by novel gain-of-function mutants of Syk and ZAP-70
    • Zeitlmann, L., T. Knorr, M. Knoll, C. Romeo, P. Sirim, and W. Kolanus. 1998. T cell activation induced by novel gain-of-function mutants of Syk and ZAP-70. J. Biol. Chem. 273:15445.
    • (1998) J. Biol. Chem. , vol.273 , pp. 15445
    • Zeitlmann, L.1    Knorr, T.2    Knoll, M.3    Romeo, C.4    Sirim, P.5    Kolanus, W.6
  • 22
    • 10144243337 scopus 로고    scopus 로고
    • A novel PTB 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 PTB 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., Jr.1    Reedquist, K.A.2    Miyake, S.3    Langdon, W.Y.4    Band, H.5
  • 23
    • 14444276991 scopus 로고    scopus 로고
    • The Cbl phosphotyrosine-binding domain selects a D(N/D)XpY motif and binds to the TyrP292 negative regulatory phosphorylation site of ZAP-70
    • Lupher, M. L., 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 TyrP292 negative regulatory phosphorylation site of ZAP-70. J. Biol. Chem. 272:33140.
    • (1997) J. Biol. Chem. , vol.272 , pp. 33140
    • Lupher, M.L.1    Songyang, Z.2    Shoelson, S.E.3    Cantley, L.C.4    Band, H.5
  • 24
    • 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.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 15547
    • Naramura, M.1    Kole, H.K.2    Hu, R.-J.3    Gu, H.4
  • 25
    • 0033522219 scopus 로고    scopus 로고
    • Structure of the N-terminal domain of Cbl in complex with its binding site in ZAP-70
    • Meng, W., S. Sawasdikosol, S. J. Burakoff, and M. J. Eck. 1999. Structure of the N-terminal domain of Cbl in complex with its binding site in ZAP-70. Nature 398:84.
    • (1999) Nature , vol.398 , pp. 84
    • Meng, W.1    Sawasdikosol, S.2    Burakoff, S.J.3    Eck, M.J.4
  • 26
    • 0029124883 scopus 로고
    • Similarity of sli-1, a regulator of vulval development in C. elegans, to the mammalian protooncogene 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 protooncogene c-cbl. Science 269:1102.
    • (1995) Science , vol.269 , pp. 1102
    • Yoon, C.H.1    Lee, J.2    Jongeward, G.D.3    Sternberg, P.W.4
  • 27
    • 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
  • 29
    • 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.
    • (1997) J. Biol. Chem. , vol.272 , pp. 8739
    • Ueno, H.1    Sasaki, K.2    Miyagawa, K.3    Honda, H.4    Mitani, K.5    Yazaki, Y.6    Hirai, H.7
  • 30
    • 0028865896 scopus 로고
    • The protein product of the c-cbl oncogene rapidly complexes with the EGF receptor and is tyrosine phosphorylated following EGF stimulation
    • Bowtell, D. D. L., and W. Y. Langdon. 1995. The protein product of the c-cbl oncogene rapidly complexes with the EGF receptor and is tyrosine phosphorylated following EGF stimulation. Oncogene 11:1561.
    • (1995) Oncogene , vol.11 , pp. 1561
    • Bowtell, D.D.L.1    Langdon, W.Y.2
  • 32
    • 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 E. R. Stanley. 1996. c-cbl is transiently tyrosine-phosphorylated, ubiquitinated, and membrane-targeted following CSF-1 stimulation of macrophages. J. Biol. Chem. 271:17.
    • (1996) J. Biol. Chem. , vol.271 , pp. 17
    • Wang, Y.1    Yeung, Y.G.2    Langdon, W.Y.3    Stanley, E.R.4
  • 34
    • 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.
    • (1998) J. Biol. Chem. , vol.273 , pp. 8323
    • Feshchenko, E.A.1    Langdon, W.Y.2    Tsygankov, A.Y.3
  • 35
    • 0032493444 scopus 로고    scopus 로고
    • The tyrosine kinase regulator Cbl enhances the ubiquitination and degradation of the platelet-derived growth factor receptor α
    • 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 α. Proc. Natl. Acad. Sci. USA 95:7927.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 7927
    • Miyake, S.1    Lupher M.L., Jr.2    Druker, B.3    Band, H.4
  • 37
    • 0030812812 scopus 로고    scopus 로고
    • Maintenance of human T cell anergy: Blocking of IL-2 gene transcription by activated Rap1
    • Boussiotis, V. A., G. J. Freeman, A. Berezovskaya, D. L. Barber, and L. M. Nadler. 1997. Maintenance of human T cell anergy: blocking of IL-2 gene transcription by activated Rap1. Science 278:124.
    • (1997) Science , vol.278 , pp. 124
    • Boussiotis, V.A.1    Freeman, G.J.2    Berezovskaya, A.3    Barber, D.L.4    Nadler, L.M.5
  • 39
    • 0029034440 scopus 로고
    • Interactions of Cbl with Grb2 and phosphatidylinositol 3′-kinase in activated Jurkat cells
    • Meisner, H., B. R. Conway, D. Hartley, and M. P. Czech. 1995. Interactions of Cbl with Grb2 and phosphatidylinositol 3′-kinase in activated Jurkat cells. Mol. Cell. Biol. 15:3571.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 3571
    • Meisner, H.1    Conway, B.R.2    Hartley, D.3    Czech, M.P.4
  • 40
    • 0029117423 scopus 로고
    • Specific association of the β isoform of the p85 subunit of phosphatidylinositol-3 kinase with the proto-oncogene c-cbl
    • Hartley, D., H. Meisner, and S. Corvera. 1995. Specific association of the β isoform of the p85 subunit of phosphatidylinositol-3 kinase with the proto-oncogene c-cbl. J. Biol. Chem. 270:18260.
    • (1995) J. Biol. Chem. , vol.270 , pp. 18260
    • Hartley, D.1    Meisner, H.2    Corvera, S.3
  • 41
    • 0029671073 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.
    • (1995) J. Biol. Chem. , vol.271 , pp. 3187
    • Panchamoorthy, G.1    Fukazawa, T.2    Miyake, S.3    Soltoff, S.4    Reedquist, K.5    Druker, B.6    Shoelson, S.7    Cantley, L.8    Band, H.9
  • 43
    • 0029671427 scopus 로고    scopus 로고
    • cbl is a cytosolic adapter protein that associates with phosphoinositide 3-kinase in response to epidermal growth factor in PC12 and other cells
    • cbl is a cytosolic adapter protein that associates with phosphoinositide 3-kinase in response to epidermal growth factor in PC12 and other cells. J. Biol. Chem. 271:563.
    • (1996) J. Biol. Chem. , vol.271 , pp. 563
    • Soltoff, S.P.1    Cantley, L.C.2
  • 45
    • 0030612386 scopus 로고    scopus 로고
    • cbl BCR/abl-transformed hematopoietic cells mediates enhanced association with phosphatidylinositol 3-kinase
    • cbl BCR/abl-transformed hematopoietic cells mediates enhanced association with phosphatidylinositol 3-kinase. Oncogene 14:2217.
    • (1997) Oncogene , vol.14 , pp. 2217
    • Jain, S.K.1    Langdon, W.Y.2    Varticovski, L.3
  • 46
    • 0032479979 scopus 로고    scopus 로고
    • 1 integrin signaling pathway involving Src-family kinases, Cbl, and PI-3 kinase is required for macrophage spreading and migration
    • 1 integrin signaling pathway involving Src-family kinases, Cbl, and PI-3 kinase is required for macrophage spreading and migration. EMBO J. 17:4391.
    • (1998) EMBO J. , vol.17 , pp. 4391
    • Meng, F.1    Lowell, C.A.2
  • 47
    • 0032512821 scopus 로고    scopus 로고
    • A role for CAP, a novel, multifunctional Src homology 3 domain-containing protein in formation of actin stress fibers and focal adhesion
    • Ribon, V., R. Herrera, B. K. Kay, and A. R. Saltiel. 1998. A role for CAP, a novel, multifunctional Src homology 3 domain-containing protein in formation of actin stress fibers and focal adhesion. J. Biol. Chem. 273:4073.
    • (1998) J. Biol. Chem. , vol.273 , pp. 4073
    • Ribon, V.1    Herrera, R.2    Kay, B.K.3    Saltiel, A.R.4
  • 48
    • 0032543778 scopus 로고    scopus 로고
    • Oncogenic forms of Cbl abrogate the anchorage requirement but not the growth factor requirement for proliferation
    • Ojaniemi, M., W. Y. Langdon, and K. Vuori. 1998. Oncogenic forms of Cbl abrogate the anchorage requirement but not the growth factor requirement for proliferation. Oncogene 16:3159.
    • (1998) Oncogene , vol.16 , pp. 3159
    • Ojaniemi, M.1    Langdon, W.Y.2    Vuori, K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.