메뉴 건너뛰기




Volumn 7, Issue 8, 2007, Pages 599-609

Molecular mechanisms of CD4+ T-cell anergy

Author keywords

[No Author keywords available]

Indexed keywords

BINDING PROTEIN; CASITAS B LINEAGE LYMPHOMA B PROTEIN; CD3 ANTIGEN; CYCLOSPORIN A; CYTOKINE; DIACYLGLYCEROL; EARLY GROWTH RESPONSE FACTOR; GUANINE NUCLEOTIDE EXCHANGE FACTOR; IONOMYCIN; LAT PROTEIN; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 2; PROTEIN; PROTEIN GRAIL; RAS GUANYL RELEASING PROTEIN 1; SUPERANTIGEN; T LYMPHOCYTE RECEPTOR; TRANSCRIPTION FACTOR AP 1; TRANSCRIPTION FACTOR NFAT; UBIQUITIN; UBIQUITIN BINDING PROTEIN; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG;

EID: 34547222902     PISSN: 14741733     EISSN: None     Source Type: Journal    
DOI: 10.1038/nri2131     Document Type: Review
Times cited : (145)

References (105)
  • 1
    • 20444490383 scopus 로고    scopus 로고
    • Regulation of immunity by self-reactive T cells
    • Kronenberg, M. & Rudensky, A. Regulation of immunity by self-reactive T cells. Nature 435, 598-604 (2005).
    • (2005) Nature , vol.435 , pp. 598-604
    • Kronenberg, M.1    Rudensky, A.2
  • 2
    • 0036234468 scopus 로고    scopus 로고
    • Pathways of apoptosis in lymphocyte development, homeostasis, and disease
    • Rathmell, J. C. & Thompson, C. B. Pathways of apoptosis in lymphocyte development, homeostasis, and disease. Cell 109, S97-S107 (2002).
    • (2002) Cell , vol.109
    • Rathmell, J.C.1    Thompson, C.B.2
  • 4
    • 0023161666 scopus 로고
    • T-cell unresponsiveness in vivo and in vitro: Fine specificity of induction and molecular characterization of the unresponsive state
    • Jenkins, M. K., Pardoll, D. M., Mizuguchi, J., Quill, H. & Schwartz, R. H. T-cell unresponsiveness in vivo and in vitro: fine specificity of induction and molecular characterization of the unresponsive state. Immunol. Rev. 95, 113-135 (1987).
    • (1987) Immunol. Rev , vol.95 , pp. 113-135
    • Jenkins, M.K.1    Pardoll, D.M.2    Mizuguchi, J.3    Quill, H.4    Schwartz, R.H.5
  • 5
    • 0042389785 scopus 로고    scopus 로고
    • Schwartz, R. H. T cell anergy. Annu. Rev. Immunol. 21, 305-334 (2003). An outstanding in-depth review about the experiments used to originally identify and define both clonal T-cell anergy and adaptive tolerance.
    • Schwartz, R. H. T cell anergy. Annu. Rev. Immunol. 21, 305-334 (2003). An outstanding in-depth review about the experiments used to originally identify and define both clonal T-cell anergy and adaptive tolerance.
  • 6
    • 0023390431 scopus 로고
    • Molecular events in the induction of a nonresponsive state in interleukin 2-producing helper T-lymphocyte clones
    • Jenkins, M. K., Pardoll, D. M., Mizuguchi, J., Chused, T. M. & Schwartz, R. H. Molecular events in the induction of a nonresponsive state in interleukin 2-producing helper T-lymphocyte clones. Proc. Natl Acad. Sci. USA 84, 5409-5413 (1987).
    • (1987) Proc. Natl Acad. Sci. USA , vol.84 , pp. 5409-5413
    • Jenkins, M.K.1    Pardoll, D.M.2    Mizuguchi, J.3    Chused, T.M.4    Schwartz, R.H.5
  • 7
    • 0023266396 scopus 로고
    • Stimulation of normal inducer T cell clones with antigen presented by purified Ia molecules in planar lipid membranes: Specific induction of a long-lived state of proliferative nonresponsiveness
    • Quill, H. & Schwartz, R. H. Stimulation of normal inducer T cell clones with antigen presented by purified Ia molecules in planar lipid membranes: specific induction of a long-lived state of proliferative nonresponsiveness. J. Immunol. 138, 3704-3712 (1987).
    • (1987) J. Immunol , vol.138 , pp. 3704-3712
    • Quill, H.1    Schwartz, R.H.2
  • 8
    • 0025058266 scopus 로고
    • Inhibition of antigen-specific proliferation of type 1 murine T cell clones after stimulation with immobilized anti-CD3 monoclonal antibody
    • Jenkins, M. K., Chen, C. A., Jung, G., Mueller, D. L. & Schwartz, R. H. Inhibition of antigen-specific proliferation of type 1 murine T cell clones after stimulation with immobilized anti-CD3 monoclonal antibody. J. Immunol. 144, 16-22 (1990).
    • (1990) J. Immunol , vol.144 , pp. 16-22
    • Jenkins, M.K.1    Chen, C.A.2    Jung, G.3    Mueller, D.L.4    Schwartz, R.H.5
  • 9
    • 0031111910 scopus 로고    scopus 로고
    • Dissociation of T cell anergy from apoptosis by blockade of Fas/Apo-1 (CD95) signaling
    • Hargreaves, R. G. et al. Dissociation of T cell anergy from apoptosis by blockade of Fas/Apo-1 (CD95) signaling. J. Immunol. 158, 3099-3107 (1997).
    • (1997) J. Immunol , vol.158 , pp. 3099-3107
    • Hargreaves, R.G.1
  • 10
    • 0026687519 scopus 로고
    • Reversal of in vitro T cell clonal anergy by IL-2 stimulation
    • Beverly, B., Kang, S. M., Lenardo, M. J. & Schwartz, R. H. Reversal of in vitro T cell clonal anergy by IL-2 stimulation. Int. Immunol. 4, 661-671 (1992).
    • (1992) Int. Immunol , vol.4 , pp. 661-671
    • Beverly, B.1    Kang, S.M.2    Lenardo, M.J.3    Schwartz, R.H.4
  • 11
    • 0026667860 scopus 로고
    • Transactivation by AP-1 is a molecular target of T cell clonal anergy
    • Kang, S. M. et al. Transactivation by AP-1 is a molecular target of T cell clonal anergy. Science 257, 1134-1138 (1992).
    • (1992) Science , vol.257 , pp. 1134-1138
    • Kang, S.M.1
  • 14
    • 0029952223 scopus 로고    scopus 로고
    • Anergic T cells are defective in both jun NH2-terminal kinase and mitogen-activated protein kinase signaling pathways
    • DeSilva, D. R., Feeser, W. S., Tancula, E. J. & Scherle, P. A. Anergic T cells are defective in both jun NH2-terminal kinase and mitogen-activated protein kinase signaling pathways. J. Exp. Med. 183, 2017-2023 (1996).
    • (1996) J. Exp. Med , vol.183 , pp. 2017-2023
    • DeSilva, D.R.1    Feeser, W.S.2    Tancula, E.J.3    Scherle, P.A.4
  • 15
    • 0030949834 scopus 로고    scopus 로고
    • Expression of NFAT-family proteins in normal human T cells
    • Lyakh, L., Ghosh, P. & Rice, N. R. Expression of NFAT-family proteins in normal human T cells. Mol. Cell. Biol. 17, 2475-2484 (1997).
    • (1997) Mol. Cell. Biol , vol.17 , pp. 2475-2484
    • Lyakh, L.1    Ghosh, P.2    Rice, N.R.3
  • 17
    • 0031882452 scopus 로고    scopus 로고
    • Differences between responses of naive and activated T cells to anergy induction
    • Hayashi, R. J., Loh, D. Y., Kanagawa, O. & Wang, F. Differences between responses of naive and activated T cells to anergy induction. J. Immunol. 160, 33-38 (1998).
    • (1998) J. Immunol , vol.160 , pp. 33-38
    • Hayashi, R.J.1    Loh, D.Y.2    Kanagawa, O.3    Wang, F.4
  • 18
    • 0028291525 scopus 로고
    • JNK is involved in signal integration during costimulation of T lymphocytes
    • Su, B. et al. JNK is involved in signal integration during costimulation of T lymphocytes. Cell 77, 727-736 (1994).
    • (1994) Cell , vol.77 , pp. 727-736
    • Su, B.1
  • 19
    • 0033082519 scopus 로고    scopus 로고
    • Evidence for repression of IL-2 gene activation in anergic T cells
    • Telander, D. G., Malvey, E. N. & Mueller, D. L. Evidence for repression of IL-2 gene activation in anergic T cells. J. Immunol. 162, 1460-1465 (1999).
    • (1999) J. Immunol , vol.162 , pp. 1460-1465
    • Telander, D.G.1    Malvey, E.N.2    Mueller, D.L.3
  • 20
    • 0024381358 scopus 로고
    • A nondeletional mechanism of thymic self tolerance
    • Ramsdell, F., Lantz, T. & Fowlkes, B. J. A nondeletional mechanism of thymic self tolerance. Science 246, 1038-1041 (1989).
    • (1989) Science , vol.246 , pp. 1038-1041
    • Ramsdell, F.1    Lantz, T.2    Fowlkes, B.J.3
  • 22
    • 0025096424 scopus 로고
    • + T cells in Staphylococcus enterotoxin B-primed mice
    • + T cells in Staphylococcus enterotoxin B-primed mice. J. Exp. Med. 172, 1065-1070 (1990).
    • (1990) J. Exp. Med , vol.172 , pp. 1065-1070
    • Kawabe, Y.1    Ochi, A.2
  • 25
    • 0027532184 scopus 로고
    • Clonal anergy blocks in vivo growth of mature T cells and can be reversed in the absence of antigen
    • Rocha, B., Tanchot, C. & Von Boehmer, H. Clonal anergy blocks in vivo growth of mature T cells and can be reversed in the absence of antigen. J. Exp. Med. 177, 1517-1521 (1993).
    • (1993) J. Exp. Med , vol.177 , pp. 1517-1521
    • Rocha, B.1    Tanchot, C.2    Von Boehmer, H.3
  • 26
    • 0028957496 scopus 로고
    • Anergy and exhaustion are independent mechanisms of peripheral T cell tolerance
    • Rocha, B., Grandien, A. & Freitas, A. A. Anergy and exhaustion are independent mechanisms of peripheral T cell tolerance. J. Exp. Med. 181, 993-1003 (1995).
    • (1995) J. Exp. Med , vol.181 , pp. 993-1003
    • Rocha, B.1    Grandien, A.2    Freitas, A.A.3
  • 27
    • 0034653393 scopus 로고    scopus 로고
    • Induction of T cell anergy in the absence of CTLA-4/B7 interaction
    • Frauwirth, K. A., Alegre, M. L. & Thompson, C. B. Induction of T cell anergy in the absence of CTLA-4/B7 interaction. J. Immunol. 164, 2987-2993 (2000).
    • (2000) J. Immunol , vol.164 , pp. 2987-2993
    • Frauwirth, K.A.1    Alegre, M.L.2    Thompson, C.B.3
  • 28
    • 0030966217 scopus 로고    scopus 로고
    • Induction of peripheral T cell tolerance in vivo requires CTLA-4 engagement
    • Perez, V. L. et al. Induction of peripheral T cell tolerance in vivo requires CTLA-4 engagement. Immunity 6, 411-417 (1997).
    • (1997) Immunity , vol.6 , pp. 411-417
    • Perez, V.L.1
  • 30
    • 0026708592 scopus 로고
    • Role of protein kinase C in T-cell antigen receptor regulation of p21ras: Evidence that two p21ras regulatory pathways coexist in T cells
    • Izquierdo, M., Downward, J., Graves, J. D. & Cantrell, D. A. Role of protein kinase C in T-cell antigen receptor regulation of p21ras: evidence that two p21ras regulatory pathways coexist in T cells. Mol. Cell. Biol. 12, 3305-3312 (1992).
    • (1992) Mol. Cell. Biol , vol.12 , pp. 3305-3312
    • Izquierdo, M.1    Downward, J.2    Graves, J.D.3    Cantrell, D.A.4
  • 32
    • 0032524389 scopus 로고    scopus 로고
    • RasGRP, a Ras guanyl nucleotide-releasing protein with calcium-and diacylglycerol-binding motifs
    • Ebinu, J. O. et al. RasGRP, a Ras guanyl nucleotide-releasing protein with calcium-and diacylglycerol-binding motifs. Science 280, 1082-1086 (1998).
    • (1998) Science , vol.280 , pp. 1082-1086
    • Ebinu, J.O.1
  • 33
    • 0041488671 scopus 로고    scopus 로고
    • Phospholipase C? activates Ras on the Golgi apparatus by means of RasGRP1
    • Bivona, T. G. et al. Phospholipase C? activates Ras on the Golgi apparatus by means of RasGRP1. Nature 424, 694-698 (2003).
    • (2003) Nature , vol.424 , pp. 694-698
    • Bivona, T.G.1
  • 34
    • 0034658333 scopus 로고    scopus 로고
    • RasGRP links T-cell receptor signaling to Ras
    • Ebinu, J. O. et al. RasGRP links T-cell receptor signaling to Ras. Blood 95, 3199-3203 (2000).
    • (2000) Blood , vol.95 , pp. 3199-3203
    • Ebinu, J.O.1
  • 35
    • 0034303371 scopus 로고    scopus 로고
    • RasGRP is essential for mouse thymocyte differentiation and TCR signaling
    • Dower, N. A. et al. RasGRP is essential for mouse thymocyte differentiation and TCR signaling. Nature Immunol. 1, 317-321 (2000).
    • (2000) Nature Immunol , vol.1 , pp. 317-321
    • Dower, N.A.1
  • 36
    • 33750094147 scopus 로고    scopus 로고
    • Disruption of diacylglycerol metabolism impairs the induction of T cell anergy
    • Olenchock, B. A. et al. Disruption of diacylglycerol metabolism impairs the induction of T cell anergy. Nature Immunol. 7, 1174-1181 (2006).
    • (2006) Nature Immunol , vol.7 , pp. 1174-1181
    • Olenchock, B.A.1
  • 37
    • 33750093594 scopus 로고    scopus 로고
    • Zha, Y. et al. T cell anergy is reversed by active Ras and is regulated by diacylglycerol kinase-α. Nature Immunol. 7, 1166-1173 (2006). References 36 and 37 describe the identification of attenuated DAG signalling due to its conversion to phosphatidic acid in multiple model systems of T-cell anergy.
    • Zha, Y. et al. T cell anergy is reversed by active Ras and is regulated by diacylglycerol kinase-α. Nature Immunol. 7, 1166-1173 (2006). References 36 and 37 describe the identification of attenuated DAG signalling due to its conversion to phosphatidic acid in multiple model systems of T-cell anergy.
  • 38
    • 0037163130 scopus 로고    scopus 로고
    • Regulation of T cell receptor-induced activation of the Ras-ERK pathway by diacylglycerol kinase ζ
    • Zhong, X. P. et al. Regulation of T cell receptor-induced activation of the Ras-ERK pathway by diacylglycerol kinase ζ. J. Biol. Chem. 277, 31089-31098 (2002).
    • (2002) J. Biol. Chem , vol.277 , pp. 31089-31098
    • Zhong, X.P.1
  • 39
    • 0042383362 scopus 로고    scopus 로고
    • Enhanced T cell responses due to diacylglycerol kinase ζ deficiency
    • Zhong, X. P. et al. Enhanced T cell responses due to diacylglycerol kinase ζ deficiency. Nature Immunol. 4, 882-890 (2003).
    • (2003) Nature Immunol , vol.4 , pp. 882-890
    • Zhong, X.P.1
  • 40
    • 0037077135 scopus 로고    scopus 로고
    • Macian, F. et al. Transcriptional mechanisms underlying lymphocyte tolerance. Cell 109, 719-731 (2002). This paper shows that the presence of NFAT in the nucleus, in the absence of the AP1 heterodimer, imparts an anergic gene-expression profile that is distinct from that seen during full T-cell activation.
    • Macian, F. et al. Transcriptional mechanisms underlying lymphocyte tolerance. Cell 109, 719-731 (2002). This paper shows that the presence of NFAT in the nucleus, in the absence of the AP1 heterodimer, imparts an anergic gene-expression profile that is distinct from that seen during full T-cell activation.
  • 41
    • 0036708385 scopus 로고    scopus 로고
    • 2+ signals without interfering with the induction of clonal anergy
    • 2+ signals without interfering with the induction of clonal anergy. Eur. J. Immunol. 32, 2500-2509 (2002).
    • (2002) Eur. J. Immunol , vol.32 , pp. 2500-2509
    • Crespi, D.1
  • 42
    • 0036888651 scopus 로고    scopus 로고
    • Regulation of life and death by the zinc finger transcription factor Egr-1
    • Thiel, G. & Cibelli, G. Regulation of life and death by the zinc finger transcription factor Egr-1. J. Cell. Physiol. 193, 287-292 (2002).
    • (2002) J. Cell. Physiol , vol.193 , pp. 287-292
    • Thiel, G.1    Cibelli, G.2
  • 43
    • 10344239897 scopus 로고    scopus 로고
    • + T cells
    • + T cells. J. Immunol. 173, 7331-7338 (2004).
    • (2004) J. Immunol , vol.173 , pp. 7331-7338
    • Harris, J.E.1
  • 44
    • 18244375249 scopus 로고    scopus 로고
    • Safford, M. et al. Egr-2 and Egr-3 are negative regulators of T cell activation. Nature Immunol. 6, 472-480 (2005). This paper shows that EGR2 and EGR3 expression is associated with T-cell anergy and also contributes to T-cell anergy induction by upregulating the expression of CBL-B.
    • Safford, M. et al. Egr-2 and Egr-3 are negative regulators of T cell activation. Nature Immunol. 6, 472-480 (2005). This paper shows that EGR2 and EGR3 expression is associated with T-cell anergy and also contributes to T-cell anergy induction by upregulating the expression of CBL-B.
  • 45
    • 27644439861 scopus 로고    scopus 로고
    • Examining multiprotein signaling complexes from all angles
    • Houtman, J. C., Barda-Saad, M. & Samelson, L. E. Examining multiprotein signaling complexes from all angles. FEBS J. 272, 5426-5435 (2005).
    • (2005) FEBS J , vol.272 , pp. 5426-5435
    • Houtman, J.C.1    Barda-Saad, M.2    Samelson, L.E.3
  • 46
    • 33646568738 scopus 로고    scopus 로고
    • Hundt, M. et al. Impaired activation and localization of LAT in anergic T cells as a consequence of a selective palmitoylation defect. Immunity 24, 513-522 (2006). This study shows attenuated LAT signalling due to altered palmitoylation and membrane relocalization in multiple systems of T-cell anergy.
    • Hundt, M. et al. Impaired activation and localization of LAT in anergic T cells as a consequence of a selective palmitoylation defect. Immunity 24, 513-522 (2006). This study shows attenuated LAT signalling due to altered palmitoylation and membrane relocalization in multiple systems of T-cell anergy.
  • 47
    • 2442437350 scopus 로고
    • Isolation of a polypeptide that has lymphocyte-differentiating properties and is probably represented universally in living cells
    • Goldstein, G. et al. Isolation of a polypeptide that has lymphocyte-differentiating properties and is probably represented universally in living cells. Proc. Natl Acad. Sci. USA 72, 11-15 (1975).
    • (1975) Proc. Natl Acad. Sci. USA , vol.72 , pp. 11-15
    • Goldstein, G.1
  • 48
    • 0019174693 scopus 로고
    • Ubiquitin is the ATP-dependent proteolysis factor I of rabbit reticulocytes
    • Wilkinson, K. D., Urban, M. K. & Haas, A. L. Ubiquitin is the ATP-dependent proteolysis factor I of rabbit reticulocytes. J. Biol. Chem. 255, 7529-7532 (1980).
    • (1980) J. Biol. Chem , vol.255 , pp. 7529-7532
    • Wilkinson, K.D.1    Urban, M.K.2    Haas, A.L.3
  • 49
    • 8844237615 scopus 로고    scopus 로고
    • Polyubiquitin chains: Polymeric protein signals
    • Pickart, C. M. & Fushman, D. Polyubiquitin chains: polymeric protein signals. Curr. Opin. Chem. Biol. 8, 610-616 (2004).
    • (2004) Curr. Opin. Chem. Biol , vol.8 , pp. 610-616
    • Pickart, C.M.1    Fushman, D.2
  • 50
    • 20444476625 scopus 로고    scopus 로고
    • SLIM is a nuclear ubiquitin E3 ligase that negatively regulates STAT signaling
    • Tanaka, T., Soriano, M. A. & Grusby, M. J. SLIM is a nuclear ubiquitin E3 ligase that negatively regulates STAT signaling. Immunity 22, 729-736 (2005).
    • (2005) Immunity , vol.22 , pp. 729-736
    • Tanaka, T.1    Soriano, M.A.2    Grusby, M.J.3
  • 51
    • 13444292166 scopus 로고    scopus 로고
    • Deltex regulates T-cell activation by targeted degradation of active MEKK1
    • Liu, W. H. & Lai, M. Z. Deltex regulates T-cell activation by targeted degradation of active MEKK1. Mol. Cell. Biol. 25, 1367-1378 (2005).
    • (2005) Mol. Cell. Biol , vol.25 , pp. 1367-1378
    • Liu, W.H.1    Lai, M.Z.2
  • 52
    • 20944434221 scopus 로고    scopus 로고
    • A novel E3 ubiquitin ligase TRAC-1 positively regulates T cell activation
    • Zhao, H. et al. A novel E3 ubiquitin ligase TRAC-1 positively regulates T cell activation. J. Immunol. 174, 5288-5297 (2005).
    • (2005) J. Immunol , vol.174 , pp. 5288-5297
    • Zhao, H.1
  • 53
    • 21144438325 scopus 로고    scopus 로고
    • A RING-type ubiquitin ligase family member required to repress follicular helper T cells and autoimmunity
    • Vinuesa, C. G. et al. A RING-type ubiquitin ligase family member required to repress follicular helper T cells and autoimmunity. Nature 435, 452-458 (2005).
    • (2005) Nature , vol.435 , pp. 452-458
    • Vinuesa, C.G.1
  • 54
    • 12144290293 scopus 로고    scopus 로고
    • Calcineurin imposes T cell unresponsiveness through targeted proteolysis of signaling proteins
    • Heissmeyer, V. et al. Calcineurin imposes T cell unresponsiveness through targeted proteolysis of signaling proteins. Nature Immunol. 5, 255-265 (2004).
    • (2004) Nature Immunol , vol.5 , pp. 255-265
    • Heissmeyer, V.1
  • 55
    • 0037396674 scopus 로고    scopus 로고
    • + T cells. Immunity 18, 535-547 (2003). References 54, 55 and 69 describe for the first time the role of the E3 ubiquitin ligases CBL-B, GRAIL and ITCH in the induction of T-cell anergy.
    • + T cells. Immunity 18, 535-547 (2003). References 54, 55 and 69 describe for the first time the role of the E3 ubiquitin ligases CBL-B, GRAIL and ITCH in the induction of T-cell anergy.
  • 56
    • 4644285392 scopus 로고    scopus 로고
    • E3 ubiquitin ligases as T cell anergy factors
    • Mueller, D. L. E3 ubiquitin ligases as T cell anergy factors. Nature Immunol. 5, 883-890 (2004).
    • (2004) Nature Immunol , vol.5 , pp. 883-890
    • Mueller, D.L.1
  • 57
    • 0029006745 scopus 로고
    • Cloning and characterization of Cbl-b: A SH3 binding protein with homology to the c-Cbl proto-oncogene
    • Keane, M. M., Rivero-Lezcano, O. M., Mitchell, J. A., Robbins, K. C. & Lipkowitz, S. Cloning and characterization of Cbl-b: a SH3 binding protein with homology to the c-Cbl proto-oncogene. Oncogene 10, 2367-2377 (1995).
    • (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
  • 58
    • 0033521883 scopus 로고    scopus 로고
    • Tyrosine phosphorylation and complex formation of Cbl-b upon T cell receptor stimulation
    • Elly, C. et al. Tyrosine phosphorylation and complex formation of Cbl-b upon T cell receptor stimulation. Oncogene 18, 1147-1156 (1999).
    • (1999) Oncogene , vol.18 , pp. 1147-1156
    • Elly, C.1
  • 59
    • 0034642499 scopus 로고    scopus 로고
    • Negative regulation of lymphocyte activation and autoimmunity by the molecular adaptor Cbl-b
    • Bachmaier, K. et al. Negative regulation of lymphocyte activation and autoimmunity by the molecular adaptor Cbl-b. Nature 403, 211-216 (2000).
    • (2000) Nature , vol.403 , pp. 211-216
    • Bachmaier, K.1
  • 60
    • 0034642534 scopus 로고    scopus 로고
    • Cbl-b regulates the CD28 dependence of T-cell activation
    • Chiang, Y. J. et al. Cbl-b regulates the CD28 dependence of T-cell activation. Nature 403, 216-220 (2000).
    • (2000) Nature , vol.403 , pp. 216-220
    • Chiang, Y.J.1
  • 61
    • 10344259631 scopus 로고    scopus 로고
    • Cutting edge: Cbl-b: one of the key molecules tuning CD28- and CTLA-4-mediated T cell costimulation
    • Li, D. et al. Cutting edge: Cbl-b: one of the key molecules tuning CD28- and CTLA-4-mediated T cell costimulation. J. Immunol. 173, 7135-7139 (2004).
    • (2004) J. Immunol , vol.173 , pp. 7135-7139
    • Li, D.1
  • 62
    • 0036721780 scopus 로고    scopus 로고
    • Cutting edge: Regulation of T cell activation threshold by CD28 costimulation through targeting Cbl-b for ubiquitination
    • Zhang, J. et al. Cutting edge: regulation of T cell activation threshold by CD28 costimulation through targeting Cbl-b for ubiquitination. J. Immunol. 169, 2236-2240 (2002).
    • (2002) J. Immunol , vol.169 , pp. 2236-2240
    • Zhang, J.1
  • 63
    • 0030713407 scopus 로고    scopus 로고
    • Cbl-b, a member of the Sli-1/c-Cbl protein family, inhibits Vav-mediated c-Jun N-terminal kinase activation
    • Bustelo, X. R., Crespo, P., Lopez-Barahona, M., Gutkind, J. S. & Barbacid, M. Cbl-b, a member of the Sli-1/c-Cbl protein family, inhibits Vav-mediated c-Jun N-terminal kinase activation. Oncogene 15, 2511-2520 (1997).
    • (1997) Oncogene , vol.15 , pp. 2511-2520
    • Bustelo, X.R.1    Crespo, P.2    Lopez-Barahona, M.3    Gutkind, J.S.4    Barbacid, M.5
  • 64
    • 0033680925 scopus 로고    scopus 로고
    • Cbl-b is a negative regulator of receptor clustering and raft aggregation in T cells
    • Krawczyk, C. et al. Cbl-b is a negative regulator of receptor clustering and raft aggregation in T cells. Immunity 13, 463-473 (2000).
    • (2000) Immunity , vol.13 , pp. 463-473
    • Krawczyk, C.1
  • 65
    • 0033613826 scopus 로고    scopus 로고
    • T lymphocyte costimulation mediated by reorganization of membrane microdomains
    • Viola, A., Schroeder, S., Sakakibara, Y. & Lanzavecchia, A. T lymphocyte costimulation mediated by reorganization of membrane microdomains. Science 283, 680-682 (1999).
    • (1999) Science , vol.283 , pp. 680-682
    • Viola, A.1    Schroeder, S.2    Sakakibara, Y.3    Lanzavecchia, A.4
  • 66
    • 0035555195 scopus 로고    scopus 로고
    • Proteolysis-independent regulation of PI3K by Cbl-b-mediated ubiquitination in T cells
    • Fang, D. & Liu, Y. C. Proteolysis-independent regulation of PI3K by Cbl-b-mediated ubiquitination in T cells. Nature Immunol. 2, 870-875 (2001).
    • (2001) Nature Immunol , vol.2 , pp. 870-875
    • Fang, D.1    Liu, Y.C.2
  • 67
    • 0035895959 scopus 로고    scopus 로고
    • Cbl-b, a RING-type E3 ubiquitin ligase, targets phosphatidylinositol 3-kinase for ubiquitination in T cells
    • Fang, D. et al. Cbl-b, a RING-type E3 ubiquitin ligase, targets phosphatidylinositol 3-kinase for ubiquitination in T cells. J. Biol. Chem. 276, 4872-4878 (2001).
    • (2001) J. Biol. Chem , vol.276 , pp. 4872-4878
    • Fang, D.1
  • 68
    • 15144353776 scopus 로고    scopus 로고
    • Role of substrates and products of PI 3-kinase in regulating activation of Rac-related guanosine triphosphatases by Vav
    • Han, J. et al. Role of substrates and products of PI 3-kinase in regulating activation of Rac-related guanosine triphosphatases by Vav. Science 279, 558-560 (1998).
    • (1998) Science , vol.279 , pp. 558-560
    • Han, J.1
  • 69
    • 4143137360 scopus 로고    scopus 로고
    • Essential role of the E3 ubiquitin ligase Cbl-b in T cell anergy induction
    • Jeon, M. S. et al. Essential role of the E3 ubiquitin ligase Cbl-b in T cell anergy induction. Immunity 21, 167-177 (2004).
    • (2004) Immunity , vol.21 , pp. 167-177
    • Jeon, M.S.1
  • 70
    • 0242708772 scopus 로고    scopus 로고
    • Scaffolding of antigen receptors for immunogenic versus tolerogenic signaling
    • Jun, J. E. & Goodnow, C. C. Scaffolding of antigen receptors for immunogenic versus tolerogenic signaling. Nature Immunol. 4, 1057-1064 (2003).
    • (2003) Nature Immunol , vol.4 , pp. 1057-1064
    • Jun, J.E.1    Goodnow, C.C.2
  • 71
    • 0026756460 scopus 로고
    • Activation-induced ubiquitination of the T cell antigen receptor
    • Cenciarelli, C. et al. Activation-induced ubiquitination of the T cell antigen receptor. Science 257, 795-797 (1992).
    • (1992) Science , vol.257 , pp. 795-797
    • Cenciarelli, C.1
  • 72
    • 0028303252 scopus 로고
    • Activation-dependent ubiquitination of a T cell antigen receptor subunit on multiple intracellular lysines
    • Hou, D., Cenciarelli, C., Jensen, J. P., Nguygen, H. B. & Weissman, A. M. Activation-dependent ubiquitination of a T cell antigen receptor subunit on multiple intracellular lysines. J. Biol. Chem. 269, 14244-14247 (1994).
    • (1994) J. Biol. Chem , vol.269 , pp. 14244-14247
    • Hou, D.1    Cenciarelli, C.2    Jensen, J.P.3    Nguygen, H.B.4    Weissman, A.M.5
  • 73
    • 0029916504 scopus 로고    scopus 로고
    • T cell antigen receptor ubiquitination is a consequence of receptor-mediated tyrosine kinase activation
    • Cenciarelli, C., Wilhelm, K. G. Jr, Guo, A. & Weissman, A. M. T cell antigen receptor ubiquitination is a consequence of receptor-mediated tyrosine kinase activation. J. Biol. Chem. 271, 8709-8713 (1996).
    • (1996) J. Biol. Chem , vol.271 , pp. 8709-8713
    • Cenciarelli, C.1    Wilhelm Jr, K.G.2    Guo, A.3    Weissman, A.M.4
  • 74
    • 0025872395 scopus 로고
    • Down-regulation of T cell receptors on self-reactive T cells as a novel mechanism for extrathymic tolerance induction
    • Schonrich, G. et al. Down-regulation of T cell receptors on self-reactive T cells as a novel mechanism for extrathymic tolerance induction. Cell 65, 293-304 (1991).
    • (1991) Cell , vol.65 , pp. 293-304
    • Schonrich, G.1
  • 75
    • 0032438114 scopus 로고    scopus 로고
    • Altered thymic positive selection and intracellular signals in Cbl-deficient mice
    • Naramura, M., Kole, H. K., Hu, R. J. & Gu, H. Altered thymic positive selection and intracellular signals in Cbl-deficient mice. Proc. Natl Acad. Sci. USA 95, 15547-15552 (1998).
    • (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
  • 76
    • 27744485874 scopus 로고    scopus 로고
    • Loss of c-Cbl RING finger function results in high-intensity TCR signaling and thymic deletion
    • Thien, C. B. et al. Loss of c-Cbl RING finger function results in high-intensity TCR signaling and thymic deletion. EMBO J. 24, 3807-3819 (2005).
    • (2005) EMBO J , vol.24 , pp. 3807-3819
    • Thien, C.B.1
  • 77
    • 0036911112 scopus 로고    scopus 로고
    • c-Cbl and Cbl-b regulate T cell responsiveness by promoting ligand-induced TCR down-modulation
    • Naramura, M. et al. c-Cbl and Cbl-b regulate T cell responsiveness by promoting ligand-induced TCR down-modulation. Nature Immunol. 3, 1192-1199 (2002).
    • (2002) Nature Immunol , vol.3 , pp. 1192-1199
    • Naramura, M.1
  • 78
    • 33749536260 scopus 로고    scopus 로고
    • + T cells by the Cbl family proteins
    • + T cells by the Cbl family proteins. Immunity 25, 571-581 (2006).
    • (2006) Immunity , vol.25 , pp. 571-581
    • Huang, F.1
  • 79
    • 2942707976 scopus 로고    scopus 로고
    • The gene related to anergy in lymphocytes, an E3 ubiquitin ligase, is necessary for anergy induction in CD4 T cells
    • Seroogy, C. M. et al. The gene related to anergy in lymphocytes, an E3 ubiquitin ligase, is necessary for anergy induction in CD4 T cells. J. Immunol. 173, 79-85 (2004).
    • (2004) J. Immunol , vol.173 , pp. 79-85
    • Seroogy, C.M.1
  • 80
    • 0036434157 scopus 로고    scopus 로고
    • The E3 ubiquitin ligase GREUL1 anteriorizes ectoderm during Xenopus development
    • Borchers, A. G. et al. The E3 ubiquitin ligase GREUL1 anteriorizes ectoderm during Xenopus development. Dev. Biol. 251, 395-408 (2002).
    • (2002) Dev. Biol , vol.251 , pp. 395-408
    • Borchers, A.G.1
  • 81
    • 0347756727 scopus 로고    scopus 로고
    • Two isoforms of otubain 1 regulate T cell anergy via GRAIL
    • Soares, L. et al. Two isoforms of otubain 1 regulate T cell anergy via GRAIL. Nature Immunol. 5, 45-54 (2004).
    • (2004) Nature Immunol , vol.5 , pp. 45-54
    • Soares, L.1
  • 82
    • 33751583077 scopus 로고    scopus 로고
    • A novel E3 ubiquitin ligase substrate screen identifies Rho guanine dissociation inhibitor as a substrate of gene related to anergy in lymphocytes
    • Su, L., Lineberry, N., Huh, Y., Soares, L. & Fathman, C. G. A novel E3 ubiquitin ligase substrate screen identifies Rho guanine dissociation inhibitor as a substrate of gene related to anergy in lymphocytes. J. Immunol. 177, 7559-7566 (2006).
    • (2006) J. Immunol , vol.177 , pp. 7559-7566
    • Su, L.1    Lineberry, N.2    Huh, Y.3    Soares, L.4    Fathman, C.G.5
  • 83
    • 10944244704 scopus 로고    scopus 로고
    • Rho signalling at a glance
    • Schwartz, M. Rho signalling at a glance. J. Cell Sci. 117, 5457-5458 (2004).
    • (2004) J. Cell Sci , vol.117 , pp. 5457-5458
    • Schwartz, M.1
  • 84
  • 85
    • 1642565079 scopus 로고    scopus 로고
    • The HECT domain ligase itch ubiquitinates endophilin and localizes to the trans-Golgi network and endosomal system
    • Angers, A., Ramjaun, A. R. & McPherson, P. S. The HECT domain ligase itch ubiquitinates endophilin and localizes to the trans-Golgi network and endosomal system. J. Biol. Chem. 279, 11471-11479 (2004).
    • (2004) J. Biol. Chem , vol.279 , pp. 11471-11479
    • Angers, A.1    Ramjaun, A.R.2    McPherson, P.S.3
  • 86
    • 0030239829 scopus 로고    scopus 로고
    • Defective transcription of the IL-2 gene is associated with impaired expression of c-Fos, FosB, and JunB in anergic T helper 1 cells
    • Mondino, A. et al. Defective transcription of the IL-2 gene is associated with impaired expression of c-Fos, FosB, and JunB in anergic T helper 1 cells. J. Immunol. 157, 2048-2057 (1996).
    • (1996) J. Immunol , vol.157 , pp. 2048-2057
    • Mondino, A.1
  • 87
    • 0036197639 scopus 로고    scopus 로고
    • Dysregulation of T lymphocyte function in itchy mice: A role for Itch in TH2 differentiation
    • Fang, D. et al. Dysregulation of T lymphocyte function in itchy mice: a role for Itch in TH2 differentiation. Nature Immunol. 3, 281-287 (2002).
    • (2002) Nature Immunol , vol.3 , pp. 281-287
    • Fang, D.1
  • 88
    • 5044225158 scopus 로고    scopus 로고
    • Gao, M. et al. Jun turnover is controlled through JNK-dependent phosphorylation of the E3 ligase Itch. Science 306, 271-275 (2004). This paper nicely shows how extracellular stimuli through the MAPK pathway regulate the turnover of the JUN family of transcription factors by ITCH.
    • Gao, M. et al. Jun turnover is controlled through JNK-dependent phosphorylation of the E3 ligase Itch. Science 306, 271-275 (2004). This paper nicely shows how extracellular stimuli through the MAPK pathway regulate the turnover of the JUN family of transcription factors by ITCH.
  • 89
    • 32444437676 scopus 로고    scopus 로고
    • Activation of the E3 ubiquitin ligase Itch through a phosphorylation-induced conformational change
    • Gallagher, E., Gao, M., Liu, Y. C. & Karin, M. Activation of the E3 ubiquitin ligase Itch through a phosphorylation-induced conformational change. Proc. Natl Acad. Sci. USA 103, 1717-1722 (2006).
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 1717-1722
    • Gallagher, E.1    Gao, M.2    Liu, Y.C.3    Karin, M.4
  • 90
    • 29544433771 scopus 로고    scopus 로고
    • Negative regulation of the E3 ubiquitin ligase itch via Fyn-mediated tyrosine phosphorylation
    • Yang, C. et al. Negative regulation of the E3 ubiquitin ligase itch via Fyn-mediated tyrosine phosphorylation. Mol. Cell 21, 135-141 (2006).
    • (2006) Mol. Cell , vol.21 , pp. 135-141
    • Yang, C.1
  • 91
    • 6944227833 scopus 로고    scopus 로고
    • Ubiquitin-mediated fluorescence complementation reveals that Jun ubiquitinated by Itch/AIP4 is localized to lysosomes
    • Fang, D. & Kerppola, T. K. Ubiquitin-mediated fluorescence complementation reveals that Jun ubiquitinated by Itch/AIP4 is localized to lysosomes. Proc. Natl Acad. Sci. USA 101, 14782-14787 (2004).
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 14782-14787
    • Fang, D.1    Kerppola, T.K.2
  • 92
    • 33645531744 scopus 로고    scopus 로고
    • Convergence of Itch-induced ubiquitination with MEKK1-JNK signaling in Th2 tolerance and airway inflammation
    • Venuprasad, K. et al. Convergence of Itch-induced ubiquitination with MEKK1-JNK signaling in Th2 tolerance and airway inflammation. J. Clin. Invest. 116, 1117-1126 (2006).
    • (2006) J. Clin. Invest , vol.116 , pp. 1117-1126
    • Venuprasad, K.1
  • 93
    • 0037088688 scopus 로고    scopus 로고
    • Harvey, K. F., Shearwin-Whyatt, L. M., Fotia, A., Parton, R. G. & Kumar, S. N4WBP5, a potential target for ubiquitination by the Nedd4 family of proteins, is a novel Golgi-associated protein. J. Biol. Chem. 277, 9307-9317 (2002).
    • Harvey, K. F., Shearwin-Whyatt, L. M., Fotia, A., Parton, R. G. & Kumar, S. N4WBP5, a potential target for ubiquitination by the Nedd4 family of proteins, is a novel Golgi-associated protein. J. Biol. Chem. 277, 9307-9317 (2002).
  • 94
    • 33845386442 scopus 로고    scopus 로고
    • Ndfip1 protein promotes the function of itch ubiquitin ligase to prevent T cell activation and T helper 2 cell-mediated inflammation
    • Oliver, P. M. et al. Ndfip1 protein promotes the function of itch ubiquitin ligase to prevent T cell activation and T helper 2 cell-mediated inflammation. Immunity 25, 929-940 (2006).
    • (2006) Immunity , vol.25 , pp. 929-940
    • Oliver, P.M.1
  • 95
    • 0141446030 scopus 로고    scopus 로고
    • Cloning and characterization of N4WBP5A, an inducible, cyclosporine-sensitive, Nedd4-binding protein in human T lymphocytes
    • Cristillo, A. D., Nie, L., Macri, M. J. & Bierer, B. E. Cloning and characterization of N4WBP5A, an inducible, cyclosporine-sensitive, Nedd4-binding protein in human T lymphocytes. J. Biol. Chem. 278, 34587-34597 (2003).
    • (2003) J. Biol. Chem , vol.278 , pp. 34587-34597
    • Cristillo, A.D.1    Nie, L.2    Macri, M.J.3    Bierer, B.E.4
  • 96
    • 0242290342 scopus 로고    scopus 로고
    • WW domain HECT E3s target Cbl RING finger E3s for proteasomal degradation
    • Magnifico, A. et al. WW domain HECT E3s target Cbl RING finger E3s for proteasomal degradation. J. Biol. Chem. 278, 43169-43177 (2003).
    • (2003) J. Biol. Chem , vol.278 , pp. 43169-43177
    • Magnifico, A.1
  • 97
    • 33846019272 scopus 로고    scopus 로고
    • The ubiquitin ligase itch is auto-ubiquitylated in vivo and in vitro but is protected from degradation by interacting with the deubiquitylating enzyme FAM/USP9X
    • Mouchantaf, R. et al. The ubiquitin ligase itch is auto-ubiquitylated in vivo and in vitro but is protected from degradation by interacting with the deubiquitylating enzyme FAM/USP9X. J. Biol. Chem. 281, 38738-38747 (2006).
    • (2006) J. Biol. Chem , vol.281 , pp. 38738-38747
    • Mouchantaf, R.1
  • 99
    • 1642456674 scopus 로고    scopus 로고
    • Regulation of ZAP-70 activation and TCR signaling by two related proteins, Sts-1 and Sts-2
    • Carpino, N. et al. Regulation of ZAP-70 activation and TCR signaling by two related proteins, Sts-1 and Sts-2. Immunity 20, 37-46 (2004).
    • (2004) Immunity , vol.20 , pp. 37-46
    • Carpino, N.1
  • 100
    • 3543046114 scopus 로고    scopus 로고
    • Suppressors of T-cell receptor signaling Sts-1 and Sts-2 bind to Cbl and inhibit endocytosis of receptor tyrosine kinases
    • Kowanetz, K. et al. Suppressors of T-cell receptor signaling Sts-1 and Sts-2 bind to Cbl and inhibit endocytosis of receptor tyrosine kinases. J. Biol. Chem. 279, 32786-32795 (2004).
    • (2004) J. Biol. Chem , vol.279 , pp. 32786-32795
    • Kowanetz, K.1
  • 101
    • 2942720847 scopus 로고    scopus 로고
    • TULA: An SH3- and UBA-containing protein that binds to c-Cbl and ubiquitin
    • Feshchenko, E. A. et al. TULA: an SH3- and UBA-containing protein that binds to c-Cbl and ubiquitin. Oncogene 23, 4690-4706 (2004).
    • (2004) Oncogene , vol.23 , pp. 4690-4706
    • Feshchenko, E.A.1
  • 102
    • 0034915764 scopus 로고    scopus 로고
    • Mechanisms underlying ubiquitination
    • Pickart, C. M. Mechanisms underlying ubiquitination. Annu. Rev. Biochem. 70, 503-533 (2001).
    • (2001) Annu. Rev. Biochem , vol.70 , pp. 503-533
    • Pickart, C.M.1
  • 103
    • 28344456279 scopus 로고    scopus 로고
    • A genomic and functional inventory of deubiquitinating enzymes
    • Nijman, S. M. et al. A genomic and functional inventory of deubiquitinating enzymes. Cell 123, 773-786 (2005).
    • (2005) Cell , vol.123 , pp. 773-786
    • Nijman, S.M.1
  • 104
    • 21744433861 scopus 로고    scopus 로고
    • Ubiquitination on nonlysine residues by a viral E3 ubiquitin ligase
    • Cadwell, K. & Coscoy, L. Ubiquitination on nonlysine residues by a viral E3 ubiquitin ligase. Science 309, 127-130 (2005).
    • (2005) Science , vol.309 , pp. 127-130
    • Cadwell, K.1    Coscoy, L.2
  • 105
    • 34547193611 scopus 로고    scopus 로고
    • B-cell anergy: From transgenic models to naturally occurring anergic B cells?
    • Cambier, J. C., Gauld, S. B. Merrell, K. T. & Vilen, B. J. B-cell anergy: from transgenic models to naturally occurring anergic B cells? Nature Rev. Immunol. 7, 633-643 (2007).
    • (2007) Nature Rev. Immunol , vol.7 , pp. 633-643
    • Cambier, J.C.1    Gauld, S.B.2    Merrell, K.T.3    Vilen, B.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.