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Volumn 228, Issue 1, 2009, Pages 199-211

CARMA1-mediated NF-κB and JNK activation in lymphocytes

Author keywords

AP 1; CARMA1; IKK; JNK; Jun; NF B

Indexed keywords

ACTIVATED PROTEIN C; CASPASE RECRUITMENT DOMAIN SIGNALING PROTEIN; GUANYLATE KINASE; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; MEMBRANE ASSOCIATED GUANYLATE CYCLASE KINASE; PHOSPHOTRANSFERASE; SCAFFOLD PROTEIN; STRESS ACTIVATED PROTEIN KINASE; SYNAPSIN I; TRANSCRIPTION FACTOR;

EID: 61849113179     PISSN: 01052896     EISSN: 1600065X     Source Type: Journal    
DOI: 10.1111/j.1600-065X.2008.00749.x     Document Type: Article
Times cited : (88)

References (119)
  • 1
    • 0036221481 scopus 로고    scopus 로고
    • Signal transduction mediated by the T cell antigen receptor: The role of adapter proteins
    • Samelson LE. Signal transduction mediated by the T cell antigen receptor: the role of adapter proteins. Annu Rev Immunol 2002 20 : 371 394.
    • (2002) Annu Rev Immunol , vol.20 , pp. 371-394
    • Samelson, L.E.1
  • 2
    • 0033047309 scopus 로고    scopus 로고
    • Integration of T cell receptor-dependent signaling pathways by adapter proteins
    • Clements JL, Boerth NJ, Lee JR, Koretzky GA. Integration of T cell receptor-dependent signaling pathways by adapter proteins. Annu Rev Immunol 1999 17 : 89 108.
    • (1999) Annu Rev Immunol , vol.17 , pp. 89-108
    • Clements, J.L.1    Boerth, N.J.2    Lee, J.R.3    Koretzky, G.A.4
  • 3
    • 33846228444 scopus 로고    scopus 로고
    • Antigen-receptor signaling to nuclear factor kappa B
    • Schulze-Luehrmann J, Ghosh S. Antigen-receptor signaling to nuclear factor kappa B. Immunity 2006 25 : 701 715.
    • (2006) Immunity , vol.25 , pp. 701-715
    • Schulze-Luehrmann, J.1    Ghosh, S.2
  • 4
    • 0036009115 scopus 로고    scopus 로고
    • NF-kappaB at the crossroads of life and death
    • Karin M, Lin A. NF-kappaB at the crossroads of life and death. Nat Immunol 2002 3 : 221 227.
    • (2002) Nat Immunol , vol.3 , pp. 221-227
    • Karin, M.1    Lin, A.2
  • 5
    • 0034084163 scopus 로고    scopus 로고
    • Phosphorylation meets ubiquitination: The control of NF-[kappa]B activity
    • Karin M, Ben-Neriah Y. Phosphorylation meets ubiquitination: the control of NF-[kappa]B activity. Annu Rev Immunol 2000 18 : 621 663.
    • (2000) Annu Rev Immunol , vol.18 , pp. 621-663
    • Karin, M.1    Ben-Neriah, Y.2
  • 6
    • 38849199203 scopus 로고    scopus 로고
    • Shared principles in NF-kappaB signaling
    • Hayden MS, Ghosh S. Shared principles in NF-kappaB signaling. Cell 2008 132 : 344 362.
    • (2008) Cell , vol.132 , pp. 344-362
    • Hayden, M.S.1    Ghosh, S.2
  • 7
    • 0036707520 scopus 로고    scopus 로고
    • A requirement for CARMA1 in TCR-induced NF-kappa B activation
    • Wang D, et al. A requirement for CARMA1 in TCR-induced NF-kappa B activation. Nat Immunol 2002 3 : 830 835.
    • (2002) Nat Immunol , vol.3 , pp. 830-835
    • Wang, D.1
  • 8
    • 0346993668 scopus 로고    scopus 로고
    • CD3/CD28 costimulation-induced NF-kappaB activation is mediated by recruitment of protein kinase C-theta, Bcl10, and IkappaB kinase beta to the immunological synapse through CARMA1
    • Wang D, et al. CD3/CD28 costimulation-induced NF-kappaB activation is mediated by recruitment of protein kinase C-theta, Bcl10, and IkappaB kinase beta to the immunological synapse through CARMA1. Mol Cell Biol 2004 24 : 164 171.
    • (2004) Mol Cell Biol , vol.24 , pp. 164-171
    • Wang, D.1
  • 9
    • 1942469524 scopus 로고    scopus 로고
    • MALT1/paracaspase is a signaling component downstream of CARMA1 and mediates T cell receptor-induced NF-kappaB activation
    • Che T, You Y, Wang D, Tanner MJ, Dixit VM, Lin X. MALT1/paracaspase is a signaling component downstream of CARMA1 and mediates T cell receptor-induced NF-kappaB activation. J Biol Chem 2004 279 : 15870 15876.
    • (2004) J Biol Chem , vol.279 , pp. 15870-15876
    • Che, T.1    You, Y.2    Wang, D.3    Tanner, M.J.4    Dixit, V.M.5    Lin, X.6
  • 10
    • 28844499919 scopus 로고    scopus 로고
    • Phosphorylation of CARMA1 plays a critical role in T cell receptor-mediated NF-kappaB activation
    • Matsumoto R, et al. Phosphorylation of CARMA1 plays a critical role in T cell receptor-mediated NF-kappaB activation. Immunity 2005 23 : 575 585.
    • (2005) Immunity , vol.23 , pp. 575-585
    • Matsumoto, R.1
  • 11
    • 34247205985 scopus 로고    scopus 로고
    • Phosphorylation and ubiquitination of the IkappaB kinase complex by two distinct signaling pathways
    • Shambharkar PB, et al. Phosphorylation and ubiquitination of the IkappaB kinase complex by two distinct signaling pathways. EMBO J 2007 26 : 1794 1805.
    • (2007) EMBO J , vol.26 , pp. 1794-1805
    • Shambharkar, P.B.1
  • 12
    • 34447126345 scopus 로고    scopus 로고
    • CARMA1 coiled-coil domain is involved in the oligomerization and subcellular localization of CARMA1 and is required for T cell receptor-induced NF-kappaB activation
    • Tanner MJ, Hanel W, Gaffen SL, Lin X. CARMA1 coiled-coil domain is involved in the oligomerization and subcellular localization of CARMA1 and is required for T cell receptor-induced NF-kappaB activation. J Biol Chem 2007 282 : 17141 17147.
    • (2007) J Biol Chem , vol.282 , pp. 17141-17147
    • Tanner, M.J.1    Hanel, W.2    Gaffen, S.L.3    Lin, X.4
  • 13
    • 33846235557 scopus 로고    scopus 로고
    • The CARMA1-Bcl10 signaling complex selectively regulates JNK2 kinase in the T cell receptor-signaling pathway
    • Blonska M, et al. The CARMA1-Bcl10 signaling complex selectively regulates JNK2 kinase in the T cell receptor-signaling pathway. Immunity 2007 26 : 55 66.
    • (2007) Immunity , vol.26 , pp. 55-66
    • Blonska, M.1
  • 14
    • 0032483559 scopus 로고    scopus 로고
    • A novel adaptor protein orchestrates receptor patterning and cytoskeletal polarity in T-cell contacts
    • Dustin ML, et al. A novel adaptor protein orchestrates receptor patterning and cytoskeletal polarity in T-cell contacts. Cell 1998 94 : 667 677.
    • (1998) Cell , vol.94 , pp. 667-677
    • Dustin, M.L.1
  • 15
    • 0032986671 scopus 로고    scopus 로고
    • Membrane compartmentation and the response to antigen
    • Xavier R, Seed B. Membrane compartmentation and the response to antigen. Curr Opin Immunol 1999 11 : 265 269.
    • (1999) Curr Opin Immunol , vol.11 , pp. 265-269
    • Xavier, R.1    Seed, B.2
  • 16
    • 0035059418 scopus 로고    scopus 로고
    • The immunological synapse
    • Bromley SK, et al. The immunological synapse. Annu Rev Immunol 2001 19 : 375 396.
    • (2001) Annu Rev Immunol , vol.19 , pp. 375-396
    • Bromley, S.K.1
  • 17
    • 0031012266 scopus 로고    scopus 로고
    • Selective modulation of protein kinase C-theta during T-cell activation
    • Monks CR, Kupfer H, Tamir I, Barlow A, Kupfer A. Selective modulation of protein kinase C-theta during T-cell activation. Nature 1997 385 : 83 86.
    • (1997) Nature , vol.385 , pp. 83-86
    • Monks, C.R.1    Kupfer, H.2    Tamir, I.3    Barlow, A.4    Kupfer, A.5
  • 18
    • 0034031401 scopus 로고    scopus 로고
    • Protein kinase C-theta participates in NF-kappaB activation induced by CD3-CD28 costimulation through selective activation of IkappaB kinase beta
    • Lin X, O'Mahony A, Mu Y, Geleziunas R, Greene WC. Protein kinase C-theta participates in NF-kappaB activation induced by CD3-CD28 costimulation through selective activation of IkappaB kinase beta. Mol Cell Biol 2000 20 : 2933 2940.
    • (2000) Mol Cell Biol , vol.20 , pp. 2933-2940
    • Lin, X.1    O'Mahony, A.2    Mu, Y.3    Geleziunas, R.4    Greene, W.C.5
  • 19
    • 0034724201 scopus 로고    scopus 로고
    • NF-kappa B activation induced by T cell receptor/CD28 costimulation is mediated by protein kinase C-theta
    • Coudronniere N, Villalba M, Englund N, Altman A. NF-kappa B activation induced by T cell receptor/CD28 costimulation is mediated by protein kinase C-theta. Proc Natl Acad Sci USA 2000 97 : 3394 3399.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 3394-3399
    • Coudronniere, N.1    Villalba, M.2    Englund, N.3    Altman, A.4
  • 20
    • 18844473151 scopus 로고    scopus 로고
    • PKC-theta is required for TCR-induced NF-kappaB activation in mature but not immature T lymphocytes
    • Sun Z, et al. PKC-theta is required for TCR-induced NF-kappaB activation in mature but not immature T lymphocytes. Nature 2000 404 : 402 407.
    • (2000) Nature , vol.404 , pp. 402-407
    • Sun, Z.1
  • 21
    • 0036707522 scopus 로고    scopus 로고
    • CARMA1 is a critical lipid raft-associated regulator of TCR-induced NF-kappa B activation
    • Gaide O, et al. CARMA1 is a critical lipid raft-associated regulator of TCR-induced NF-kappa B activation. Nat Immunol 2002 3 : 836 843.
    • (2002) Nat Immunol , vol.3 , pp. 836-843
    • Gaide, O.1
  • 22
    • 0036790507 scopus 로고    scopus 로고
    • CARD11 mediates factor-specific activation of NF-kappaB by the T cell receptor complex
    • Pomerantz JL, Denny EM, Baltimore D. CARD11 mediates factor-specific activation of NF-kappaB by the T cell receptor complex. EMBO J 2002 21 : 5184 5194.
    • (2002) EMBO J , vol.21 , pp. 5184-5194
    • Pomerantz, J.L.1    Denny, E.M.2    Baltimore, D.3
  • 23
    • 0037490078 scopus 로고    scopus 로고
    • The MAGUK family protein CARD11 is essential for lymphocyte activation
    • Hara H, et al. The MAGUK family protein CARD11 is essential for lymphocyte activation. Immunity 2003 18 : 763 775.
    • (2003) Immunity , vol.18 , pp. 763-775
    • Hara, H.1
  • 24
    • 0038375851 scopus 로고    scopus 로고
    • Requirement for CARMA1 in antigen receptor-induced NF-kappa B activation and lymphocyte proliferation
    • Egawa T, et al. Requirement for CARMA1 in antigen receptor-induced NF-kappa B activation and lymphocyte proliferation. Curr Biol 2003 13 : 1252 1258.
    • (2003) Curr Biol , vol.13 , pp. 1252-1258
    • Egawa, T.1
  • 25
    • 0038037580 scopus 로고    scopus 로고
    • Mice lacking the CARD of CARMA1 exhibit defective B lymphocyte development and impaired proliferation of their B and T lymphocytes
    • Newton K, Dixit V. Mice lacking the CARD of CARMA1 exhibit defective B lymphocyte development and impaired proliferation of their B and T lymphocytes. Curr Biol 2003 13 : 1247 1251.
    • (2003) Curr Biol , vol.13 , pp. 1247-1251
    • Newton, K.1    Dixit, V.2
  • 26
    • 0037827638 scopus 로고    scopus 로고
    • Identifying the MAGUK protein Carma-1 as a central regulator of humoral immune responses and atopy by genome-wide mouse mutagenesis
    • Jun J, et al. Identifying the MAGUK protein Carma-1 as a central regulator of humoral immune responses and atopy by genome-wide mouse mutagenesis. Immunity 2003 18 : 751 762.
    • (2003) Immunity , vol.18 , pp. 751-762
    • Jun, J.1
  • 27
    • 33751273254 scopus 로고    scopus 로고
    • Potential role of CARMA1 in CD40-induced splenic B cell proliferation and marginal zone B cell maturation
    • Pappu BP, Lin X. Potential role of CARMA1 in CD40-induced splenic B cell proliferation and marginal zone B cell maturation. Eur J Immunol 2006 36 : 3033 3043.
    • (2006) Eur J Immunol , vol.36 , pp. 3033-3043
    • Pappu, B.P.1    Lin, X.2
  • 28
    • 0035853841 scopus 로고    scopus 로고
    • CARD11 and CARD14 are novel caspase recruitment domain (CARD)/membrane-associated guanylate kinase (MAGUK) family members that interact with BCL10 and activate NF-kappa B
    • Bertin J, et al. CARD11 and CARD14 are novel caspase recruitment domain (CARD)/membrane-associated guanylate kinase (MAGUK) family members that interact with BCL10 and activate NF-kappa B. J Biol Chem 2001 276 : 11877 11882.
    • (2001) J Biol Chem , vol.276 , pp. 11877-11882
    • Bertin, J.1
  • 29
    • 0035843970 scopus 로고    scopus 로고
    • Carma1, a CARD-containing binding partner of Bcl10, induces Bcl10 phosphorylation and NF-kappaB activation
    • Gaide O, Martinon F, Micheau O, Bonnet D, Thome M, Tschopp J. Carma1, a CARD-containing binding partner of Bcl10, induces Bcl10 phosphorylation and NF-kappaB activation. FEBS Lett 2001 496 : 121 127.
    • (2001) FEBS Lett , vol.496 , pp. 121-127
    • Gaide, O.1    Martinon, F.2    Micheau, O.3    Bonnet, D.4    Thome, M.5    Tschopp, J.6
  • 30
    • 0033230122 scopus 로고    scopus 로고
    • Signaling pathways are focused at specialized regions of the plasma membrane by scaffolding proteins of the MAGUK family
    • Dimitratos SD, Woods DF, Stathakis DG, Bryant PJ. Signaling pathways are focused at specialized regions of the plasma membrane by scaffolding proteins of the MAGUK family. Bioessays 1999 21 : 912 921.
    • (1999) Bioessays , vol.21 , pp. 912-921
    • Dimitratos, S.D.1    Woods, D.F.2    Stathakis, D.G.3    Bryant, P.J.4
  • 31
    • 0035877776 scopus 로고    scopus 로고
    • Card10 is a novel caspase recruitment domain/membrane-associated guanylate kinase family member that interacts with BCL10 and activates NF-kappa B
    • Wang L, et al. Card10 is a novel caspase recruitment domain/membrane- associated guanylate kinase family member that interacts with BCL10 and activates NF-kappa B. J Biol Chem 2001 276 : 21405 21409.
    • (2001) J Biol Chem , vol.276 , pp. 21405-21409
    • Wang, L.1
  • 32
    • 0035903154 scopus 로고    scopus 로고
    • Bimp1, a MAGUK family member linking protein kinase C activation to Bcl10-mediated NF-kappaB induction
    • McAllister-Lucas LM, et al. Bimp1, a MAGUK family member linking protein kinase C activation to Bcl10-mediated NF-kappaB induction. J Biol Chem 2001 276 : 30589 30597.
    • (2001) J Biol Chem , vol.276 , pp. 30589-30597
    • McAllister-Lucas, L.M.1
  • 33
    • 34247240413 scopus 로고    scopus 로고
    • CARMA3 deficiency abrogates G protein-coupled receptor-induced NF- kappa B activation
    • Grabiner BC, et al. CARMA3 deficiency abrogates G protein-coupled receptor-induced NF- kappa B activation. Genes Dev 2007 21 : 984 996.
    • (2007) Genes Dev , vol.21 , pp. 984-996
    • Grabiner, B.C.1
  • 34
    • 8644283766 scopus 로고    scopus 로고
    • The molecular adapter Carma1 controls entry of IkappaB kinase into the central immune synapse
    • Hara H, et al. The molecular adapter Carma1 controls entry of IkappaB kinase into the central immune synapse. J Exp Med 2004 200 : 1167 1177.
    • (2004) J Exp Med , vol.200 , pp. 1167-1177
    • Hara, H.1
  • 35
    • 0033534627 scopus 로고    scopus 로고
    • Bcl10 is involved in t(1;14)(p22;q32) of MALT B cell lymphoma and mutated in multiple tumor types
    • Willis TG, et al. Bcl10 is involved in t(1;14)(p22;q32) of MALT B cell lymphoma and mutated in multiple tumor types. Cell 1999 96 : 35 45.
    • (1999) Cell , vol.96 , pp. 35-45
    • Willis, T.G.1
  • 36
    • 0032958801 scopus 로고    scopus 로고
    • Inactivating mutations and overexpression of BCL10, a caspase recruitment domain-containing gene, in MALT lymphoma with t(1;14)(p22;q32)
    • Zhang Q, et al. Inactivating mutations and overexpression of BCL10, a caspase recruitment domain-containing gene, in MALT lymphoma with t(1;14)(p22;q32). Nat Genet 1999 22 : 63 68.
    • (1999) Nat Genet , vol.22 , pp. 63-68
    • Zhang, Q.1
  • 37
    • 0033537840 scopus 로고    scopus 로고
    • CIPER, a novel NF kappaB-activating protein containing a caspase recruitment domain with homology to Herpesvirus-2 protein E10
    • Koseki T, et al. CIPER, a novel NF kappaB-activating protein containing a caspase recruitment domain with homology to Herpesvirus-2 protein E10. J Biol Chem 1999 274 : 9955 9961.
    • (1999) J Biol Chem , vol.274 , pp. 9955-9961
    • Koseki, T.1
  • 38
    • 0033537851 scopus 로고    scopus 로고
    • Equine herpesvirus-2 E10 gene product, but not its cellular homologue, activates NF-kappaB transcription factor and c-Jun N-terminal kinase
    • Thome M, et al. Equine herpesvirus-2 E10 gene product, but not its cellular homologue, activates NF-kappaB transcription factor and c-Jun N-terminal kinase. J Biol Chem 1999 274 : 9962 9968.
    • (1999) J Biol Chem , vol.274 , pp. 9962-9968
    • Thome, M.1
  • 39
    • 0033537887 scopus 로고    scopus 로고
    • ME10, a novel caspase recruitment domain-containing proapoptotic molecule
    • Yan M, Lee J, Schilbach S, Goddard A, Dixit V. mE10, a novel caspase recruitment domain-containing proapoptotic molecule. J Biol Chem 1999 274 : 10287 10292.
    • (1999) J Biol Chem , vol.274 , pp. 10287-10292
    • Yan, M.1    Lee, J.2    Schilbach, S.3    Goddard, A.4    Dixit, V.5
  • 40
    • 17744386318 scopus 로고    scopus 로고
    • Bcl10 is a positive regulator of antigen receptor-induced activation of NF-kappaB and neural tube closure
    • Ruland J, et al. Bcl10 is a positive regulator of antigen receptor-induced activation of NF-kappaB and neural tube closure. Cell 2001 104 : 33 42.
    • (2001) Cell , vol.104 , pp. 33-42
    • Ruland, J.1
  • 41
    • 0033151510 scopus 로고    scopus 로고
    • The apoptosis inhibitor gene API2 and a novel 18q gene, MLT, are recurrently rearranged in the t(11;18)(q21;q21) associated with mucosa-associated lymphoid tissue lymphomas
    • Dierlamm J, et al. The apoptosis inhibitor gene API2 and a novel 18q gene, MLT, are recurrently rearranged in the t(11;18)(q21;q21) associated with mucosa-associated lymphoid tissue lymphomas. Blood 1999 93 : 3601 3609.
    • (1999) Blood , vol.93 , pp. 3601-3609
    • Dierlamm, J.1
  • 42
    • 0033554647 scopus 로고    scopus 로고
    • A novel gene, MALT1 at 18q21, is involved in t(11;18) (q21;q21) found in low-grade B-cell lymphoma of mucosa-associated lymphoid tissue
    • Akagi T, et al. A novel gene, MALT1 at 18q21, is involved in t(11;18) (q21;q21) found in low-grade B-cell lymphoma of mucosa-associated lymphoid tissue. Oncogene 1999 18 : 5785 5794.
    • (1999) Oncogene , vol.18 , pp. 5785-5794
    • Akagi, T.1
  • 43
    • 0033638182 scopus 로고    scopus 로고
    • Identification of paracaspases and metacaspases: Two ancient families of caspase-like proteins, one of which plays a key role in MALT lymphoma
    • Uren AG, et al. Identification of paracaspases and metacaspases: two ancient families of caspase-like proteins, one of which plays a key role in MALT lymphoma. Mol Cell 2000 6 : 961 967.
    • (2000) Mol Cell , vol.6 , pp. 961-967
    • Uren, A.G.1
  • 44
    • 0345374583 scopus 로고    scopus 로고
    • Regulation of NF-kappaB-dependent lymphocyte activation and development by paracaspase
    • Ruefli-Brasse AA, French DM, Dixit VM. Regulation of NF-kappaB-dependent lymphocyte activation and development by paracaspase. Science 2003 302 : 1581 1584.
    • (2003) Science , vol.302 , pp. 1581-1584
    • Ruefli-Brasse, A.A.1    French, D.M.2    Dixit, V.M.3
  • 45
    • 0345358541 scopus 로고    scopus 로고
    • Differential requirement for Malt1 in T and B cell antigen receptor signaling
    • Ruland J, Duncan GS, Wakeham A, Mak TW. Differential requirement for Malt1 in T and B cell antigen receptor signaling. Immunity 2003 19 : 749 758.
    • (2003) Immunity , vol.19 , pp. 749-758
    • Ruland, J.1    Duncan, G.S.2    Wakeham, A.3    Mak, T.W.4
  • 46
    • 34548136086 scopus 로고    scopus 로고
    • MALT1 directs B cell receptor-induced canonical nuclear factor-kappaB signaling selectively to the c-Rel subunit
    • Ferch U, et al. MALT1 directs B cell receptor-induced canonical nuclear factor-kappaB signaling selectively to the c-Rel subunit. Nat Immunol 2007 8 : 984 991.
    • (2007) Nat Immunol , vol.8 , pp. 984-991
    • Ferch, U.1
  • 47
    • 15944410614 scopus 로고    scopus 로고
    • PDK1 nucleates T cell receptor-induced signaling complex for NF-kappaB activation
    • Lee KY, D'Acquisto F, Hayden MS, Shim JH, Ghosh S. PDK1 nucleates T cell receptor-induced signaling complex for NF-kappaB activation. Science 2005 308 : 114 118.
    • (2005) Science , vol.308 , pp. 114-118
    • Lee, K.Y.1    D'Acquisto, F.2    Hayden, M.S.3    Shim, J.H.4    Ghosh, S.5
  • 48
    • 34248157637 scopus 로고    scopus 로고
    • Regulation of NF-kappaB activation in T cells via association of the adapter proteins ADAP and CARMA1
    • Medeiros RB, et al. Regulation of NF-kappaB activation in T cells via association of the adapter proteins ADAP and CARMA1. Science 2007 316 : 754 758.
    • (2007) Science , vol.316 , pp. 754-758
    • Medeiros, R.B.1
  • 49
    • 0036344276 scopus 로고    scopus 로고
    • PKC-beta controls i kappa B kinase lipid raft recruitment and activation in response to BCR signaling
    • Su TT, et al. PKC-beta controls I kappa B kinase lipid raft recruitment and activation in response to BCR signaling. Nat Immunol 2002 3 : 780 786.
    • (2002) Nat Immunol , vol.3 , pp. 780-786
    • Su, T.T.1
  • 51
    • 28844500398 scopus 로고    scopus 로고
    • Phosphorylation of the CARMA1 linker controls NF-kappaB activation
    • Sommer K, et al. Phosphorylation of the CARMA1 linker controls NF-kappaB activation. Immunity 2005 23 : 561 574.
    • (2005) Immunity , vol.23 , pp. 561-574
    • Sommer, K.1
  • 52
    • 27944503997 scopus 로고    scopus 로고
    • PKC beta regulates BCR-mediated IKK activation by facilitating the interaction between TAK1 and CARMA1
    • Shinohara H, et al. PKC beta regulates BCR-mediated IKK activation by facilitating the interaction between TAK1 and CARMA1. J Exp Med 2005 202 : 1423 1431.
    • (2005) J Exp Med , vol.202 , pp. 1423-1431
    • Shinohara, H.1
  • 53
    • 37549011707 scopus 로고    scopus 로고
    • IkappaB kinase beta-induced phosphorylation of CARMA1 contributes to CARMA1 Bcl10 MALT1 complex formation in B cells
    • Shinohara H, Maeda S, Watarai H, Kurosaki T. IkappaB kinase beta-induced phosphorylation of CARMA1 contributes to CARMA1 Bcl10 MALT1 complex formation in B cells. J Exp Med 2007 204 : 3285 3293.
    • (2007) J Exp Med , vol.204 , pp. 3285-3293
    • Shinohara, H.1    Maeda, S.2    Watarai, H.3    Kurosaki, T.4
  • 54
    • 33644772836 scopus 로고    scopus 로고
    • CARMA1 is required for Akt-mediated NF-kappaB activation in T cells
    • Narayan P, Holt B, Tosti R, Kane LP. CARMA1 is required for Akt-mediated NF-kappaB activation in T cells. Mol Cell Biol 2006 26 : 2327 2336.
    • (2006) Mol Cell Biol , vol.26 , pp. 2327-2336
    • Narayan, P.1    Holt, B.2    Tosti, R.3    Kane, L.P.4
  • 55
    • 41149145089 scopus 로고    scopus 로고
    • T-cell receptor-induced NF-kappaB activation is negatively regulated by E3 ubiquitin ligase Cbl-b
    • Qiao G, et al. T-cell receptor-induced NF-kappaB activation is negatively regulated by E3 ubiquitin ligase Cbl-b. Mol Cell Biol 2008 28 : 2470 2480.
    • (2008) Mol Cell Biol , vol.28 , pp. 2470-2480
    • Qiao, G.1
  • 56
    • 51349164412 scopus 로고    scopus 로고
    • The protein kinase C-responsive inhibitory domain of CARD11 functions in NF-kappaB activation to regulate the association of multiple signaling cofactors that differentially depend on Bcl10 and MALT1 for association
    • McCully RR, Pomerantz JL. The protein kinase C-responsive inhibitory domain of CARD11 functions in NF-kappaB activation to regulate the association of multiple signaling cofactors that differentially depend on Bcl10 and MALT1 for association. Mol Cell Biol 2008 28 : 5668 5686.
    • (2008) Mol Cell Biol , vol.28 , pp. 5668-5686
    • McCully, R.R.1    Pomerantz, J.L.2
  • 57
    • 33745818394 scopus 로고    scopus 로고
    • Ca2+/calmodulin-dependent protein kinase II is a modulator of CARMA1-mediated NF-kappaB activation
    • Ishiguro K, et al. Ca2+/calmodulin-dependent protein kinase II is a modulator of CARMA1-mediated NF-kappaB activation. Mol Cell Biol 2006 26 : 5497 5508.
    • (2006) Mol Cell Biol , vol.26 , pp. 5497-5508
    • Ishiguro, K.1
  • 58
    • 0742270964 scopus 로고    scopus 로고
    • Complex and dynamic redistribution of NF-kappaB signaling intermediates in response to T cell receptor stimulation
    • Schaefer BC, Kappler JW, Kupfer A, Marrack P. Complex and dynamic redistribution of NF-kappaB signaling intermediates in response to T cell receptor stimulation. Proc Natl Acad Sci USA 2004 101 : 1004 1009.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 1004-1009
    • Schaefer, B.C.1    Kappler, J.W.2    Kupfer, A.3    Marrack, P.4
  • 60
    • 42949098959 scopus 로고    scopus 로고
    • NEMO recognition of ubiquitinated Bcl10 is required for T cell receptor-mediated NF-kappaB activation
    • Wu CJ, Ashwell JD. NEMO recognition of ubiquitinated Bcl10 is required for T cell receptor-mediated NF-kappaB activation. Proc Natl Acad Sci USA 2008 105 : 3023 3028.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 3023-3028
    • Wu, C.J.1    Ashwell, J.D.2
  • 61
    • 0347093172 scopus 로고    scopus 로고
    • Rip2 participates in Bcl10 signaling and T-cell receptor-mediated NF-kappaB activation
    • Ruefli-Brasse AA, Lee WP, Hurst S, Dixit VM. Rip2 participates in Bcl10 signaling and T-cell receptor-mediated NF-kappaB activation. J Biol Chem 2004 279 : 1570 1574.
    • (2004) J Biol Chem , vol.279 , pp. 1570-1574
    • Ruefli-Brasse, A.A.1    Lee, W.P.2    Hurst, S.3    Dixit, V.M.4
  • 62
    • 33745494351 scopus 로고    scopus 로고
    • Essential role for IkappaB kinase beta in remodeling Carma1-Bcl10-Malt1 complexes upon T cell activation
    • Wegener E, et al. Essential role for IkappaB kinase beta in remodeling Carma1-Bcl10-Malt1 complexes upon T cell activation. Mol Cell 2006 23 : 13 23.
    • (2006) Mol Cell , vol.23 , pp. 13-23
    • Wegener, E.1
  • 63
    • 34247231879 scopus 로고    scopus 로고
    • Bcl10 is phosphorylated on Ser138 by Ca2+/calmodulin-dependent protein kinase II
    • Ishiguro K, Ando T, Goto H, Xavier R. Bcl10 is phosphorylated on Ser138 by Ca2+/calmodulin-dependent protein kinase II. Mol Immunol 2007 44 : 2095 2100.
    • (2007) Mol Immunol , vol.44 , pp. 2095-2100
    • Ishiguro, K.1    Ando, T.2    Goto, H.3    Xavier, R.4
  • 64
    • 34447503930 scopus 로고    scopus 로고
    • Phosphorylation of Bcl10 negatively regulates T-cell receptor-mediated NF-kappaB activation
    • Zeng H, et al. Phosphorylation of Bcl10 negatively regulates T-cell receptor-mediated NF-kappaB activation. Mol Cell Biol 2007 27 : 5235 5245.
    • (2007) Mol Cell Biol , vol.27 , pp. 5235-5245
    • Zeng, H.1
  • 65
    • 33846528701 scopus 로고    scopus 로고
    • Negative feedback loop in T cell activation through IkappaB kinase-induced phosphorylation and degradation of Bcl10
    • Lobry C, Lopez T, Israel A, Weil R. Negative feedback loop in T cell activation through IkappaB kinase-induced phosphorylation and degradation of Bcl10. Proc Natl Acad Sci USA 2007 104 : 908 913.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 908-913
    • Lobry, C.1    Lopez, T.2    Israel, A.3    Weil, R.4
  • 66
    • 1942453854 scopus 로고    scopus 로고
    • Degradation of Bcl10 induced by T-cell activation negatively regulates NF-kappa B signaling
    • Scharschmidt E, Wegener E, Heissmeyer V, Rao A, Krappmann D. Degradation of Bcl10 induced by T-cell activation negatively regulates NF-kappa B signaling. Mol Cell Biol 2004 24 : 3860 3873.
    • (2004) Mol Cell Biol , vol.24 , pp. 3860-3873
    • Scharschmidt, E.1    Wegener, E.2    Heissmeyer, V.3    Rao, A.4    Krappmann, D.5
  • 67
    • 0345826149 scopus 로고    scopus 로고
    • Bcl10 activates the NF-kappaB pathway through ubiquitination of NEMO
    • Zhou H, et al. Bcl10 activates the NF-kappaB pathway through ubiquitination of NEMO. Nature 2004 427 : 167 171.
    • (2004) Nature , vol.427 , pp. 167-171
    • Zhou, H.1
  • 68
    • 2342629277 scopus 로고    scopus 로고
    • The TRAF6 ubiquitin ligase and TAK1 kinase mediate IKK activation by BCL10 and MALT1 in T lymphocytes
    • Sun L, Deng L, Ea CK, Xia ZP, Chen ZJ. The TRAF6 ubiquitin ligase and TAK1 kinase mediate IKK activation by BCL10 and MALT1 in T lymphocytes. Mol Cell 2004 14 : 289 301.
    • (2004) Mol Cell , vol.14 , pp. 289-301
    • Sun, L.1    Deng, L.2    Ea, C.K.3    Xia, Z.P.4    Chen, Z.J.5
  • 69
    • 36249008032 scopus 로고    scopus 로고
    • Malt1 ubiquitination triggers NF-kappaB signaling upon T-cell activation
    • Oeckinghaus A, et al. Malt1 ubiquitination triggers NF-kappaB signaling upon T-cell activation. EMBO J 2007 26 : 4634 4645.
    • (2007) EMBO J , vol.26 , pp. 4634-4645
    • Oeckinghaus, A.1
  • 70
    • 39449085547 scopus 로고    scopus 로고
    • The proteolytic activity of the paracaspase MALT1 is key in T cell activation
    • Rebeaud F, et al. The proteolytic activity of the paracaspase MALT1 is key in T cell activation. Nat Immunol 2008 9 : 272 281.
    • (2008) Nat Immunol , vol.9 , pp. 272-281
    • Rebeaud, F.1
  • 71
    • 39449131430 scopus 로고    scopus 로고
    • T cell antigen receptor stimulation induces MALT1 paracaspase-mediated cleavage of the NF-kappaB inhibitor A20
    • Coornaert B, et al. T cell antigen receptor stimulation induces MALT1 paracaspase-mediated cleavage of the NF-kappaB inhibitor A20. Nat Immunol 2008 9 : 263 271.
    • (2008) Nat Immunol , vol.9 , pp. 263-271
    • Coornaert, B.1
  • 72
    • 48349125069 scopus 로고    scopus 로고
    • The paracaspase MALT1 controls caspase-8 activation during lymphocyte proliferation
    • Kawadler H, Gantz MA, Riley JL, Yang X. The paracaspase MALT1 controls caspase-8 activation during lymphocyte proliferation. Mol Cell 2008 31 : 415 421.
    • (2008) Mol Cell , vol.31 , pp. 415-421
    • Kawadler, H.1    Gantz, M.A.2    Riley, J.L.3    Yang, X.4
  • 73
    • 20044368626 scopus 로고    scopus 로고
    • Requirement for caspase-8 in NF-kappaB activation by antigen receptor
    • Su H, et al. Requirement for caspase-8 in NF-kappaB activation by antigen receptor. Science 2005 307 : 1465 1468.
    • (2005) Science , vol.307 , pp. 1465-1468
    • Su, H.1
  • 74
    • 33748460821 scopus 로고    scopus 로고
    • TRAF6 is a T cell-intrinsic negative regulator required for the maintenance of immune homeostasis
    • King CG, et al. TRAF6 is a T cell-intrinsic negative regulator required for the maintenance of immune homeostasis. Nat Med 2006 12 : 1088 1092.
    • (2006) Nat Med , vol.12 , pp. 1088-1092
    • King, C.G.1
  • 75
    • 47249087279 scopus 로고    scopus 로고
    • Cutting edge: K63-linked polyubiquitination of NEMO modulates TLR signaling and inflammation in vivo
    • Ni CY, et al. Cutting edge: K63-linked polyubiquitination of NEMO modulates TLR signaling and inflammation in vivo. J Immunol 2008 180 : 7107 7111.
    • (2008) J Immunol , vol.180 , pp. 7107-7111
    • Ni, C.Y.1
  • 76
    • 0033537719 scopus 로고    scopus 로고
    • Positive and negative regulation of IkappaB kinase activity through IKKbeta subunit phosphorylation
    • Delhase M, Hayakawa M, Chen Y, Karin M. Positive and negative regulation of IkappaB kinase activity through IKKbeta subunit phosphorylation. Science 1999 284 : 309 313.
    • (1999) Science , vol.284 , pp. 309-313
    • Delhase, M.1    Hayakawa, M.2    Chen, Y.3    Karin, M.4
  • 77
    • 0032583947 scopus 로고    scopus 로고
    • NF-kappaB-inducing kinase activates IKK-alpha by phosphorylation of Ser-176
    • Ling L, Cao Z, Goeddel DV. NF-kappaB-inducing kinase activates IKK-alpha by phosphorylation of Ser-176. Proc Natl Acad Sci USA 1998 95 : 3792 3797.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 3792-3797
    • Ling, L.1    Cao, Z.2    Goeddel, D.V.3
  • 78
    • 0033580466 scopus 로고    scopus 로고
    • The kinase TAK1 can activate the NIK-I kappaB as well as the MAP kinase cascade in the IL-1 signalling pathway
    • Ninomiya-Tsuji J, Kishimoto K, Hiyama A, Inoue J, Cao Z, Matsumoto K. The kinase TAK1 can activate the NIK-I kappaB as well as the MAP kinase cascade in the IL-1 signalling pathway. Nature 1999 398 : 252 256.
    • (1999) Nature , vol.398 , pp. 252-256
    • Ninomiya-Tsuji, J.1    Kishimoto, K.2    Hiyama, A.3    Inoue, J.4    Cao, Z.5    Matsumoto, K.6
  • 80
    • 27544434183 scopus 로고    scopus 로고
    • Essential function for the kinase TAK1 in innate and adaptive immune responses
    • Sato S, et al. Essential function for the kinase TAK1 in innate and adaptive immune responses. Nat Immunol 2005 6 : 1087 1095.
    • (2005) Nat Immunol , vol.6 , pp. 1087-1095
    • Sato, S.1
  • 81
    • 27744577296 scopus 로고    scopus 로고
    • TAK1, but not TAB1 or TAB2, plays an essential role in multiple signaling pathways in vivo
    • Shim JH, et al. TAK1, but not TAB1 or TAB2, plays an essential role in multiple signaling pathways in vivo. Genes Dev 2005 19 : 2668 2681.
    • (2005) Genes Dev , vol.19 , pp. 2668-2681
    • Shim, J.H.1
  • 82
    • 33746857795 scopus 로고    scopus 로고
    • Essential role of TAK1 in thymocyte development and activation
    • Liu HH, Xie M, Schneider MD, Chen ZJ. Essential role of TAK1 in thymocyte development and activation. Proc Natl Acad Sci USA 2006 103 : 11677 11682.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 11677-11682
    • Liu, H.H.1    Xie, M.2    Schneider, M.D.3    Chen, Z.J.4
  • 83
    • 33748999526 scopus 로고    scopus 로고
    • TAK1 is indispensable for development of T cells and prevention of colitis by the generation of regulatory T cells
    • Sato S, et al. TAK1 is indispensable for development of T cells and prevention of colitis by the generation of regulatory T cells. Int Immunol 2006 18 : 1405 1411.
    • (2006) Int Immunol , vol.18 , pp. 1405-1411
    • Sato, S.1
  • 84
    • 33746111852 scopus 로고    scopus 로고
    • The kinase TAK1 integrates antigen and cytokine receptor signaling for T cell development, survival and function
    • Wan YY, Chi H, Xie M, Schneider MD, Flavell RA. The kinase TAK1 integrates antigen and cytokine receptor signaling for T cell development, survival and function. Nat Immunol 2006 7 : 851 858.
    • (2006) Nat Immunol , vol.7 , pp. 851-858
    • Wan, Y.Y.1    Chi, H.2    Xie, M.3    Schneider, M.D.4    Flavell, R.A.5
  • 85
    • 32044447161 scopus 로고    scopus 로고
    • The E3 ubiquitin ligase itch couples JNK activation to TNFalpha-induced cell death by inducing c-FLIP(L) turnover
    • Chang L, et al. The E3 ubiquitin ligase itch couples JNK activation to TNFalpha-induced cell death by inducing c-FLIP(L) turnover. Cell 2006 124 : 601 613.
    • (2006) Cell , vol.124 , pp. 601-613
    • Chang, L.1
  • 86
    • 0028291525 scopus 로고
    • JNK is involved in signal integration during costimulation of T lymphocytes
    • Su B, Jacinto E, Hibi M, Kallunki T, Karin M, Ben-Neriah Y. JNK is involved in signal integration during costimulation of T lymphocytes. Cell 1994 77 : 727 736.
    • (1994) Cell , vol.77 , pp. 727-736
    • Su, B.1    Jacinto, E.2    Hibi, M.3    Kallunki, T.4    Karin, M.5    Ben-Neriah, Y.6
  • 88
    • 0029885419 scopus 로고    scopus 로고
    • Selective interaction of JNK protein kinase isoforms with transcription factors
    • Gupta S, et al. Selective interaction of JNK protein kinase isoforms with transcription factors. EMBO J 1996 15 : 2760 2770.
    • (1996) EMBO J , vol.15 , pp. 2760-2770
    • Gupta, S.1
  • 89
    • 0028609209 scopus 로고
    • JNK2 contains a specificity-determining region responsible for efficient c-Jun binding and phosphorylation
    • Kallunki T, et al. JNK2 contains a specificity-determining region responsible for efficient c-Jun binding and phosphorylation. Genes Dev 1994 8 : 2996 3007.
    • (1994) Genes Dev , vol.8 , pp. 2996-3007
    • Kallunki, T.1
  • 91
    • 0034604093 scopus 로고    scopus 로고
    • JNK is required for effector T-cell function but not for T-cell activation
    • Dong C, et al. JNK is required for effector T-cell function but not for T-cell activation. Nature 2000 405 : 91 94.
    • (2000) Nature , vol.405 , pp. 91-94
    • Dong, C.1
  • 92
    • 0032191173 scopus 로고    scopus 로고
    • Differentiation of CD4+ T cells to Th1 cells requires MAP kinase JNK2
    • Yang DD, et al. Differentiation of CD4+ T cells to Th1 cells requires MAP kinase JNK2. Immunity 1998 9 : 575 585.
    • (1998) Immunity , vol.9 , pp. 575-585
    • Yang, D.D.1
  • 93
    • 0034598346 scopus 로고    scopus 로고
    • Regulation of c-Jun NH(2)-terminal kinase (Jnk) gene expression during T cell activation
    • Weiss L, Whitmarsh AJ, Yang DD, Rincon M, Davis RJ, Flavell RA. Regulation of c-Jun NH(2)-terminal kinase (Jnk) gene expression during T cell activation. J Exp Med 2000 191 : 139 146.
    • (2000) J Exp Med , vol.191 , pp. 139-146
    • Weiss, L.1    Whitmarsh, A.J.2    Yang, D.D.3    Rincon, M.4    Davis, R.J.5    Flavell, R.A.6
  • 94
    • 0029829562 scopus 로고    scopus 로고
    • Phosphorylation-dependent targeting of c-Jun ubiquitination by Jun N-kinase
    • Fuchs SY, Dolan L, Davis RJ, Ronai Z. Phosphorylation-dependent targeting of c-Jun ubiquitination by Jun N-kinase. Oncogene 1996 13 : 1531 1535.
    • (1996) Oncogene , vol.13 , pp. 1531-1535
    • Fuchs, S.Y.1    Dolan, L.2    Davis, R.J.3    Ronai, Z.4
  • 95
    • 0031283180 scopus 로고    scopus 로고
    • C-Jun NH2-terminal kinases target the ubiquitination of their associated transcription factors
    • Fuchs SY, Xie B, Adler V, Fried VA, Davis RJ, Ronai Z. c-Jun NH2-terminal kinases target the ubiquitination of their associated transcription factors. J Biol Chem 1997 272 : 32163 32168.
    • (1997) J Biol Chem , vol.272 , pp. 32163-32168
    • Fuchs, S.Y.1    Xie, B.2    Adler, V.3    Fried, V.A.4    Davis, R.J.5    Ronai, Z.6
  • 96
    • 0028329953 scopus 로고
    • JNK1: A protein kinase stimulated by UV light and Ha-Ras that binds and phosphorylates the c-Jun activation domain
    • Derijard B, et al. JNK1: a protein kinase stimulated by UV light and Ha-Ras that binds and phosphorylates the c-Jun activation domain. Cell 1994 76 : 1025 1037.
    • (1994) Cell , vol.76 , pp. 1025-1037
    • Derijard, B.1
  • 97
    • 0034644522 scopus 로고    scopus 로고
    • Signal transduction by the JNK group of MAP kinases
    • Davis RJ. Signal transduction by the JNK group of MAP kinases. Cell 2000 103 : 239 252.
    • (2000) Cell , vol.103 , pp. 239-252
    • Davis, R.J.1
  • 98
    • 34248563299 scopus 로고    scopus 로고
    • Role of mitogen-activated protein kinase kinase kinases in signal integration
    • Cuevas BD, Abell AN, Johnson GL. Role of mitogen-activated protein kinase kinase kinases in signal integration. Oncogene 2007 26 : 3159 3171.
    • (2007) Oncogene , vol.26 , pp. 3159-3171
    • Cuevas, B.D.1    Abell, A.N.2    Johnson, G.L.3
  • 99
    • 0036098552 scopus 로고    scopus 로고
    • AP-1 as a regulator of cell life and death
    • Shaulian E, Karin M. AP-1 as a regulator of cell life and death. Nat Cell Biol 2002 4 : E131 E136.
    • (2002) Nat Cell Biol , vol.4
    • Shaulian, E.1    Karin, M.2
  • 100
    • 0242691046 scopus 로고    scopus 로고
    • AP-1: A double-edged sword in tumorigenesis
    • Eferl R, Wagner EF. AP-1: a double-edged sword in tumorigenesis. Nat Rev Cancer 2003 3 : 859 868.
    • (2003) Nat Rev Cancer , vol.3 , pp. 859-868
    • Eferl, R.1    Wagner, E.F.2
  • 101
    • 0035971493 scopus 로고    scopus 로고
    • AP-1 in cell proliferation and survival
    • Shaulian E, Karin M. AP-1 in cell proliferation and survival. Oncogene 2001 20 : 2390 2400.
    • (2001) Oncogene , vol.20 , pp. 2390-2400
    • Shaulian, E.1    Karin, M.2
  • 102
    • 18444369000 scopus 로고    scopus 로고
    • Aberrantly expressed c-Jun and JunB are a hallmark of Hodgkin lymphoma cells, stimulate proliferation and synergize with NF-kappa B
    • Mathas S, et al. Aberrantly expressed c-Jun and JunB are a hallmark of Hodgkin lymphoma cells, stimulate proliferation and synergize with NF-kappa B. EMBO J 2002 21 : 4104 4113.
    • (2002) EMBO J , vol.21 , pp. 4104-4113
    • Mathas, S.1
  • 103
    • 8744307100 scopus 로고    scopus 로고
    • Constitutive expression of the AP-1 transcription factors c-jun, junD, junB, and c-fos and the marginal zone B-cell transcription factor Notch2 in splenic marginal zone lymphoma
    • Troen G, et al. Constitutive expression of the AP-1 transcription factors c-jun, junD, junB, and c-fos and the marginal zone B-cell transcription factor Notch2 in splenic marginal zone lymphoma. J Mol Diagn 2004 6 : 297 307.
    • (2004) J Mol Diagn , vol.6 , pp. 297-307
    • Troen, G.1
  • 104
    • 34548821219 scopus 로고    scopus 로고
    • NPM-ALK oncogenic kinase promotes cell-cycle progression through activation of JNK/cJun signaling in anaplastic large-cell lymphoma
    • Leventaki V, et al. NPM-ALK oncogenic kinase promotes cell-cycle progression through activation of JNK/cJun signaling in anaplastic large-cell lymphoma. Blood 2007 110 : 1621 1630.
    • (2007) Blood , vol.110 , pp. 1621-1630
    • Leventaki, V.1
  • 105
    • 0027407940 scopus 로고
    • Regulation of c-jun gene expression in human T lymphocytes
    • Chauhan D, et al. Regulation of c-jun gene expression in human T lymphocytes. Blood 1993 81 : 1540 1548.
    • (1993) Blood , vol.81 , pp. 1540-1548
    • Chauhan, D.1
  • 106
    • 0024276523 scopus 로고
    • The jun proto-oncogene is positively autoregulated by its product, Jun/AP-1
    • Angel P, Hattori K, Smeal T, Karin M. The jun proto-oncogene is positively autoregulated by its product, Jun/AP-1. Cell 1988 55 : 875 885.
    • (1988) Cell , vol.55 , pp. 875-885
    • Angel, P.1    Hattori, K.2    Smeal, T.3    Karin, M.4
  • 107
    • 32644468347 scopus 로고    scopus 로고
    • Ubiquitin chains in the ladder of MAPK signaling
    • Laine A, Ronai Z. Ubiquitin chains in the ladder of MAPK signaling. Sci STKE 2005 2005 : re5.
    • (2005) Sci STKE , vol.2005 , pp. 5
    • Laine, A.1    Ronai, Z.2
  • 108
    • 4444341881 scopus 로고    scopus 로고
    • Distinct roles for JNK1 and JNK2 in regulating JNK activity and c-Jun-dependent cell proliferation
    • Sabapathy K, Hochedlinger K, Nam SY, Bauer A, Karin M, Wagner EF. Distinct roles for JNK1 and JNK2 in regulating JNK activity and c-Jun-dependent cell proliferation. Mol Cell 2004 15 : 713 725.
    • (2004) Mol Cell , vol.15 , pp. 713-725
    • Sabapathy, K.1    Hochedlinger, K.2    Nam, S.Y.3    Bauer, A.4    Karin, M.5    Wagner, E.F.6
  • 109
    • 0031023756 scopus 로고    scopus 로고
    • Reduced ubiquitin-dependent degradation of c-Jun after phosphorylation by MAP kinases
    • Musti AM, Treier M, Bohmann D. Reduced ubiquitin-dependent degradation of c-Jun after phosphorylation by MAP kinases. Science 1997 275 : 400 402.
    • (1997) Science , vol.275 , pp. 400-402
    • Musti, A.M.1    Treier, M.2    Bohmann, D.3
  • 110
    • 17144371848 scopus 로고    scopus 로고
    • JNK2: A negative regulator of cellular proliferation
    • Sabapathy K, Wagner EF. JNK2: a negative regulator of cellular proliferation. Cell Cycle 2004 3 : 1520 1523.
    • (2004) Cell Cycle , vol.3 , pp. 1520-1523
    • Sabapathy, K.1    Wagner, E.F.2
  • 111
    • 5044225158 scopus 로고    scopus 로고
    • Jun turnover is controlled through JNK-dependent phosphorylation of the E3 ligase Itch
    • Gao M, et al. Jun turnover is controlled through JNK-dependent phosphorylation of the E3 ligase Itch. Science 2004 306 : 271 275.
    • (2004) Science , vol.306 , pp. 271-275
    • Gao, M.1
  • 112
    • 38549086019 scopus 로고    scopus 로고
    • FBW7 ubiquitin ligase: A tumour suppressor at the crossroads of cell division, growth and differentiation
    • Welcker M, Clurman BE. FBW7 ubiquitin ligase: a tumour suppressor at the crossroads of cell division, growth and differentiation. Nat Rev Cancer 2008 8 : 83 93.
    • (2008) Nat Rev Cancer , vol.8 , pp. 83-93
    • Welcker, M.1    Clurman, B.E.2
  • 113
    • 0038433303 scopus 로고    scopus 로고
    • JunD mediates survival signaling by the JNK signal transduction pathway
    • Lamb JA, Ventura JJ, Hess P, Flavell RA, Davis RJ. JunD mediates survival signaling by the JNK signal transduction pathway. Mol Cell 2003 11 : 1479 1489.
    • (2003) Mol Cell , vol.11 , pp. 1479-1489
    • Lamb, J.A.1    Ventura, J.J.2    Hess, P.3    Flavell, R.A.4    Davis, R.J.5
  • 114
    • 0037119354 scopus 로고    scopus 로고
    • Regulation of two JunD isoforms by Jun N-terminal kinases
    • Yazgan O, Pfarr CM. Regulation of two JunD isoforms by Jun N-terminal kinases. J Biol Chem 2002 277 : 29710 29718.
    • (2002) J Biol Chem , vol.277 , pp. 29710-29718
    • Yazgan, O.1    Pfarr, C.M.2
  • 115
    • 0028409131 scopus 로고
    • Generation of normal T and B lymphocytes by c-jun deficient embryonic stem cells
    • Chen J, Stewart V, Spyrou G, Hilberg F, Wagner EF, Alt FW. Generation of normal T and B lymphocytes by c-jun deficient embryonic stem cells. Immunity 1994 1 : 65 72.
    • (1994) Immunity , vol.1 , pp. 65-72
    • Chen, J.1    Stewart, V.2    Spyrou, G.3    Hilberg, F.4    Wagner, E.F.5    Alt, F.W.6
  • 116
    • 33744464235 scopus 로고    scopus 로고
    • Identification of subtype-specific genomic alterations in aggressive adult T-cell leukemia/lymphoma
    • Oshiro A, et al. Identification of subtype-specific genomic alterations in aggressive adult T-cell leukemia/lymphoma. Blood 2006 107 : 4500 4507.
    • (2006) Blood , vol.107 , pp. 4500-4507
    • Oshiro, A.1
  • 117
    • 27244458985 scopus 로고    scopus 로고
    • Overexpression of caspase recruitment domain (CARD) membrane-associated guanylate kinase 1 (CARMA1) and CARD9 in primary gastric B-cell lymphoma
    • Nakamura S, et al. Overexpression of caspase recruitment domain (CARD) membrane-associated guanylate kinase 1 (CARMA1) and CARD9 in primary gastric B-cell lymphoma. Cancer 2005 104 : 1885 1893.
    • (2005) Cancer , vol.104 , pp. 1885-1893
    • Nakamura, S.1
  • 118
    • 33645306041 scopus 로고    scopus 로고
    • A loss-of-function RNA interference screen for molecular targets in cancer
    • Ngo VN, et al. A loss-of-function RNA interference screen for molecular targets in cancer. Nature 2006 441 : 106 110.
    • (2006) Nature , vol.441 , pp. 106-110
    • Ngo, V.N.1
  • 119
    • 41149136296 scopus 로고    scopus 로고
    • Oncogenic CARD11 mutations in human diffuse large B cell lymphoma
    • Lenz G, et al. Oncogenic CARD11 mutations in human diffuse large B cell lymphoma. Science 2008 319 : 1676 1679.
    • (2008) Science , vol.319 , pp. 1676-1679
    • Lenz, G.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.