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Volumn 14, Issue 3, 2010, Pages 710-725

HSP70 interacts with TRAF2 and differentially regulates TNFα signalling in human colon cancer cells

Author keywords

Apoptosis; HSP70; JNK; Lipid raft; NF B; TNF ; TRAF2; Ubiquitination

Indexed keywords

HEAT SHOCK PROTEIN 70; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; STRESS ACTIVATED PROTEIN KINASE; TUMOR NECROSIS FACTOR ALPHA; TUMOR NECROSIS FACTOR RECEPTOR 1; TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED DEATH DOMAIN PROTEIN; TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED FACTOR 2;

EID: 77953520542     PISSN: 15821838     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1582-4934.2009.00716.x     Document Type: Article
Times cited : (18)

References (59)
  • 1
    • 85047692516 scopus 로고    scopus 로고
    • Signalling pathways of the TNF superfamily: a double-edged sword
    • Aggarwal BB. Signalling pathways of the TNF superfamily: a double-edged sword. Nat Rev Immunol. 2003, 3:745-56.
    • (2003) Nat Rev Immunol. , vol.3 , pp. 745-756
    • Aggarwal, B.B.1
  • 2
    • 0037204948 scopus 로고    scopus 로고
    • TNF-R1 signaling: a beautiful pathway
    • Chen G, Goeddel DV. TNF-R1 signaling: a beautiful pathway. Science. 2002, 296:1634-5.
    • (2002) Science. , vol.296 , pp. 1634-1635
    • Chen, G.1    Goeddel, D.V.2
  • 3
    • 0027275490 scopus 로고
    • A novel domain within the 55 kD TNF receptor signals cell death
    • Tartaglia LA, Ayres TM, Wong GH. A novel domain within the 55 kD TNF receptor signals cell death. Cell. 1993, 74:845-53.
    • (1993) Cell. , vol.74 , pp. 845-853
    • Tartaglia, L.A.1    Ayres, T.M.2    Wong, G.H.3
  • 4
    • 0029007855 scopus 로고
    • The TNF receptor 1-associated protein TRADD signals cell death and NF-kappa B activation
    • Hsu H, Xiong J, Goeddel DV. The TNF receptor 1-associated protein TRADD signals cell death and NF-kappa B activation. Cell. 1995, 81:495-504.
    • (1995) Cell. , vol.81 , pp. 495-504
    • Hsu, H.1    Xiong, J.2    Goeddel, D.V.3
  • 5
    • 0030032106 scopus 로고    scopus 로고
    • TRADD-TRAF2 and TRADD-FADD interactions define two distinct TNF receptor 1 signal transduction pathways
    • Hsu H, Shu HB, Pan MG. TRADD-TRAF2 and TRADD-FADD interactions define two distinct TNF receptor 1 signal transduction pathways. Cell. 1996, 84:299-308.
    • (1996) Cell. , vol.84 , pp. 299-308
    • Hsu, H.1    Shu, H.B.2    Pan, M.G.3
  • 6
    • 4444341939 scopus 로고    scopus 로고
    • Compartmentalization of TNF receptor 1 signaling: internalized TNF receptosomes as death signaling vesicles
    • Schneider-Brachert W, Tchikov V, Neumeyer J. Compartmentalization of TNF receptor 1 signaling: internalized TNF receptosomes as death signaling vesicles. Immunity. 2004, 21:415-28.
    • (2004) Immunity. , vol.21 , pp. 415-428
    • Schneider-Brachert, W.1    Tchikov, V.2    Neumeyer, J.3
  • 7
    • 0030298294 scopus 로고    scopus 로고
    • Dissection of TNF receptor 1 effector functions: JNK activation is not linked to apoptosis while NF-kappaB activation prevents cell death
    • Liu ZG, Hsu H, Goeddel DV. Dissection of TNF receptor 1 effector functions: JNK activation is not linked to apoptosis while NF-kappaB activation prevents cell death. Cell. 1996, 87:565-76.
    • (1996) Cell. , vol.87 , pp. 565-576
    • Liu, Z.G.1    Hsu, H.2    Goeddel, D.V.3
  • 8
    • 0029858348 scopus 로고    scopus 로고
    • RIP mediates tumor necrosis factor receptor 1 activation of NF-kappaB but not Fas/APO-1-initiated apoptosis
    • Ting AT, Pimentel-Muiños FX, Seed B. RIP mediates tumor necrosis factor receptor 1 activation of NF-kappaB but not Fas/APO-1-initiated apoptosis. EMBO J. 1996, 15:6189-96.
    • (1996) EMBO J. , vol.15 , pp. 6189-6196
    • Ting, A.T.1    Pimentel-Muiños, F.X.2    Seed, B.3
  • 9
    • 0032033132 scopus 로고    scopus 로고
    • The death domain kinase RIP mediates the TNF-induced NF-kappaB signal
    • Kelliher MA, Grimm S, Ishida Y. The death domain kinase RIP mediates the TNF-induced NF-kappaB signal. Immunity. 1998, 8:297-303.
    • (1998) Immunity. , vol.8 , pp. 297-303
    • Kelliher, M.A.1    Grimm, S.2    Ishida, Y.3
  • 10
    • 0033725155 scopus 로고    scopus 로고
    • The distinct roles of TRAF2 and RIP in IKK activation by TNF-R1: TRAF2 recruits IKK to TNF-R1 while RIP mediates IKK activation
    • Devin A, Cook A, Lin Y. The distinct roles of TRAF2 and RIP in IKK activation by TNF-R1: TRAF2 recruits IKK to TNF-R1 while RIP mediates IKK activation. Immunity. 2000, 12:419-29.
    • (2000) Immunity. , vol.12 , pp. 419-429
    • Devin, A.1    Cook, A.2    Lin, Y.3
  • 11
    • 0033198702 scopus 로고    scopus 로고
    • TRAF2 deficiency results in hyperactivity of certain TNFR1 signals and impairment of CD40-mediated responses
    • Nguyen LT, Duncan GS, Mirtsos C. TRAF2 deficiency results in hyperactivity of certain TNFR1 signals and impairment of CD40-mediated responses. Immunity. 1999, 11:379-89.
    • (1999) Immunity. , vol.11 , pp. 379-389
    • Nguyen, L.T.1    Duncan, G.S.2    Mirtsos, C.3
  • 12
    • 0033712615 scopus 로고    scopus 로고
    • Recruitment of the IKK signalosome to the p55 TNF receptor: RIP and A20 bind to NEMO (IKKgamma) upon receptor stimulation
    • Zhang SQ, Kovalenko A, Cantarella G. Recruitment of the IKK signalosome to the p55 TNF receptor: RIP and A20 bind to NEMO (IKKgamma) upon receptor stimulation. Immunity. 2000, 12:301-11.
    • (2000) Immunity. , vol.12 , pp. 301-311
    • Zhang, S.Q.1    Kovalenko, A.2    Cantarella, G.3
  • 13
    • 0029949257 scopus 로고    scopus 로고
    • TNF-dependent recruitment of the protein kinase RIP to the TNF receptor-1 signaling complex
    • Hsu H, Huang J, Shu HB. TNF-dependent recruitment of the protein kinase RIP to the TNF receptor-1 signaling complex. Immunity. 1996, 4:387-96.
    • (1996) Immunity. , vol.4 , pp. 387-396
    • Hsu, H.1    Huang, J.2    Shu, H.B.3
  • 14
    • 33646034316 scopus 로고    scopus 로고
    • Activation of IKK by TNFalpha requires site-specific ubiquitination of RIP1 and polyubiquitin binding by NEMO
    • Ea CK, Deng L, Xia ZP. Activation of IKK by TNFalpha requires site-specific ubiquitination of RIP1 and polyubiquitin binding by NEMO. Mol Cell. 2006, 22:245-57.
    • (2006) Mol Cell. , vol.22 , pp. 245-257
    • Ea, C.K.1    Deng, L.2    Xia, Z.P.3
  • 15
    • 0032158987 scopus 로고    scopus 로고
    • ASK1 is essential for JNK/SAPK activation by TRAF2
    • Nishitoh H, Saitoh M, Mochida Y. ASK1 is essential for JNK/SAPK activation by TRAF2. Mol Cell. 1998, 2:389-95.
    • (1998) Mol Cell. , vol.2 , pp. 389-395
    • Nishitoh, H.1    Saitoh, M.2    Mochida, Y.3
  • 16
    • 0033554554 scopus 로고    scopus 로고
    • Mediation of TNF receptor-associated factor effector functions by apoptosis signal-regulating kinase-1 (ASK1)
    • Hoeflich KP, Yeh WC, Yao Z. Mediation of TNF receptor-associated factor effector functions by apoptosis signal-regulating kinase-1 (ASK1). Oncogene. 1999, 18:5814-20.
    • (1999) Oncogene. , vol.18 , pp. 5814-5820
    • Hoeflich, K.P.1    Yeh, W.C.2    Yao, Z.3
  • 17
    • 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. The kinase TAK1 can activate the NIK-I kappaB as well as the MAP kinase cascade in the IL-1 signalling pathway. Nature. 1999, 398:252-6.
    • (1999) Nature. , vol.398 , pp. 252-256
    • Ninomiya-Tsuji, J.1    Kishimoto, K.2    Hiyama, A.3
  • 18
    • 0033537866 scopus 로고    scopus 로고
    • Functional interactions of transforming growth factor beta-activated kinase 1 with IkappaB kinases to stimulate NF-kappaB activation
    • Sakurai H, Miyoshi H, Toriumi W. Functional interactions of transforming growth factor beta-activated kinase 1 with IkappaB kinases to stimulate NF-kappaB activation. J Biol Chem. 1999, 274:10641-8.
    • (1999) J Biol Chem. , vol.274 , pp. 10641-10648
    • Sakurai, H.1    Miyoshi, H.2    Toriumi, W.3
  • 19
    • 27744577296 scopus 로고    scopus 로고
    • TAK1, but not TAB1 or TAB2, plays an essential role in multiple signaling pathways in vivo
    • Shim JH, Xiao C, Paschal AE. TAK1, but not TAB1 or TAB2, plays an essential role in multiple signaling pathways in vivo. Genes Dev. 2005, 19:2668-81.
    • (2005) Genes Dev. , vol.19 , pp. 2668-2681
    • Shim, J.H.1    Xiao, C.2    Paschal, A.E.3
  • 20
    • 50049125047 scopus 로고    scopus 로고
    • Function of TRADD in tumor necrosis factor receptor 1 signaling and in TRIF-dependent inflammatory responses
    • Ermolaeva MA, Michallet MC, Papadopoulou N. Function of TRADD in tumor necrosis factor receptor 1 signaling and in TRIF-dependent inflammatory responses. Nat Immunol. 2008, 9:1037-46.
    • (2008) Nat Immunol. , vol.9 , pp. 1037-1046
    • Ermolaeva, M.A.1    Michallet, M.C.2    Papadopoulou, N.3
  • 21
    • 7144263731 scopus 로고    scopus 로고
    • FADD: essential for embryo development and signaling from some, but not all, inducers of apoptosis
    • Yeh WC, Pompa JL, McCurrach ME. FADD: essential for embryo development and signaling from some, but not all, inducers of apoptosis. Science. 1998, 279:1954-8.
    • (1998) Science. , vol.279 , pp. 1954-1958
    • Yeh, W.C.1    Pompa, J.L.2    McCurrach, M.E.3
  • 22
    • 0035883151 scopus 로고    scopus 로고
    • NF-kappaB signaling pathways in mammalian and insect innate immunity
    • Silverman N, Maniatis T. NF-kappaB signaling pathways in mammalian and insect innate immunity. Genes Dev. 2001, 15:2321-42.
    • (2001) Genes Dev. , vol.15 , pp. 2321-2342
    • Silverman, N.1    Maniatis, T.2
  • 23
    • 0030780804 scopus 로고    scopus 로고
    • Absence of excitotoxicity-induced apoptosis in the hippocampus of mice lacking the Jnk3 gene
    • Yang DD, Kuan CY, Whitmarsh AJ. Absence of excitotoxicity-induced apoptosis in the hippocampus of mice lacking the Jnk3 gene. Nature. 1997, 389:865-70.
    • (1997) Nature. , vol.389 , pp. 865-870
    • Yang, D.D.1    Kuan, C.Y.2    Whitmarsh, A.J.3
  • 24
    • 0032509479 scopus 로고    scopus 로고
    • Defective T cell differentiation in the absence of Jnk1
    • Dong C, Yang DD, Wysk M. Defective T cell differentiation in the absence of Jnk1. Science. 1998, 282:2092-5.
    • (1998) Science. , vol.282 , pp. 2092-2095
    • Dong, C.1    Yang, D.D.2    Wysk, M.3
  • 25
    • 0033545386 scopus 로고    scopus 로고
    • JNK2 is required for efficient T-cell activation and apoptosis but not for normal lymphocyte development
    • Sabapathy K, Hu Y, Kallunki T. JNK2 is required for efficient T-cell activation and apoptosis but not for normal lymphocyte development. Curr Biol. 1999, 9:116-125.
    • (1999) Curr Biol. , vol.9 , pp. 116-125
    • Sabapathy, K.1    Hu, Y.2    Kallunki, T.3
  • 26
    • 0034607702 scopus 로고    scopus 로고
    • Requirement of JNK for stress-induced activation of the cytochrome c-mediated death pathway
    • Tournier C, Hess P, Yang DD. Requirement of JNK for stress-induced activation of the cytochrome c-mediated death pathway. Science. 2000, 288:870-4.
    • (2000) Science. , vol.288 , pp. 870-874
    • Tournier, C.1    Hess, P.2    Yang, D.D.3
  • 27
    • 0038719671 scopus 로고    scopus 로고
    • JNK-dependent release of mitochondrial protein, Smac, during apoptosis in multiple myeloma (MM) cells
    • Chauhan D, Li G, Hideshima T. JNK-dependent release of mitochondrial protein, Smac, during apoptosis in multiple myeloma (MM) cells. J Biol Chem. 2003, 278:17593-6.
    • (2003) J Biol Chem. , vol.278 , pp. 17593-17596
    • Chauhan, D.1    Li, G.2    Hideshima, T.3
  • 28
    • 0031463025 scopus 로고    scopus 로고
    • Early lethality, functional NF-kappaB activation, and increased sensitivity to TNF-induced cell death in TRAF2-deficient mice
    • Yeh WC, Shahinian A, Speiser D. Early lethality, functional NF-kappaB activation, and increased sensitivity to TNF-induced cell death in TRAF2-deficient mice. Immunity. 1997, 7:715-25.
    • (1997) Immunity. , vol.7 , pp. 715-725
    • Yeh, W.C.1    Shahinian, A.2    Speiser, D.3
  • 29
    • 44149104599 scopus 로고    scopus 로고
    • Heat shock proteins: essential proteins for apoptosis regulation
    • Lanneau D, Brunet M, Frisan E. Heat shock proteins: essential proteins for apoptosis regulation. J Cell Mol Med. 2008, 12:743-61.
    • (2008) J Cell Mol Med. , vol.12 , pp. 743-761
    • Lanneau, D.1    Brunet, M.2    Frisan, E.3
  • 30
    • 3242879188 scopus 로고    scopus 로고
    • " The stress of dying": the role of heat shock proteins in the regulation of apoptosis
    • Beere HM. " The stress of dying": the role of heat shock proteins in the regulation of apoptosis. J Cell Sci. 2004, 117:2641-51.
    • (2004) J Cell Sci. , vol.117 , pp. 2641-2651
    • Beere, H.M.1
  • 31
    • 26444495615 scopus 로고    scopus 로고
    • Death versus survival: functional interaction between the apoptotic and stress-inducible heat shock protein pathways
    • Beere HM. Death versus survival: functional interaction between the apoptotic and stress-inducible heat shock protein pathways. J Clin Invest. 2005, 115:2633-9.
    • (2005) J Clin Invest. , vol.115 , pp. 2633-2639
    • Beere, H.M.1
  • 32
    • 0034011577 scopus 로고    scopus 로고
    • Sensitization of tumor cells to fas killing through overexpression of heat-shock transcription factor 1
    • Xia W, Voellmy R, Spector NL. Sensitization of tumor cells to fas killing through overexpression of heat-shock transcription factor 1. J Cell Physiol. 2000, 183:425-31.
    • (2000) J Cell Physiol. , vol.183 , pp. 425-431
    • Xia, W.1    Voellmy, R.2    Spector, N.L.3
  • 33
    • 0031570448 scopus 로고    scopus 로고
    • Overexpression of the heat shock protein 70 enhances the TCR/CD3- and Fas/Apo-1/CD95-mediated apoptotic cell death in Jurkat T cells
    • Liossis SN, Ding XZ, Kiang JG. Overexpression of the heat shock protein 70 enhances the TCR/CD3- and Fas/Apo-1/CD95-mediated apoptotic cell death in Jurkat T cells. J Immunol. 1997, 158:5668-75.
    • (1997) J Immunol. , vol.158 , pp. 5668-5675
    • Liossis, S.N.1    Ding, X.Z.2    Kiang, J.G.3
  • 34
    • 0029937051 scopus 로고    scopus 로고
    • Susceptibility of AML cells to in vitro apoptosis correlates with heat shock protein 70 (hsp 70) expression
    • Chant ID, Rose PE, Morris AG. Susceptibility of AML cells to in vitro apoptosis correlates with heat shock protein 70 (hsp 70) expression. Br J Haematol. 1996, 93:898-902.
    • (1996) Br J Haematol. , vol.93 , pp. 898-902
    • Chant, I.D.1    Rose, P.E.2    Morris, A.G.3
  • 35
    • 0032111928 scopus 로고    scopus 로고
    • Pyrrolidine dithiocarbamate activates the heat shock response and thereby induces apoptosis in primed endothelial cells
    • DeMeester SL, Buchman TG, Qiu Y. Pyrrolidine dithiocarbamate activates the heat shock response and thereby induces apoptosis in primed endothelial cells. Shock. 1998, 10:1-6.
    • (1998) Shock. , vol.10 , pp. 1-6
    • DeMeester, S.L.1    Buchman, T.G.2    Qiu, Y.3
  • 36
    • 0037099176 scopus 로고    scopus 로고
    • Relationship between the activation of heat shock factor and the suppression of nuclear factor-kappaB activity in rat hepatocyte cultures treated with cyclosporine A
    • Andrés D, Díez-Fernández C, Castrillo A. Relationship between the activation of heat shock factor and the suppression of nuclear factor-kappaB activity in rat hepatocyte cultures treated with cyclosporine A. Biochem Pharmacol. 2002, 64:247-56.
    • (2002) Biochem Pharmacol. , vol.64 , pp. 247-256
    • Andrés, D.1    Díez-Fernández, C.2    Castrillo, A.3
  • 37
    • 0033551787 scopus 로고    scopus 로고
    • Heat shock inhibits radiation-induced activation of NF-kappaB via inhibition of I-kappaB kinase
    • Curry HA, Clemens RA, Shah S. Heat shock inhibits radiation-induced activation of NF-kappaB via inhibition of I-kappaB kinase. J Biol Chem. 1999, 274:23061-7.
    • (1999) J Biol Chem. , vol.274 , pp. 23061-23067
    • Curry, H.A.1    Clemens, R.A.2    Shah, S.3
  • 38
    • 0031414944 scopus 로고    scopus 로고
    • Suppression of glial nitric oxide synthase induction by heat shock: effects on proteolytic degradation of IkappaB-alpha
    • Feinstein DL, Galea E, Reis DJ. Suppression of glial nitric oxide synthase induction by heat shock: effects on proteolytic degradation of IkappaB-alpha. Nitric Oxide. 1997, 1:167-76.
    • (1997) Nitric Oxide. , vol.1 , pp. 167-176
    • Feinstein, D.L.1    Galea, E.2    Reis, D.J.3
  • 39
    • 0030747256 scopus 로고    scopus 로고
    • Major stress protein Hsp70 interacts with NF-kB regulatory complex in human T-lymphoma cells
    • Guzhova IV, Darieva ZA, Melo AR. Major stress protein Hsp70 interacts with NF-kB regulatory complex in human T-lymphoma cells. Cell Stress Chaperones. 1997, 2:132-9.
    • (1997) Cell Stress Chaperones. , vol.2 , pp. 132-139
    • Guzhova, I.V.1    Darieva, Z.A.2    Melo, A.R.3
  • 40
    • 0034303209 scopus 로고    scopus 로고
    • Heat shock inhibits phosphorylation of I-kappaBalpha
    • Shanley TP, Ryan MA, Eaves-Pyles T. Heat shock inhibits phosphorylation of I-kappaBalpha. Shock. 2000, 14:447-50.
    • (2000) Shock. , vol.14 , pp. 447-450
    • Shanley, T.P.1    Ryan, M.A.2    Eaves-Pyles, T.3
  • 41
    • 2942650958 scopus 로고    scopus 로고
    • Hsp70 promotes TNF-mediated apoptosis by binding IKK gamma and impairing NF-kappa B survival signaling
    • Ran R, Lu A, Zhang L. Hsp70 promotes TNF-mediated apoptosis by binding IKK gamma and impairing NF-kappa B survival signaling. Genes Dev. 2004, 18:1466-81.
    • (2004) Genes Dev. , vol.18 , pp. 1466-1481
    • Ran, R.1    Lu, A.2    Zhang, L.3
  • 42
    • 0034657795 scopus 로고    scopus 로고
    • Anti-inflammatory effect of heat shock protein induction is related to stabilization of I kappa B alpha through preventing I kappa B kinase activation in respiratory epithelial cells
    • Yoo CG, Lee S, Lee CT. Anti-inflammatory effect of heat shock protein induction is related to stabilization of I kappa B alpha through preventing I kappa B kinase activation in respiratory epithelial cells. J Immunol. 2000, 164:5416-23.
    • (2000) J Immunol. , vol.164 , pp. 5416-5423
    • Yoo, C.G.1    Lee, S.2    Lee, C.T.3
  • 43
    • 41949099869 scopus 로고    scopus 로고
    • Dissecting lipid raft facilitated cell signaling pathways in cancer
    • Patra SK. Dissecting lipid raft facilitated cell signaling pathways in cancer. Biochim Biophys Acta. 2008, 1785:182-206.
    • (2008) Biochim Biophys Acta. , vol.1785 , pp. 182-206
    • Patra, S.K.1
  • 44
    • 33845901815 scopus 로고    scopus 로고
    • Lipid rafts: at a crossroad between cell biology and physics
    • Jacobson K, Mouritsen OG, Anderson RG. Lipid rafts: at a crossroad between cell biology and physics. Nat Cell Biol. 2007, 9:7-14.
    • (2007) Nat Cell Biol. , vol.9 , pp. 7-14
    • Jacobson, K.1    Mouritsen, O.G.2    Anderson, R.G.3
  • 45
    • 0033564253 scopus 로고    scopus 로고
    • TNF-alpha-mediated apoptosis is initiated in caveolae-like domains
    • Ko YG, Lee JS, Kang YS. TNF-alpha-mediated apoptosis is initiated in caveolae-like domains. J Immunol. 1999, 162:7217-23.
    • (1999) J Immunol. , vol.162 , pp. 7217-7223
    • Ko, Y.G.1    Lee, J.S.2    Kang, Y.S.3
  • 46
    • 0037090252 scopus 로고    scopus 로고
    • Restricted localization of the TNF receptor CD120a to lipid rafts: a novel role for the death domain
    • Cottin V, Doan JE, Riches DW. Restricted localization of the TNF receptor CD120a to lipid rafts: a novel role for the death domain. J Immunol. 2002, 168:4095-102.
    • (2002) J Immunol. , vol.168 , pp. 4095-4102
    • Cottin, V.1    Doan, J.E.2    Riches, D.W.3
  • 47
    • 0035340071 scopus 로고    scopus 로고
    • A neutral sphingomyelinase resides in sphingolipid-enriched microdomains and is inhibited by the caveolin-scaffolding domain: potential implications in tumour necrosis factor signalling
    • Veldman RJ, Maestre N, Aduib OM. A neutral sphingomyelinase resides in sphingolipid-enriched microdomains and is inhibited by the caveolin-scaffolding domain: potential implications in tumour necrosis factor signalling. Biochem J. 2001, 355:859-68.
    • (2001) Biochem J. , vol.355 , pp. 859-868
    • Veldman, R.J.1    Maestre, N.2    Aduib, O.M.3
  • 48
    • 0038742813 scopus 로고    scopus 로고
    • Recruitment of TNF receptor 1 to lipid rafts is essential for TNFalpha-mediated NF-kappaB activation
    • Legler DF, Micheau O, Doucey MA. Recruitment of TNF receptor 1 to lipid rafts is essential for TNFalpha-mediated NF-kappaB activation. Immunity. 2003, 18:655-64.
    • (2003) Immunity. , vol.18 , pp. 655-664
    • Legler, D.F.1    Micheau, O.2    Doucey, M.A.3
  • 49
    • 30044449755 scopus 로고    scopus 로고
    • TAK1 is recruited to the tumor necrosis factor-alpha (TNF-alpha) receptor 1 complex in a receptor-interacting protein (RIP)-dependent manner and cooperates with MEKK3 leading to NF-kappaB activation
    • Blonska M, Shambharkar PB, Kobayashi M. TAK1 is recruited to the tumor necrosis factor-alpha (TNF-alpha) receptor 1 complex in a receptor-interacting protein (RIP)-dependent manner and cooperates with MEKK3 leading to NF-kappaB activation. J Biol Chem. 2005, 280:43056-63.
    • (2005) J Biol Chem. , vol.280 , pp. 43056-43063
    • Blonska, M.1    Shambharkar, P.B.2    Kobayashi, M.3
  • 50
    • 33845921822 scopus 로고    scopus 로고
    • Spatial compartmentalization of tumor necrosis factor (TNF) receptor 1-dependent signaling pathways in human airway smooth muscle cells. Lipid rafts are essential for TNF-alpha-mediated activation of RhoA but dispensable for the activation of the NF-kappaB and MAPK pathways
    • Hunter I, Nixon GF. Spatial compartmentalization of tumor necrosis factor (TNF) receptor 1-dependent signaling pathways in human airway smooth muscle cells. Lipid rafts are essential for TNF-alpha-mediated activation of RhoA but dispensable for the activation of the NF-kappaB and MAPK pathways. J Biol Chem. 2006, 281:34705-15.
    • (2006) J Biol Chem. , vol.281 , pp. 34705-34715
    • Hunter, I.1    Nixon, G.F.2
  • 51
    • 41149172340 scopus 로고    scopus 로고
    • Phase I clinical trial of autologous ascites-derived exosomes combined with GM-CSF for colorectal cancer
    • Dai S, Wei D, Wu Z. Phase I clinical trial of autologous ascites-derived exosomes combined with GM-CSF for colorectal cancer. Mol Ther. 2008, 16:782-90.
    • (2008) Mol Ther. , vol.16 , pp. 782-790
    • Dai, S.1    Wei, D.2    Wu, Z.3
  • 52
    • 46149125267 scopus 로고    scopus 로고
    • Membrane-associated stress proteins: more than simply chaperones
    • Horváth I, Multhoff G, Sonnleitner A. Membrane-associated stress proteins: more than simply chaperones. Biochim Biophys Acta. 2008, 1778:1653-64.
    • (2008) Biochim Biophys Acta. , vol.1778 , pp. 1653-1664
    • Horváth, I.1    Multhoff, G.2    Sonnleitner, A.3
  • 53
    • 23144449789 scopus 로고    scopus 로고
    • Ubiquitin signalling in the NF-kappaB pathway
    • Chen ZJ. Ubiquitin signalling in the NF-kappaB pathway. Nat Cell Biol. 2005, 7:758-65.
    • (2005) Nat Cell Biol. , vol.7 , pp. 758-765
    • Chen, Z.J.1
  • 54
    • 0038150358 scopus 로고    scopus 로고
    • Tumor necrosis factor (TNF)-induced germinal center kinase-related (GCKR) and stress-activated protein kinase (SAPK) activation depends upon the E2/E3 complex Ubc13-Uev1A/TNF receptor-associated factor 2 (TRAF2)
    • Shi CS, Kehrl JH. Tumor necrosis factor (TNF)-induced germinal center kinase-related (GCKR) and stress-activated protein kinase (SAPK) activation depends upon the E2/E3 complex Ubc13-Uev1A/TNF receptor-associated factor 2 (TRAF2). J Biol Chem. 2003, 278:15429-34.
    • (2003) J Biol Chem. , vol.278 , pp. 15429-15434
    • Shi, C.S.1    Kehrl, J.H.2
  • 55
    • 4043136609 scopus 로고    scopus 로고
    • The kinase activity of Rip1 is not required for tumor necrosis factor-alpha-induced IkappaB kinase or p38 MAP kinase activation or for the ubiquitination of Rip1 by Traf2
    • Lee TH, Shank J, Cusson N. The kinase activity of Rip1 is not required for tumor necrosis factor-alpha-induced IkappaB kinase or p38 MAP kinase activation or for the ubiquitination of Rip1 by Traf2. J Biol Chem. 2004, 279:33185-91.
    • (2004) J Biol Chem. , vol.279 , pp. 33185-33191
    • Lee, T.H.1    Shank, J.2    Cusson, N.3
  • 56
    • 1542380581 scopus 로고    scopus 로고
    • Ubiquitination and translocation of TRAF2 is required for activation of JNK but not of p38 or NF-kappaB
    • Habelhah H, Takahashi S, Cho SG. Ubiquitination and translocation of TRAF2 is required for activation of JNK but not of p38 or NF-kappaB. EMBO J. 2004, 23:322-32.
    • (2004) EMBO J. , vol.23 , pp. 322-332
    • Habelhah, H.1    Takahashi, S.2    Cho, S.G.3
  • 57
    • 0001033803 scopus 로고    scopus 로고
    • Structural basis for self-association and receptor recognition of human TRAF2
    • Park YC, Burkitt V, Villa AR. Structural basis for self-association and receptor recognition of human TRAF2. Nature. 1999, 398:533-8.
    • (1999) Nature. , vol.398 , pp. 533-538
    • Park, Y.C.1    Burkitt, V.2    Villa, A.R.3
  • 58
    • 0033563101 scopus 로고    scopus 로고
    • Signaling by proinflammatory cytokines: oligomerization of TRAF2 and TRAF6 is sufficient for JNK and IKK activation and target gene induction via: an amino-terminal effector domain
    • Baud V, Liu ZG, Bennett B. Signaling by proinflammatory cytokines: oligomerization of TRAF2 and TRAF6 is sufficient for JNK and IKK activation and target gene induction via: an amino-terminal effector domain. Genes Dev. 1999, 13:1297-308.
    • (1999) Genes Dev. , vol.13 , pp. 1297-1308
    • Baud, V.1    Liu, Z.G.2    Bennett, B.3
  • 59
    • 0036840931 scopus 로고    scopus 로고
    • Heat shock protein hsp72 is a negative regulator of apoptosis signal-regulating kinase 1
    • Park HS, Cho SG, Kim CK. Heat shock protein hsp72 is a negative regulator of apoptosis signal-regulating kinase 1. Mol Cell Biol. 2002, 22:7721-30.
    • (2002) Mol Cell Biol. , vol.22 , pp. 7721-7730
    • Park, H.S.1    Cho, S.G.2    Kim, C.K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.