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Volumn 10, Issue 2, 1998, Pages 205-219

Signal transduction by the c-Jun N-terminal kinase (JNK) - From inflammation to development

Author keywords

[No Author keywords available]

Indexed keywords

CYTOKINE; MITOGEN ACTIVATED PROTEIN KINASE; PHOSPHOTRANSFERASE;

EID: 0032054723     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0955-0674(98)80143-9     Document Type: Article
Times cited : (1405)

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    • Dissection of TNF receptor 1 effector functions: JNK activation is not linked to apoptosis while NF-kappaB activation prevents cell death
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    • Liu ZG, Hsu H, Goeddel DV, Karin M. Dissection of TNF receptor 1 effector functions: JNK activation is not linked to apoptosis while NF-kappaB activation prevents cell death. of special interest Nature. 383:1996;716-719 See annotation to [43].
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    • Liu, Z.G.1    Hsu, H.2    Goeddel, D.V.3    Karin, M.4
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    • Activation of SAPK/JNK by TNF receptor 1 through a noncytotoxic TRAF2- dependent pathway
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    • Natoli G, Costanzo A, Ianni A, Templeton DJ, Woodgett JR, Balsano C, Levrero M. Activation of SAPK/JNK by TNF receptor 1 through a noncytotoxic TRAF2- dependent pathway. of special interest Science. 275:1997;200-203 See annotation to [43].
    • (1997) Science , vol.275 , pp. 200-203
    • Natoli, G.1    Costanzo, A.2    Ianni, A.3    Templeton, D.J.4    Woodgett, J.R.5    Balsano, C.6    Levrero, M.7
  • 43
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    • Tumor necrosis factor alpha-induced activation of c-jun N-terminal kinase is mediated by TRAF2
    • of special interest. These three papers [41-43] identify TRAF2 as a mediator of signals from the TNF receptor that lead to JNK activation. The signaling intermediates downstream of TRAF2 remain to be described.
    • Reinhard C, Shamoon B, Shyamala V, Williams LT. Tumor necrosis factor alpha-induced activation of c-jun N-terminal kinase is mediated by TRAF2. of special interest EMBO J. 16:1997;1080-1092 These three papers [41-43] identify TRAF2 as a mediator of signals from the TNF receptor that lead to JNK activation. The signaling intermediates downstream of TRAF2 remain to be described.
    • (1997) EMBO J , vol.16 , pp. 1080-1092
    • Reinhard, C.1    Shamoon, B.2    Shyamala, V.3    Williams, L.T.4
  • 44
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    • Daxx, a novel Fas-binding protein that activates JNK and apoptosis
    • of special interest. This study identifies Daxx as a mediator of JNK activation by Fas. Interestingly, Daxx activates JNK and apoptosis. Daxx is, therefore, a common mediator of these events.
    • Yang X, Khosravi-Far R, Chang HY, Baltimore D. Daxx, a novel Fas-binding protein that activates JNK and apoptosis. of special interest Cell. 89:1997;1067-1076 This study identifies Daxx as a mediator of JNK activation by Fas. Interestingly, Daxx activates JNK and apoptosis. Daxx is, therefore, a common mediator of these events.
    • (1997) Cell , vol.89 , pp. 1067-1076
    • Yang, X.1    Khosravi-Far, R.2    Chang, H.Y.3    Baltimore, D.4
  • 45
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    • Signaling from G protein-coupled receptors to c-Jun kinase involves beta gamma subunits of heterotrimeric G proteins acting on a Ras and Rac1-dependent pathway
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    • Coso, O.A.1    Teramoto, H.2    Simonds, W.F.3    Gutkind, J.S.4
  • 46
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    • Linkage of G protein-coupled receptors to the MAPK signaling pathway through PI 3-kinase gamma
    • of special interest. See annotation to [49].
    • Lopez-Ilasaca M, Crespo P, Pellici PG, Gutkind JS, Wetzker R. Linkage of G protein-coupled receptors to the MAPK signaling pathway through PI 3-kinase gamma. of special interest Science. 275:1997;394-397 See annotation to [49].
    • (1997) Science , vol.275 , pp. 394-397
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  • 47
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    • Membrane localization of phosphatidylinositol 3-kinase is sufficient to activate multiple signal-transducing kinase pathways
    • of special interest. See annotation to [49].
    • Klippel A, Reinhard C, Kavanaugh WM, Apell G, Escobedo MA, Williams LT. Membrane localization of phosphatidylinositol 3-kinase is sufficient to activate multiple signal-transducing kinase pathways. of special interest Mol Cell Biol. 16:1996;4117-4127 See annotation to [49].
    • (1996) Mol Cell Biol , vol.16 , pp. 4117-4127
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  • 48
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    • Phosphatidylinositol 3-kinase mediates epidermal growth factor-induced activation of the c-Jun N-terminal kinase signaling pathway
    • of special interest. See annotation to [49].
    • Logan SK, Falasca M, Hu P, Schlessinger J. Phosphatidylinositol 3-kinase mediates epidermal growth factor-induced activation of the c-Jun N-terminal kinase signaling pathway. of special interest Mol Cell Biol. 17:1997;5784-5790 See annotation to [49].
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    • Logan, S.K.1    Falasca, M.2    Hu, P.3    Schlessinger, J.4
  • 49
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    • Requirement of phosphatidylinositol-3 kinase for activation of JNK/SAPKs by PDGF
    • of special interest. These four papers [46-49] identify PI-3 kinase isoforms as mediators of signals from serpentine and tyrosine kinase receptors to the JNK signaling pathway.
    • Lopez-Ilasaca M, Li W, Uren A, Yu JC, Kazlauskas A, Gutkind JS, Heidaran MA. Requirement of phosphatidylinositol-3 kinase for activation of JNK/SAPKs by PDGF. of special interest Biochem Biophys Res Commun. 232:1997;273-277 These four papers [46-49] identify PI-3 kinase isoforms as mediators of signals from serpentine and tyrosine kinase receptors to the JNK signaling pathway.
    • (1997) Biochem Biophys Res Commun , vol.232 , pp. 273-277
    • Lopez-Ilasaca, M.1    Li, W.2    Uren, A.3    Yu, J.C.4    Kazlauskas, A.5    Gutkind, J.S.6    Heidaran, M.A.7
  • 50
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    • Activation of PYK2 by stress signals and coupling with JNK signaling pathway
    • of special interest. See annotation to [51].
    • Tokiwa G, Dikic I, Lev S, Schlessinger J. Activation of PYK2 by stress signals and coupling with JNK signaling pathway. of special interest Science. 273:1996;792-794 See annotation to [51].
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    • Tokiwa, G.1    Dikic, I.2    Lev, S.3    Schlessinger, J.4
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    • Regulation of mitogen-activated protein kinases by a calcium/calmodulin-dependent protein kinase cascade
    • 2+ via a CAM kinase cascade. The mechanism by which CAM kinase 4 activates MAP kinases is not established.
    • 2+ via a CAM kinase cascade. The mechanism by which CAM kinase 4 activates MAP kinases is not established.
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  • 53
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    • Ultraviolet light and osmotic stress: Activation of the JNK cascade through multiple growth factor and cytokine receptors
    • of special interest. See annotation to [54].
    • Rosette C, Karin M. Ultraviolet light and osmotic stress: activation of the JNK cascade through multiple growth factor and cytokine receptors. of special interest Science. 274:1996;1194-1197 See annotation to [54].
    • (1996) Science , vol.274 , pp. 1194-1197
    • Rosette, C.1    Karin, M.2
  • 54
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    • Ultraviolet radiation-induced apoptosis is mediated by activation of CD-95 (Fas/APO-1)
    • of special interest. These two papers [53,54] demonstrate that induced receptor aggregation may contribute to the activation of JNK in response to UV radiation.
    • Rehemtulla A, Hamilton CA, Chinnaiyan AM, Dixit VM. Ultraviolet radiation-induced apoptosis is mediated by activation of CD-95 (Fas/APO-1). of special interest J Biol Chem. 272:1997;25783-25786 These two papers [53,54] demonstrate that induced receptor aggregation may contribute to the activation of JNK in response to UV radiation.
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    • Rehemtulla, A.1    Hamilton, C.A.2    Chinnaiyan, A.M.3    Dixit, V.M.4
  • 55
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    • Activation of p38 MAP kinase by c-ABL-dependent and independent mechanisms
    • of special interest. This study established that the c-Abl tyrosine kinase contributes to the effect of the DNA damaging agent 1-β-D-arabinofuranosylcytosine. The effects of other DNA damaging agents known to activate JNK are not mediated by ABL.
    • Pandey P, Raingeaud J, Kaneki M, Weichselbaum R, Davis RJ, Kufe D, Kharbanda S. Activation of p38 MAP kinase by c-ABL-dependent and independent mechanisms. of special interest J Biol Chem. 271:1996;23775-23779 This study established that the c-Abl tyrosine kinase contributes to the effect of the DNA damaging agent 1-β-D-arabinofuranosylcytosine. The effects of other DNA damaging agents known to activate JNK are not mediated by ABL.
    • (1996) J Biol Chem , vol.271 , pp. 23775-23779
    • Pandey, P.1    Raingeaud, J.2    Kaneki, M.3    Weichselbaum, R.4    Davis, R.J.5    Kufe, D.6    Kharbanda, S.7
  • 56
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    • The level of intracellular glutathione is a key regulator for the induction of stress-activated signal transduction pathways including Jun N-terminal protein kinases and p38 kinase by alkylating agents
    • of special interest. This study provides evidence that alkylating agents activate JNK through changes in the redox potential of intracellular glutathione. The relevant redox sensor that mediates JNK activation has not been defined.
    • Wilhelm D, Bender K, Knebel A, Angel P. The level of intracellular glutathione is a key regulator for the induction of stress-activated signal transduction pathways including Jun N-terminal protein kinases and p38 kinase by alkylating agents. of special interest Mol Cell Biol. 17:1997;4792-4800 This study provides evidence that alkylating agents activate JNK through changes in the redox potential of intracellular glutathione. The relevant redox sensor that mediates JNK activation has not been defined.
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    • Wilhelm, D.1    Bender, K.2    Knebel, A.3    Angel, P.4
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    • Ribotoxic stress response: Activation of the stress-activated protein kinase JNK1 by inhibitors of the peptidyl transferase reaction and by sequence-specific RNA damage to the α-sarcin/ricin loop in the 28S rRNA
    • of special interest. This is an interesting study which examines the mechanism of JNK activation by translational inhibitors. The authors propose that JNK activation is mediated by specific damage to the 28S ribosomal RNA.
    • Iordanov MS, Pribnow D, Magun JL, Dinh TH, Pearson JA, Chen SL, Magun BE. Ribotoxic stress response: activation of the stress-activated protein kinase JNK1 by inhibitors of the peptidyl transferase reaction and by sequence-specific RNA damage to the α-sarcin/ricin loop in the 28S rRNA. of special interest Mol Cell Biol. 17:1997;3373-3381 This is an interesting study which examines the mechanism of JNK activation by translational inhibitors. The authors propose that JNK activation is mediated by specific damage to the 28S ribosomal RNA.
    • (1997) Mol Cell Biol , vol.17 , pp. 3373-3381
    • Iordanov, M.S.1    Pribnow, D.2    Magun, J.L.3    Dinh, T.H.4    Pearson, J.A.5    Chen, S.L.6    Magun, B.E.7
  • 58
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    • RAC regulation of actin polymerization and proliferation by a pathway distinct from Jun kinase
    • of special interest. See annotation to [59].
    • Joneson T, McDonough M, Bar-Sagi D, Van Aelst L. RAC regulation of actin polymerization and proliferation by a pathway distinct from Jun kinase. of special interest Science. 274:1996;1374-1376 See annotation to [59].
    • (1996) Science , vol.274 , pp. 1374-1376
    • Joneson, T.1    McDonough, M.2    Bar-Sagi, D.3    Van Aelst, L.4
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    • Rac and Cdc42 induce actin polymerization and G1 cell cycle progression independently of p65PAK and the JNK/SAPK MAP kinase cascade
    • of special interest. These two papers [58,59] describe the use of mutant Rac and Cdc42 proteins to distinguish signaling pathways that are initiated by these small GTPases. The JNK pathway is shown to be independent of the effects of Rac and Cdc42 on actin cytoskeleton re-organization.
    • Lamarche N, Tapon N, Stowers L, Burbelo PD, Aspenstrom P, Bridges T, Chant J, Hall A. Rac and Cdc42 induce actin polymerization and G1 cell cycle progression independently of p65PAK and the JNK/SAPK MAP kinase cascade. of special interest Cell. 87:1996;519-529 These two papers [58,59] describe the use of mutant Rac and Cdc42 proteins to distinguish signaling pathways that are initiated by these small GTPases. The JNK pathway is shown to be independent of the effects of Rac and Cdc42 on actin cytoskeleton re-organization.
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    • Lamarche, N.1    Tapon, N.2    Stowers, L.3    Burbelo, P.D.4    Aspenstrom, P.5    Bridges, T.6    Chant, J.7    Hall, A.8
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    • Signaling from the small GTP-binding proteins Rac1 and Cdc42 to the c-Jun N-terminal kinase/stress-activated protein kinase pathway
    • Teramoto H, Coso OA, Miyata H, Igishi T, Miki T, Gutkind JS. Signaling from the small GTP-binding proteins Rac1 and Cdc42 to the c-Jun N-terminal kinase/stress-activated protein kinase pathway. J Biol Chem. 271:1996;27225-27228.
    • (1996) J Biol Chem , vol.271 , pp. 27225-27228
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    • The small GTP-binding protein rho activates c-Jun N-terminal kinases/stress-activated protein kinases in human kidney 293T cells. Evidence for a Pak-independent signaling pathway
    • Teramoto H, Crespo P, Coso OA, Igishi T, Xu N, Gutkind JS. The small GTP-binding protein rho activates c-Jun N-terminal kinases/stress-activated protein kinases in human kidney 293T cells. Evidence for a Pak-independent signaling pathway. J Biol Chem. 271:1996;25731-25734.
    • (1996) J Biol Chem , vol.271 , pp. 25731-25734
    • Teramoto, H.1    Crespo, P.2    Coso, O.A.3    Igishi, T.4    Xu, N.5    Gutkind, J.S.6
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    • MEK kinases are regulated by EGF and selectively interact with Rac/Cdc42
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    • C-Jun can recruit JNK to phosphorylate dimerization partners via specific docking interactions
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    • Activation of the Sap1a transcription factor by the c-Jun N-terminal kinase (JNK) mitogen-activated protein kinase
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    • Role of p38 and JNK MAP kinases in the activation of ternary complex factors
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    • The multifunctional role of the co-activator CBP in transcriptional regulation
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    • Phosphorylation-dependent targeting of c-Jun ubiquitination by Jun N-kinase
    • of special interest. See annotation to [73].
    • Fuchs SY, Dolan L, Davis RJ, Ronai Z. Phosphorylation-dependent targeting of c-Jun ubiquitination by Jun N-kinase. of special interest Oncogene. 13:1996;1531-1535 See annotation to [73].
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    • Reduced ubiquitin-dependent degradation of c-Jun after phosphorylation by MAP kinases
    • of special interest. These two papers [71,73] establish that Jun phosphorylation by JNK regulates protein stability by inhibiting ubiquitination. The c-Jun protein has a short half-life because it is rapidly degraded by proteasomes. Phosphorylation by JNK increases the half-life of the c-Jun protein by inhibiting ubiquitination, and therefore degradation by the proteasome pathway.
    • Musti AM, Treier M, Bohmann D. Reduced ubiquitin-dependent degradation of c-Jun after phosphorylation by MAP kinases. of special interest Science. 275:1997;400-402 These two papers [71,73] establish that Jun phosphorylation by JNK regulates protein stability by inhibiting ubiquitination. The c-Jun protein has a short half-life because it is rapidly degraded by proteasomes. Phosphorylation by JNK increases the half-life of the c-Jun protein by inhibiting ubiquitination, and therefore degradation by the proteasome pathway.
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    • Nuclear accumulation of NFAT4 opposed by the JNK signal transduction pathway
    • of special interest. This study demonstrates that JNK regulates the nuclear accumulation of a transcription factor.
    • Chow C-W, Rincon M, Cavanagh J, Dickens M, Davis RJ. Nuclear accumulation of NFAT4 opposed by the JNK signal transduction pathway. of special interest Science. 278:1997;1638-1641 This study demonstrates that JNK regulates the nuclear accumulation of a transcription factor.
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    • Chow C-W1    Rincon, M.2    Cavanagh, J.3    Dickens, M.4    Davis, R.J.5
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    • Activation of the JNK pathway is essential for transformation by the Met oncogene
    • Rodrigues GA, Park M, Schlessinger J. Activation of the JNK pathway is essential for transformation by the Met oncogene. EMBO J. 16:1997;2634-2645.
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    • Downstream of Crk adaptor signaling pathway: Activation of Jun kinase by v-Crk through the guanine nucleotide exchange protein C3G
    • Tanaka S, Ouchi T, Hanafusa H. Downstream of Crk adaptor signaling pathway: activation of Jun kinase by v-Crk through the guanine nucleotide exchange protein C3G. Proc Natl Acad Sci USA. 94:1997;2356-2361.
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    • Tanaka, S.1    Ouchi, T.2    Hanafusa, H.3
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    • The Bcr-Abl leukemia oncogene activates Jun kinase and requires Jun for transformation
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    • Human mitogen-activated protein kinase kinase 4 as a candidate tumor suppressor
    • of special interest. This study demonstrates that the MKK4 gene is mutated in some human tumor cells. Whether these mutations contribute to the tumor phenotype remains to be established.
    • Teng DH, Perry WL, Hogan JK, Baumgard M, Bell R, Berry S, Davis T, Frank D, Frye C, Hattier T, et al. Human mitogen-activated protein kinase kinase 4 as a candidate tumor suppressor. of special interest Cancer Res. 57:1997;4177-4182 This study demonstrates that the MKK4 gene is mutated in some human tumor cells. Whether these mutations contribute to the tumor phenotype remains to be established.
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    • Characterization of the structure and function of a new mitogen-activated protein kinase (p38β)
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    • Reprogramming the signaling requirement for AP-1 activation during differentiation of precursor CD4+ T cells to effector Th1 and Th2 cells
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    • TNF initiates E-selectin transcription in human endothelial cells through parallel TRAF-NF-kappaB and TRAF-RAC/CDC42-JNK-c-Jun/ATF2 pathways
    • Min W, Pober JS. TNF initiates E-selectin transcription in human endothelial cells through parallel TRAF-NF-kappaB and TRAF-RAC/CDC42-JNK-c-Jun/ATF2 pathways. J Immunol. 159:1997;3508-3518.
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    • Min, W.1    Pober, J.S.2
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    • TNFα induced E-selectin expression is activated by the NF-κB and JNK/p38 MAP kinase pathways
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    • Read, M.A.1    Whitely, M.Z.2    Gupta, S.3    Pierce, J.W.4    Best, J.5    Davis, R.J.6    Collins, T.7
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