메뉴 건너뛰기




Volumn 388, Issue 6642, 1997, Pages 548-554

A cytokine-responsive IκB kinase that activates the transcription factor NF-κB

Author keywords

[No Author keywords available]

Indexed keywords

CYTOKINE; PROTEIN KINASE; TRANSCRIPTION FACTOR; AUTACOID; CHUK PROTEIN, HUMAN; I KAPPA B KINASE; IKBKB PROTEIN, HUMAN; IKBKE PROTEIN, HUMAN; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; PHOSPHOPROTEIN PHOSPHATASE; PROTEIN SERINE THREONINE KINASE; TUMOR NECROSIS FACTOR ALPHA;

EID: 0030610362     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/41493     Document Type: Article
Times cited : (1946)

References (31)
  • 1
    • 0027332498 scopus 로고
    • The IκB proteins: Multifunctional regulators of Rel/NF-κB transcription factors
    • Beg, A. A. & Baldwin, A. S. Jr The IκB proteins: multifunctional regulators of Rel/NF-κB transcription factors. Genes Dev. 7, 2064-2070 (1993).
    • (1993) Genes Dev. , vol.7 , pp. 2064-2070
    • Beg, A.A.1    Baldwin Jr., A.S.2
  • 2
    • 0027333044 scopus 로고
    • The IκB proteins: Members of a multifunctional family
    • Gilmore, T. D. & Morin, P. J. The IκB proteins: members of a multifunctional family. Trends Genet. 9, 427-433 (1993).
    • (1993) Trends Genet. , vol.9 , pp. 427-433
    • Gilmore, T.D.1    Morin, P.J.2
  • 3
    • 0028929371 scopus 로고
    • Coupling of a signal response domain in IκB to multiple pathways for NF-κB activation
    • Brockman, J. A. et al. Coupling of a signal response domain in IκB to multiple pathways for NF-κB activation. Mol. Cell. Biol. 15, 2809-2818 (1995).
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 2809-2818
    • Brockman, J.A.1
  • 4
    • 0028986075 scopus 로고
    • Control of IκBαt proteolysis by site-specific, signal-induced phosphorylation
    • Brown, K., Gerstberger, F. S., Carlson, L., Franzoso, G. & Siebenlist, U. Control of IκBαt proteolysis by site-specific, signal-induced phosphorylation. Science 267, 1485-1491 (1995).
    • (1995) Science , vol.267 , pp. 1485-1491
    • Brown, K.1    Gerstberger, F.S.2    Carlson, L.3    Franzoso, G.4    Siebenlist, U.5
  • 5
    • 0028978032 scopus 로고
    • Phosphorylation of human IκB on serines 32 and 36 controls IκB proteolysis and NF-κB activation in response to diverse stimuli
    • Traenckner, E. B. et al. Phosphorylation of human IκB on serines 32 and 36 controls IκB proteolysis and NF-κB activation in response to diverse stimuli. EMBO J. 14, 2876-2883 (1995).
    • (1995) EMBO J. , vol.14 , pp. 2876-2883
    • Traenckner, E.B.1
  • 6
    • 0029122799 scopus 로고
    • N- And C-terminal sequences control degradation of MAD3/IκBα in response to inducers of NF-κB activity
    • Whiteside, T. et al. N- and C-terminal sequences control degradation of MAD3/IκBα in response to inducers of NF-κB activity. Mol. Cell. Biol. 15, 5339-5345 (1995).
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 5339-5345
    • Whiteside, T.1
  • 7
    • 0029670083 scopus 로고    scopus 로고
    • Mapping of the inducible IκB phosphorylation sites that signal its ubiquitination and degradation
    • DiDonato, J. A. et al. Mapping of the inducible IκB phosphorylation sites that signal its ubiquitination and degradation. Mol. Cell. Biol. 16, 1295-1304 (1996).
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 1295-1304
    • Didonato, J.A.1
  • 8
    • 0029146930 scopus 로고
    • Signal-induced site-specific phosphorylation targets IκB to the ubiquitin-proteasome pathway
    • Chen, Z. et al. Signal-induced site-specific phosphorylation targets IκB to the ubiquitin-proteasome pathway. Genes Dev. 9, 1586-1597 (1995).
    • (1995) Genes Dev. , vol.9 , pp. 1586-1597
    • Chen, Z.1
  • 10
    • 0026663539 scopus 로고
    • The ubiquitin system for protein degradation
    • Hershko, A. & Cienchanover, A. The ubiquitin system for protein degradation. Annu. Rev. Biochem. 61, 761-807 (1992).
    • (1992) Annu. Rev. Biochem. , vol.61 , pp. 761-807
    • Hershko, A.1    Cienchanover, A.2
  • 11
    • 0028985191 scopus 로고
    • Vivo stimulation of IκB phosphorylation is not sufficient to activate NF-κB
    • Alkalay, I. et al. In vivo stimulation of IκB phosphorylation is not sufficient to activate NF-κB. Mol. Cell. Biol. 15, 1294-1301 (1995).
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 1294-1301
    • Alkalay, I.1
  • 12
    • 0028985190 scopus 로고
    • Phosphorylation of IκBα precedes but is not sufficient for its dissociation from NF-κB
    • DiDonato, J. A., Mercurio, F. & Karin, M. Phosphorylation of IκBα precedes but is not sufficient for its dissociation from NF-κB. Mol. Cell. Biol. 15, 1302-1311 (1995).
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 1302-1311
    • Didonato, J.A.1    Mercurio, F.2    Karin, M.3
  • 14
    • 0028978217 scopus 로고
    • Activation of NF-&B by phsophatase inhibitors involves the phosphorylation of IκBα at phosphatase 2A-sensitive sites
    • Sun, S. C., Maggirwar, S. B. & Harhaj, E. Activation of NF-&B by phsophatase inhibitors involves the phosphorylation of IκBα at phosphatase 2A-sensitive sites. J. Biol. Chem. 270, 18347-18351 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 18347-18351
    • Sun, S.C.1    Maggirwar, S.B.2    Harhaj, E.3
  • 15
    • 0030004897 scopus 로고    scopus 로고
    • Site-specific phosphorylation of IκBα by a novel ubiquitination-dependent protein kinase activity
    • Chen, Z. J., Parent, L. & Maniatis, T. Site-specific phosphorylation of IκBα by a novel ubiquitination-dependent protein kinase activity. Cell 84, 853-862 (1996).
    • (1996) Cell , vol.84 , pp. 853-862
    • Chen, Z.J.1    Parent, L.2    Maniatis, T.3
  • 16
    • 0027221568 scopus 로고
    • γ-Phosphate-linked ATP-Sepharose for the affinity purification of protein kinases. Rapid purification to homogeneity of skeletal muscle mitogen-activated protein kinase kinase
    • Haystead, C. M., Gregory, P., Sturgill, T. W. & Haystead, T. A. γ-Phosphate-linked ATP-Sepharose for the affinity purification of protein kinases. Rapid purification to homogeneity of skeletal muscle mitogen-activated protein kinase kinase. Eur. J. Biochem. 214, 459-467 (1993).
    • (1993) Eur. J. Biochem. , vol.214 , pp. 459-467
    • Haystead, C.M.1    Gregory, P.2    Sturgill, T.W.3    Haystead, T.A.4
  • 17
    • 0029554095 scopus 로고
    • CHUK, a new member of the helix-loop-helix and leucine zipper families of interacting proteins, contains a serine-threonine kinase catalytic domain
    • Connely, M. A. & Marcu, K. B. CHUK, a new member of the helix-loop-helix and leucine zipper families of interacting proteins, contains a serine-threonine kinase catalytic domain. Cell. Mol. Biol. Res. 41, 537-549 (1995).
    • (1995) Cell. Mol. Biol. Res. , vol.41 , pp. 537-549
    • Connely, M.A.1    Marcu, K.B.2
  • 18
    • 0028174061 scopus 로고
    • Function and activation of NF-κB in the immune system
    • Baeuerle, P. A. & Henkel, T. Function and activation of NF-κB in the immune system. Annu. Rev. Immunol. 12, 141-179 (1994).
    • (1994) Annu. Rev. Immunol. , vol.12 , pp. 141-179
    • Baeuerle, P.A.1    Henkel, T.2
  • 19
    • 0030615201 scopus 로고    scopus 로고
    • Nuclear factor-κB - A pivotal transcription factor in chronic inflammatory diseases
    • Barnes, P. J. & Karin, M. Nuclear factor-κB - A pivotal transcription factor in chronic inflammatory diseases. New Engl. J. Med. 336, 1066-1071 (1997).
    • (1997) New Engl. J. Med. , vol.336 , pp. 1066-1071
    • Barnes, P.J.1    Karin, M.2
  • 20
    • 0030271387 scopus 로고    scopus 로고
    • NF-κB: Ten years after
    • Baeuerle, P. A. & Baltimore, D. NF-κB: ten years after. Cell 87, 13-20 (1996).
    • (1996) Cell , vol.87 , pp. 13-20
    • Baeuerle, P.A.1    Baltimore, D.2
  • 21
    • 0028124428 scopus 로고
    • A novel family of putative signal transducers associated with the cytoplamic domain of the 75 kDa tumor necrosis factor receptor
    • Rothe, M., Wong, S. C., Henzel, W. J. & Goeddel, D. V. A novel family of putative signal transducers associated with the cytoplamic domain of the 75 kDa tumor necrosis factor receptor. Cell 78, 681-692 (1994).
    • (1994) Cell , vol.78 , pp. 681-692
    • Rothe, M.1    Wong, S.C.2    Henzel, W.J.3    Goeddel, D.V.4
  • 22
    • 0029007855 scopus 로고
    • The TNF receptor 1-associated protein TRADD signals cell death and NF-κB activation
    • Hsu, H., Xiong, J. & Goeddel, D. V. The TNF receptor 1-associated protein TRADD signals cell death and NF-κB activation. Cell 81, 495-504 (1995).
    • (1995) Cell , vol.81 , pp. 495-504
    • Hsu, H.1    Xiong, J.2    Goeddel, D.V.3
  • 23
    • 0030032106 scopus 로고    scopus 로고
    • TRADD-TRAF2 and TRADD-FADD interactions define two distinct TNF receptor 1 signal transduction pathways
    • Hsu, H., Shu, B. H., Pan, M. G. & Goeddel, D. V. TRADD-TRAF2 and TRADD-FADD interactions define two distinct TNF receptor 1 signal transduction pathways. Cell 84, 299-308 (1996).
    • (1996) Cell , vol.84 , pp. 299-308
    • Hsu, H.1    Shu, B.H.2    Pan, M.G.3    Goeddel, D.V.4
  • 24
  • 25
    • 0029865142 scopus 로고    scopus 로고
    • IRAK: A kinase associated with the interleukin-1 receptor
    • Cao, Z., Henzel, W. J. & Gao, X. IRAK: a kinase associated with the interleukin-1 receptor. Science 271, 1128-1131 (1996).
    • (1996) Science , vol.271 , pp. 1128-1131
    • Cao, Z.1    Henzel, W.J.2    Gao, X.3
  • 26
    • 0030298294 scopus 로고    scopus 로고
    • Dissection of TNF receptor 1 effector functions: JNK activation is not linked to apoptosis, while NF-κB activation prevents cell death
    • Liu, Z.-G., Hu, H., Goeddel, D. V. & Karin, M. Dissection of TNF receptor 1 effector functions: JNK activation is not linked to apoptosis, while NF-κB activation prevents cell death. Cell 87, 565-576 (1996).
    • (1996) Cell , vol.87 , pp. 565-576
    • Liu, Z.-G.1    Hu, H.2    Goeddel, D.V.3    Karin, M.4
  • 27
    • 0031285250 scopus 로고    scopus 로고
    • Activation of the IκBα kinase complex by MEKK1, a kinase of the JNK pathway
    • Lee, F. S., Hagler, J., Chen, Z. J. & Maniatis, T. Activation of the IκBα kinase complex by MEKK1, a kinase of the JNK pathway. Cell 88, 213-222 (1997).
    • (1997) Cell , vol.88 , pp. 213-222
    • Lee, F.S.1    Hagler, J.2    Chen, Z.J.3    Maniatis, T.4
  • 28
    • 0030606319 scopus 로고    scopus 로고
    • C-Jun can recruit JNK to phosphorylate dimerization partners via specific docking interactions
    • Kallunki, T., Deng, T., Hibi, M. & Karin, M. c-Jun can recruit JNK to phosphorylate dimerization partners via specific docking interactions. Cell 87, 929-939 (1996).
    • (1996) Cell , vol.87 , pp. 929-939
    • Kallunki, T.1    Deng, T.2    Hibi, M.3    Karin, M.4
  • 29
    • 0028986194 scopus 로고
    • IκBβ regulates the persistent response in a biphasic activation of NF-κB
    • Thompson, J. E., Philips, R. J., Erdjument-Bromage, H., Tempst, P. & Ghosh, S. IκBβ regulates the persistent response in a biphasic activation of NF-κB. Cell 80, 573-582 (1995).
    • (1995) Cell , vol.80 , pp. 573-582
    • Thompson, J.E.1    Philips, R.J.2    Erdjument-Bromage, H.3    Tempst, P.4    Ghosh, S.5
  • 30
    • 0028609209 scopus 로고
    • JNK2 ocntains a specificity-determining region responsible for efficient c-Jun binding and phosphorylation
    • Kallunki, T. et al. JNK2 ocntains a specificity-determining region responsible for efficient c-Jun binding and phosphorylation. Genes Dev. 8, 2996-3007 (1994).
    • (1994) Genes Dev. , vol.8 , pp. 2996-3007
    • Kallunki, T.1
  • 31
    • 0028837242 scopus 로고
    • Glucocorticoid-induced apoptosis of human leukemic cells is caused by the repressive function of the glucocorticoid receptor
    • Helmberg, A., Auphan, N., Gaelles, C. & Karin, M. Glucocorticoid-induced apoptosis of human leukemic cells is caused by the repressive function of the glucocorticoid receptor EMBO J. 14, 452-460 (1995).
    • (1995) EMBO J. , vol.14 , pp. 452-460
    • Helmberg, A.1    Auphan, N.2    Gaelles, C.3    Karin, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.