메뉴 건너뛰기




Volumn 1843, Issue 7, 2014, Pages 1365-1372

Nemo-like kinase (NLK) negatively regulates NF-kappa B activity through disrupting the interaction of TAK1 with IKKβ

Author keywords

IKK ; NF B; NLK; TAK1; TNF

Indexed keywords

I KAPPA B ALPHA; I KAPPA B KINASE BETA; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; NEMO LIKE KINASE; PROTEIN SERINE THREONINE KINASE; SYNAPTOTAGMIN I; TRANSCRIPTION FACTOR RELA; TRANSFORMING GROWTH FACTOR BETA ACTIVATED KINASE 1; TUMOR NECROSIS FACTOR ALPHA; UNCLASSIFIED DRUG; I KAPPA B KINASE; IKBKB PROTEIN, HUMAN; MAP KINASE KINASE KINASE 7; MITOGEN ACTIVATED PROTEIN KINASE KINASE KINASE; NLK PROTEIN, HUMAN; PROTEIN BINDING; SIGNAL PEPTIDE; SMALL INTERFERING RNA;

EID: 84899083046     PISSN: 01674889     EISSN: 18792596     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2014.03.028     Document Type: Article
Times cited : (30)

References (31)
  • 1
    • 0035137882 scopus 로고    scopus 로고
    • Control of oncogenesis and cancer therapy resistance by the transcription factor NF-kappaB
    • Baldwin A.S. Control of oncogenesis and cancer therapy resistance by the transcription factor NF-kappaB. J. Clin. Invest. 2001, 107:241-246.
    • (2001) J. Clin. Invest. , vol.107 , pp. 241-246
    • Baldwin, A.S.1
  • 2
    • 25844459154 scopus 로고    scopus 로고
    • NF-κB: linking inflammation and immunity to cancer development and progression
    • Karin M., Greten F.R. NF-κB: linking inflammation and immunity to cancer development and progression. Nat. Rev. Immunol. 2005, 5:749-759.
    • (2005) Nat. Rev. Immunol. , vol.5 , pp. 749-759
    • Karin, M.1    Greten, F.R.2
  • 3
    • 84894534156 scopus 로고    scopus 로고
    • The IkappaB kinase complex in NF-kappaB regulation and beyond
    • Hinz M., Scheidereit C. The IkappaB kinase complex in NF-kappaB regulation and beyond. EMBO Rep. 2014, 15:46-61.
    • (2014) EMBO Rep. , vol.15 , pp. 46-61
    • Hinz, M.1    Scheidereit, C.2
  • 4
    • 73849095427 scopus 로고    scopus 로고
    • The nuclear signaling of NF-kappaB: current knowledge, new insights, and future perspectives
    • Wan F., Lenardo M.J. The nuclear signaling of NF-kappaB: current knowledge, new insights, and future perspectives. Cell Res. 2010, 20:24-33.
    • (2010) Cell Res. , vol.20 , pp. 24-33
    • Wan, F.1    Lenardo, M.J.2
  • 5
    • 0032575379 scopus 로고    scopus 로고
    • Direct phosphorylation of IkappaB by IKKalpha and IKKbeta: discrimination between free and NF-kappaB-bound substrate
    • Zandi E., Chen Y., Karin M. Direct phosphorylation of IkappaB by IKKalpha and IKKbeta: discrimination between free and NF-kappaB-bound substrate. Science 1998, 281:1360-1363.
    • (1998) Science , vol.281 , pp. 1360-1363
    • Zandi, E.1    Chen, Y.2    Karin, M.3
  • 7
    • 0036781052 scopus 로고    scopus 로고
    • NF-κB regulation in the immune system
    • Li Q., Verma I.M. NF-κB regulation in the immune system. Nat. Rev. Immunol. 2002, 2:725-734.
    • (2002) Nat. Rev. Immunol. , vol.2 , pp. 725-734
    • Li, Q.1    Verma, I.M.2
  • 8
    • 33751075720 scopus 로고    scopus 로고
    • Selective degradation of the IkappaB kinase (IKK) by autophagy
    • Li D. Selective degradation of the IkappaB kinase (IKK) by autophagy. Cell Res. 2006, 16:855-856.
    • (2006) Cell Res. , vol.16 , pp. 855-856
    • Li, D.1
  • 9
    • 0242664121 scopus 로고    scopus 로고
    • IkappaB kinase-independent IkappaBalpha degradation pathway: functional NF-kappaB activity and implications for cancer therapy
    • Tergaonkar V., Bottero V., Ikawa M., Li Q., Verma I.M. IkappaB kinase-independent IkappaBalpha degradation pathway: functional NF-kappaB activity and implications for cancer therapy. Mol. Cell. Biol. 2003, 23:8070-8083.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 8070-8083
    • Tergaonkar, V.1    Bottero, V.2    Ikawa, M.3    Li, Q.4    Verma, I.M.5
  • 10
    • 78650878363 scopus 로고    scopus 로고
    • NF-kappaB, inflammation, and metabolic disease
    • Baker R.G., Hayden M.S., Ghosh S. NF-kappaB, inflammation, and metabolic disease. Cell Metab. 2011, 13:11-22.
    • (2011) Cell Metab. , vol.13 , pp. 11-22
    • Baker, R.G.1    Hayden, M.S.2    Ghosh, S.3
  • 11
    • 79954618079 scopus 로고    scopus 로고
    • The role of TRADD in TRAIL-induced apoptosis and signaling
    • Cao X., Pobezinskaya Y.L., Morgan M.J., Liu Z.G. The role of TRADD in TRAIL-induced apoptosis and signaling. FASEB J. 2011, 25:1353-1358.
    • (2011) FASEB J. , vol.25 , pp. 1353-1358
    • Cao, X.1    Pobezinskaya, Y.L.2    Morgan, M.J.3    Liu, Z.G.4
  • 12
    • 81055145273 scopus 로고    scopus 로고
    • Crucial role for TNF receptor-associated factor 2 (TRAF2) in regulating NFkappaB2 signaling that contributes to autoimmunity
    • Lin W.J., Su Y.W., Lu Y.C., Hao Z., Chio I.I., Chen N.J., Brustle A., Li W.Y., Mak T.W. Crucial role for TNF receptor-associated factor 2 (TRAF2) in regulating NFkappaB2 signaling that contributes to autoimmunity. Proc. Natl. Acad. Sci. U. S. A. 2011, 108:18354-18359.
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108 , pp. 18354-18359
    • Lin, W.J.1    Su, Y.W.2    Lu, Y.C.3    Hao, Z.4    Chio, I.I.5    Chen, N.J.6    Brustle, A.7    Li, W.Y.8    Mak, T.W.9
  • 13
    • 84863338304 scopus 로고    scopus 로고
    • Ubiquitination in signaling to and activation of IKK
    • Chen Z.J. Ubiquitination in signaling to and activation of IKK. Immunol. Rev. 2012, 246:95-106.
    • (2012) Immunol. Rev. , vol.246 , pp. 95-106
    • Chen, Z.J.1
  • 14
    • 38849199203 scopus 로고    scopus 로고
    • Shared principles in NF-kappaB signaling
    • Hayden M.S., 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
  • 15
    • 77957252647 scopus 로고    scopus 로고
    • The IKK complex, a central regulator of NF-kappaB activation
    • Israel A. The IKK complex, a central regulator of NF-kappaB activation. Cold Spring Harb. Perspect. Biol. 2010, 2:a000158.
    • (2010) Cold Spring Harb. Perspect. Biol. , vol.2
    • Israel, A.1
  • 16
    • 0030610362 scopus 로고    scopus 로고
    • A cytokine-responsive IκB kinase that activates the transcription factor NF-κB
    • DiDonato J.A., Hayakawa M., Rothwarf D.M., Zandi E., Karin M. A cytokine-responsive IκB kinase that activates the transcription factor NF-κB. Nature 1997, 388:548-554.
    • (1997) Nature , vol.388 , pp. 548-554
    • DiDonato, J.A.1    Hayakawa, M.2    Rothwarf, D.M.3    Zandi, E.4    Karin, M.5
  • 17
    • 0030613551 scopus 로고    scopus 로고
    • The IκB kinase complex (IKK) contains two kinase subunits, IKKα and IKKβ, necessary for IκB phosphorylation and NF-κB activation
    • Zandi E., Rothwarf D.M., Delhase M., Hayakawa M., Karin M. The IκB kinase complex (IKK) contains two kinase subunits, IKKα and IKKβ, necessary for IκB phosphorylation and NF-κB activation. Cell 1997, 91:243-252.
    • (1997) Cell , vol.91 , pp. 243-252
    • Zandi, E.1    Rothwarf, D.M.2    Delhase, M.3    Hayakawa, M.4    Karin, M.5
  • 18
    • 0034661272 scopus 로고    scopus 로고
    • Complete lack of NF-κB activity in IKK1 and IKK2 double-deficient mice: additional defect in neurulation
    • Li Q., Estepa G., Memet S., Israel A., Verma I.M. Complete lack of NF-κB activity in IKK1 and IKK2 double-deficient mice: additional defect in neurulation. Gene Dev. 2000, 14:1729-1733.
    • (2000) Gene Dev. , vol.14 , pp. 1729-1733
    • Li, Q.1    Estepa, G.2    Memet, S.3    Israel, A.4    Verma, I.M.5
  • 21
    • 0032477813 scopus 로고    scopus 로고
    • Nlk is a murine protein kinase related to Erk/MAP kinases and localized in the nucleus
    • Brott B.K., Pinsky B.A., Erikson R.L. Nlk is a murine protein kinase related to Erk/MAP kinases and localized in the nucleus. Proc. Natl. Acad. Sci. 1998, 95:963-968.
    • (1998) Proc. Natl. Acad. Sci. , vol.95 , pp. 963-968
    • Brott, B.K.1    Pinsky, B.A.2    Erikson, R.L.3
  • 22
    • 39149117397 scopus 로고    scopus 로고
    • Genetic knockouts and knockins in human somatic cells
    • Rago C., Vogelstein B., Bunz F. Genetic knockouts and knockins in human somatic cells. Nat. Protoc. 2007, 2:2734-2746.
    • (2007) Nat. Protoc. , vol.2 , pp. 2734-2746
    • Rago, C.1    Vogelstein, B.2    Bunz, F.3
  • 24
    • 1142275256 scopus 로고    scopus 로고
    • Nemo-like kinase suppresses a wide range of transcription factors, including nuclear factor-kappaB
    • Yasuda J., Yokoo H., Yamada T., Kitabayashi I., Sekiya T., Ichikawa H. Nemo-like kinase suppresses a wide range of transcription factors, including nuclear factor-kappaB. Cancer Sci. 2004, 95:52-57.
    • (2004) Cancer Sci. , vol.95 , pp. 52-57
    • Yasuda, J.1    Yokoo, H.2    Yamada, T.3    Kitabayashi, I.4    Sekiya, T.5    Ichikawa, H.6
  • 25
    • 78751499788 scopus 로고    scopus 로고
    • Homodimerization of nemo-like kinase is essential for activation and nuclear localization
    • Ishitani S., Inaba K., Matsumoto K., Ishitani T. Homodimerization of nemo-like kinase is essential for activation and nuclear localization. Mol. Biol. Cell 2011, 22:266-277.
    • (2011) Mol. Biol. Cell , vol.22 , pp. 266-277
    • Ishitani, S.1    Inaba, K.2    Matsumoto, K.3    Ishitani, T.4
  • 26
    • 33746198006 scopus 로고    scopus 로고
    • Homologous recombination is required for AAV-mediated gene targeting
    • Vasileva A., Linden R.M., Jessberger R. Homologous recombination is required for AAV-mediated gene targeting. Nucleic Acids Res. 2006, 34:3345-3360.
    • (2006) Nucleic Acids Res. , vol.34 , pp. 3345-3360
    • Vasileva, A.1    Linden, R.M.2    Jessberger, R.3
  • 27
    • 0029146930 scopus 로고
    • Signal-induced site-specific phosphorylation targets I kappa B alpha to the ubiquitin-proteasome pathway
    • Chen Z., Hagler J., Palombella V.J., Melandri F., Scherer D., Ballard D., Maniatis T. Signal-induced site-specific phosphorylation targets I kappa B alpha to the ubiquitin-proteasome pathway. Gene Dev. 1995, 9:1586-1597.
    • (1995) Gene Dev. , vol.9 , pp. 1586-1597
    • Chen, Z.1    Hagler, J.2    Palombella, V.J.3    Melandri, F.4    Scherer, D.5    Ballard, D.6    Maniatis, T.7
  • 30
  • 31
    • 0033537719 scopus 로고    scopus 로고
    • Positive and negative regulation of IκB kinase activity through IKKβ subunit phosphorylation
    • Delhase M., Hayakawa M., Chen Y., Karin M. Positive and negative regulation of IκB kinase activity through IKKβ 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.