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Volumn 64, Issue 6, 2012, Pages 499-505

Role of disorder in IκB-NFκB interaction

Author keywords

eukaryotic gene expression; NF B AP1; NMR spectroscopy; protein structure; signaling; stress activated signaling; transcriptional regulation

Indexed keywords

GLUTAMIC ACID; HOMODIMER; I KAPPA B; I KAPPA B KINASE ALPHA; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; PROLINE; SYNAPTOTAGMIN I; UBIQUITIN;

EID: 84861312715     PISSN: 15216543     EISSN: 15216551     Source Type: Journal    
DOI: 10.1002/iub.1044     Document Type: Review
Times cited : (45)

References (35)
  • 1
    • 0022930702 scopus 로고
    • Inducibility of κ immunoglobulin enhancer-binding protein NF-κB by a posttranslational mechanism
    • Sen, R., and, Baltimore, D., (1986) Inducibility of κ immunoglobulin enhancer-binding protein NF-κB by a posttranslational mechanism. Cell 47, 921-928.
    • (1986) Cell , vol.47 , pp. 921-928
    • Sen, R.1    Baltimore, D.2
  • 2
    • 0032217267 scopus 로고    scopus 로고
    • IκB-NF-κB structures: At the interface of inflammation control
    • Baeuerle, P. A., (1998) IκB-NF-κB structures: at the interface of inflammation control. Cell 95, 729-731.
    • (1998) Cell , vol.95 , pp. 729-731
    • Baeuerle, P.A.1
  • 3
    • 0028174061 scopus 로고
    • Function and activation of NF-κB in the immune system
    • Baeuerle, P. A., and, Henkel, T., (1994) Function and activation of NF-κB in the immune system. Annu. Rev. Immunol. 12, 141-179.
    • (1994) Annu. Rev. Immunol. , vol.12 , pp. 141-179
    • Baeuerle, P.A.1    Henkel, T.2
  • 4
    • 0036546501 scopus 로고    scopus 로고
    • NF-κB in cancer: From innocent bystander to major culprit
    • Karin, M., Cao, Y., Greten, F. R., and, Li, Z. W., (2002) NF-κB in cancer: from innocent bystander to major culprit. Nat. Rev. Cancer 2, 301-310.
    • (2002) Nat. Rev. Cancer , vol.2 , pp. 301-310
    • Karin, M.1    Cao, Y.2    Greten, F.R.3    Li, Z.W.4
  • 5
    • 0034746919 scopus 로고    scopus 로고
    • NF-κB: A key role in inflammatory diseases
    • Tak, P. P., and, Firestein, G. S., (2001) NF-κB: a key role in inflammatory diseases. J. Clin. Invest. 107, 7-11.
    • (2001) J. Clin. Invest. , vol.107 , pp. 7-11
    • Tak, P.P.1    Firestein, G.S.2
  • 6
    • 0036009115 scopus 로고    scopus 로고
    • NF-κB at the crossroads of life and death
    • Karin, M., and, Lin, A., (2002) NF-κB at the crossroads of life and death. Nat. Immunol. 3, 221-227.
    • (2002) Nat. Immunol. , vol.3 , pp. 221-227
    • Karin, M.1    Lin, A.2
  • 7
    • 0035411587 scopus 로고    scopus 로고
    • Role of the NF-κB pathway in the pathogenesis of human disease states
    • Yamamoto, Y., and, Gaynor, R. B., (2001) Role of the NF-κB pathway in the pathogenesis of human disease states. Curr. Mol. Med. 1, 287-296.
    • (2001) Curr. Mol. Med. , vol.1 , pp. 287-296
    • Yamamoto, Y.1    Gaynor, R.B.2
  • 8
    • 0036931719 scopus 로고    scopus 로고
    • Solvent exposed non-contacting amino acids play a critical role in NF-κB/IκBkα complex formation
    • Huxford, T., Mishler, D., Phelps, C. B., Huang, D. B., Sengchanthalangsy, L. L., et al. (2002) Solvent exposed non-contacting amino acids play a critical role in NF-κB/IκBkα complex formation. J. Mol. Biol. 324, 587-597.
    • (2002) J. Mol. Biol. , vol.324 , pp. 587-597
    • Huxford, T.1    Mishler, D.2    Phelps, C.B.3    Huang, D.B.4    Sengchanthalangsy, L.L.5
  • 9
    • 0033596120 scopus 로고    scopus 로고
    • Regulation of DNA binding by Rel/NF-κB transcription factors: Structural views
    • Chen, F. E., and, Ghosh, G., (1999) Regulation of DNA binding by Rel/NF-κB transcription factors: structural views. Oncogene 18, 6845-6852.
    • (1999) Oncogene , vol.18 , pp. 6845-6852
    • Chen, F.E.1    Ghosh, G.2
  • 12
    • 77749298990 scopus 로고    scopus 로고
    • Molecular mechanisms of system control of NF-κB signaling by IκBα
    • Ferreiro, D. U., and, Komives, E. A., (2010) Molecular mechanisms of system control of NF-κB signaling by IκBα. Biochemistry 49, 1560-1567.
    • (2010) Biochemistry , vol.49 , pp. 1560-1567
    • Ferreiro, D.U.1    Komives, E.A.2
  • 13
    • 84856641109 scopus 로고    scopus 로고
    • NF-κB, the first quarter-century: Remarkable progress and outstanding questions
    • Hayden, M. S., and, Ghosh, S., (2012) NF-κB, the first quarter-century: remarkable progress and outstanding questions. Genes Dev. 26, 203-234.
    • (2012) Genes Dev. , vol.26 , pp. 203-234
    • Hayden, M.S.1    Ghosh, S.2
  • 14
    • 0028979479 scopus 로고
    • Structure of NF-κB p50 homodimer bound to a κb site
    • Ghosh, G., Van Duyne, G., Ghosh, S., and, Sigler, P. B., (1995) Structure of NF-κB p50 homodimer bound to a κB site. Nature 373, 303-310.
    • (1995) Nature , vol.373 , pp. 303-310
    • Ghosh, G.1    Van Duyne, G.2    Ghosh, S.3    Sigler, P.B.4
  • 15
    • 0032556894 scopus 로고    scopus 로고
    • Crystal structure of p50/p65 heterodimer of transcription factor NF-κB bound to DNA
    • Chen, F. E., Huang, D. B., Chen, Y. Q., and, Ghosh, G., (1998) Crystal structure of p50/p65 heterodimer of transcription factor NF-κB bound to DNA. Nature 391, 410-413.
    • (1998) Nature , vol.391 , pp. 410-413
    • Chen, F.E.1    Huang, D.B.2    Chen, Y.Q.3    Ghosh, G.4
  • 16
    • 0031964687 scopus 로고    scopus 로고
    • A novel DNA recognition mode by the NF-κB p65 homodimer
    • Chen, Y.-Q., Ghosh, S., and, Ghosh, G., (1998) A novel DNA recognition mode by the NF-κB p65 homodimer. Nat. Struct. Biol. 5, 67-73.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 67-73
    • Chen, Y.-Q.1    Ghosh, S.2    Ghosh, G.3
  • 17
    • 0032217264 scopus 로고    scopus 로고
    • Structure of an IκBα/NF-κB complex
    • Jacobs, M. D., and, Harrison, S. C., (1998) Structure of an IκBα/NF-κB complex. Cell 95, 749-758.
    • (1998) Cell , vol.95 , pp. 749-758
    • Jacobs, M.D.1    Harrison, S.C.2
  • 18
    • 0032217268 scopus 로고    scopus 로고
    • The crystal structure of the IκBα/NF-κB complex reveals mechanisms of NF-κB inactivation
    • Huxford, T., Huang, D. B., Malek, S., and, Ghosh, G., (1998) The crystal structure of the IκBα/NF-κB complex reveals mechanisms of NF-κB inactivation. Cell 95, 759-770.
    • (1998) Cell , vol.95 , pp. 759-770
    • Huxford, T.1    Huang, D.B.2    Malek, S.3    Ghosh, G.4
  • 19
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • Koradi, R., Billeter, M., and, Wüthrich, K., (1996) MOLMOL: a program for display and analysis of macromolecular structures. J. Mol. Graph. 14, 51-55.
    • (1996) J. Mol. Graph. , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wüthrich, K.3
  • 20
    • 33847165830 scopus 로고    scopus 로고
    • Induced fit, folding, and recognition of the NF-κB-nuclear localization signals by IκBα and IκBβ
    • Lätzer, J., Papoian, G. A., Prentiss, M. C., Komives, E. A., and, Wolynes, P. G., (2007) Induced fit, folding, and recognition of the NF-κB-nuclear localization signals by IκBα and IκBβ. J. Mol. Biol. 367, 262-274.
    • (2007) J. Mol. Biol. , vol.367 , pp. 262-274
    • Lätzer, J.1    Papoian, G.A.2    Prentiss, M.C.3    Komives, E.A.4    Wolynes, P.G.5
  • 21
    • 78650873864 scopus 로고    scopus 로고
    • The RelA nuclear localization signal folds upon binding to IκBα
    • Cervantes, C. F., Bergqvist, S., Kjaergaard, M., Kroon, G., Sue, S. C., et al. (2011) The RelA nuclear localization signal folds upon binding to IκBα. J. Mol. Biol. 405, 754-764.
    • (2011) J. Mol. Biol. , vol.405 , pp. 754-764
    • Cervantes, C.F.1    Bergqvist, S.2    Kjaergaard, M.3    Kroon, G.4    Sue, S.C.5
  • 22
    • 0028148227 scopus 로고
    • A proteasome inhibitor prevents activation of NF-κB and stabilizes a newly phosphorylated form of IκBα that is still bound to NF-κB
    • Traenckner, E. B., Wilk, S., and, Baeuerle, P. A., (1994) A proteasome inhibitor prevents activation of NF-κB and stabilizes a newly phosphorylated form of IκBα that is still bound to NF-κB. EMBO J. 13, 5433-5441.
    • (1994) EMBO J. , vol.13 , pp. 5433-5441
    • Traenckner, E.B.1    Wilk, S.2    Baeuerle, P.A.3
  • 23
    • 0034653375 scopus 로고    scopus 로고
    • Crystallographic analysis of the specific yet versatile recognition of distinct nuclear localization signals by karyopherin α
    • Conti, E., and, Kuriyan, J., (2000) Crystallographic analysis of the specific yet versatile recognition of distinct nuclear localization signals by karyopherin α. Structure 8, 329-338.
    • (2000) Structure , vol.8 , pp. 329-338
    • Conti, E.1    Kuriyan, J.2
  • 24
    • 3042628330 scopus 로고    scopus 로고
    • Biophysical characterization of the free IκBα ankyrin repeat domain in solution
    • Croy, C. H., Bergqvist, S., Huxford, T., Ghosh, G., and, Komives, E. A., (2004) Biophysical characterization of the free IκBα ankyrin repeat domain in solution. Protein Sci. 13, 1767-1777.
    • (2004) Protein Sci. , vol.13 , pp. 1767-1777
    • Croy, C.H.1    Bergqvist, S.2    Huxford, T.3    Ghosh, G.4    Komives, E.A.5
  • 25
    • 34447628760 scopus 로고    scopus 로고
    • Regions of IκBα that are critical for its inhibition of NF-κB.DNA interaction fold upon binding to NF-κB
    • Truhlar, S. M., Torpey, J. W., and, Komives, E. A., (2006) Regions of IκBα that are critical for its inhibition of NF-κB.DNA interaction fold upon binding to NF-κB. Proc. Natl. Acad. Sci. USA 103, 18951-18956.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 18951-18956
    • Truhlar, S.M.1    Torpey, J.W.2    Komives, E.A.3
  • 26
    • 45849140515 scopus 로고    scopus 로고
    • Transfer of flexibility between ankyrin repeats in IκBα upon formation of the NF-κB complex
    • Sue, S. C., Cervantes, C., Komives, E. A., and, Dyson, H. J., (2008) Transfer of flexibility between ankyrin repeats in IκBα upon formation of the NF-κB complex. J. Mol. Biol. 380, 917-931.
    • (2008) J. Mol. Biol. , vol.380 , pp. 917-931
    • Sue, S.C.1    Cervantes, C.2    Komives, E.A.3    Dyson, H.J.4
  • 29
    • 56749183334 scopus 로고    scopus 로고
    • The IκBα/NF-κB complex has two hot spots, one at either end of the interface
    • Bergqvist, S., Ghosh, G., and, Komives, E. A., (2008) The IκBα/NF-κB complex has two hot spots, one at either end of the interface. Protein Sci. 17, 2051-2058.
    • (2008) Protein Sci. , vol.17 , pp. 2051-2058
    • Bergqvist, S.1    Ghosh, G.2    Komives, E.A.3
  • 30
    • 79959946164 scopus 로고    scopus 로고
    • Visualization of the nanospring dynamics of the IκBα ankyrin repeat domain in real time
    • Lamboy, J. A., Kim, H., Lee, K. S., Ha, T., and, Komives, E. A., (2011) Visualization of the nanospring dynamics of the IκBα ankyrin repeat domain in real time. Proc. Natl. Acad. Sci. USA 108, 10178-10183.
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 10178-10183
    • Lamboy, J.A.1    Kim, H.2    Lee, K.S.3    Ha, T.4    Komives, E.A.5
  • 31
    • 0025304791 scopus 로고
    • Purified human IκB can rapidly dissociate the complex of the NF-κB transcription factor with its cognate DNA
    • Zabel, U., and, Baeuerle, P. A., (1990) Purified human IκB can rapidly dissociate the complex of the NF-κB transcription factor with its cognate DNA. Cell 61, 255-265.
    • (1990) Cell , vol.61 , pp. 255-265
    • Zabel, U.1    Baeuerle, P.A.2
  • 32
    • 33745276259 scopus 로고    scopus 로고
    • Thermodynamics reveal that helix four in the NLS of NF-κB p65 anchors IκBα, forming a very stable complex
    • Bergqvist, S., Croy, C. H., Kjaergaard, M., Huxford, T., Ghosh, G., et al. (2006) Thermodynamics reveal that helix four in the NLS of NF-κB p65 anchors IκBα, forming a very stable complex. J. Mol. Biol. 360, 421-434.
    • (2006) J. Mol. Biol. , vol.360 , pp. 421-434
    • Bergqvist, S.1    Croy, C.H.2    Kjaergaard, M.3    Huxford, T.4    Ghosh, G.5
  • 34
    • 79952130173 scopus 로고    scopus 로고
    • Detection of a ternary complex of NF-κB and IκBa with DNA provides insights into how IκBα removes NF-κB from transcription sites
    • Sue, S. C., Alverdi, V., Komives, E. A., and, Dyson, H. J., (2011) Detection of a ternary complex of NF-κB and IκBa with DNA provides insights into how IκBα removes NF-κB from transcription sites. Proc. Natl. Acad. Sci. USA 108, 1367-1372.
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 1367-1372
    • Sue, S.C.1    Alverdi, V.2    Komives, E.A.3    Dyson, H.J.4
  • 35
    • 34248997836 scopus 로고    scopus 로고
    • A homeostatic model of IκB metabolism to control constitutive NF-κB activity
    • O'Dea, E. L., Barken, D., Peralta, R. Q., Tran, K. T., Werner, S. L., et al. (2007) A homeostatic model of IκB metabolism to control constitutive NF-κB activity. Mol. Syst. Biol. 3, 111.
    • (2007) Mol. Syst. Biol. , vol.3 , pp. 111
    • O'Dea, E.L.1    Barken, D.2    Peralta, R.Q.3    Tran, K.T.4    Werner, S.L.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.