메뉴 건너뛰기




Volumn 18, Issue 5, 1998, Pages 2640-2649

The N-terminal domain of IκBα masks the nuclear localization signal(s) of p50 and c-Rel homodimers

Author keywords

[No Author keywords available]

Indexed keywords

ANKYRIN; DNA BINDING PROTEIN; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; TRANSCRIPTION FACTOR;

EID: 0031897457     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/mcb.18.5.2640     Document Type: Article
Times cited : (62)

References (31)
  • 1
    • 0029874138 scopus 로고    scopus 로고
    • The NF-κB and IκB proteins: New discoveries and insights
    • Baldwin, A. S., Jr. 1996. The NF-κB and IκB proteins: new discoveries and insights. Annu. Rev. Immunol. 14:649-681.
    • (1996) Annu. Rev. Immunol. , vol.14 , pp. 649-681
    • Baldwin Jr., A.S.1
  • 2
    • 0026783210 scopus 로고
    • IκB interacts with the nuclear localization sequences of the subunits of NF-κB: A mechanism for cytoplasmic retention
    • Beg, A. A., S. M. Ruben, R. I. Scheinman, S. Haskill, C. A. Rosen, and A. S. Baldwin, Jr. 1992. IκB interacts with the nuclear localization sequences of the subunits of NF-κB: a mechanism for cytoplasmic retention. Genes Dev. 6:1899-1913.
    • (1992) Genes Dev. , vol.6 , pp. 1899-1913
    • Beg, A.A.1    Ruben, S.M.2    Scheinman, R.I.3    Haskill, S.4    Rosen, C.A.5    Baldwin Jr., A.S.6
  • 3
    • 0027530733 scopus 로고
    • Analysis of multiple mRNAs from pathogenic equine infectious anemia virus (EIAV) in an acutely infected horse reveals a novel protein, Ttm, derived from the carboxy terminus of the EIAV transmembrane protein
    • Beisel, C. E., J. F. Edwards, L. L. Dunn, and N. R. Rice. 1993. Analysis of multiple mRNAs from pathogenic equine infectious anemia virus (EIAV) in an acutely infected horse reveals a novel protein, Ttm, derived from the carboxy terminus of the EIAV transmembrane protein. J. Virol. 67:832-842.
    • (1993) J. Virol. , vol.67 , pp. 832-842
    • Beisel, C.E.1    Edwards, J.F.2    Dunn, L.L.3    Rice, N.R.4
  • 4
    • 0028929371 scopus 로고
    • Coupling of a signal response domain in IκBα to multiple pathways for NF-κB activation
    • Brockman, J., D. Scherer, T. McKinsey, S. Hall, X. Qi, W. Lee, and D. Ballard. 1995. Coupling of a signal response domain in IκBα to multiple pathways for NF-κB activation. Mol. Cell. Biol. 15:2809-2818.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 2809-2818
    • Brockman, J.1    Scherer, D.2    McKinsey, T.3    Hall, S.4    Qi, X.5    Lee, W.6    Ballard, D.7
  • 5
    • 0028986075 scopus 로고
    • Control of IκBα proteolysis by site-specific signal-induced phosphorylation
    • Brown, K., S. Gerstberger, L. Carlson, G. Franzoso, and U. Siebenlist. 1995. Control of IκBα proteolysis by site-specific signal-induced phosphorylation. Science 267:1485-1488.
    • (1995) Science , vol.267 , pp. 1485-1488
    • Brown, K.1    Gerstberger, S.2    Carlson, L.3    Franzoso, G.4    Siebenlist, U.5
  • 6
    • 0032556894 scopus 로고    scopus 로고
    • Crystal structure of p50/p65 heterodimer of transcription factor NF-κB bound to DNA
    • Chen, F. E., D.-B. Huang, Y.-Q. Chen, and G. Ghosh. 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
  • 7
    • 0031964687 scopus 로고    scopus 로고
    • A novel DNA recognition mode by the NF-κB p65 homodimer
    • Chen, Y.-Q., S. Ghosh, and G. Ghosh. 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
  • 8
    • 0029146930 scopus 로고
    • Signal-induced site-specific phosphorylation targets IκBα to the ubiquitin-proteasome pathway
    • Chen, Z., J. Hagler, V. Palombella, F. Melandri, D. Scherer, D. Ballard, and T. Maniatis. 1995. Signal-induced site-specific phosphorylation targets IκBα to the ubiquitin-proteasome pathway. Genes Dev. 9:1586-1597.
    • (1995) Genes Dev. , vol.9 , pp. 1586-1597
    • Chen, Z.1    Hagler, J.2    Palombella, V.3    Melandri, F.4    Scherer, D.5    Ballard, D.6    Maniatis, T.7
  • 9
    • 0028983432 scopus 로고
    • The PEST-like sequence of IκBα is responsible for inhibition of DNA binding but not for cytoplasmic retention of c-Rel or RelA homodimers
    • Ernst, M. K., L. L. Dunn, and N. R. Rice. 1995. The PEST-like sequence of IκBα is responsible for inhibition of DNA binding but not for cytoplasmic retention of c-Rel or RelA homodimers. Mol. Cell. Biol. 15:872-882.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 872-882
    • Ernst, M.K.1    Dunn, L.L.2    Rice, N.R.3
  • 10
    • 0027078835 scopus 로고
    • IκB/MAD-3 masks the nuclear localization signal of NF-κB p65 and requires the transactivation domain to inhibit NF-κB p65 DNA binding
    • Ganchi, P. A., S.-C. Sun, W. C. Greene, and D. W. Ballard. 1992. IκB/MAD-3 masks the nuclear localization signal of NF-κB p65 and requires the transactivation domain to inhibit NF-κB p65 DNA binding. Mol. Biol. Cell 3:1339-1352.
    • (1992) Mol. Biol. Cell , vol.3 , pp. 1339-1352
    • Ganchi, P.A.1    Sun, S.-C.2    Greene, W.C.3    Ballard, D.W.4
  • 11
    • 0028979479 scopus 로고
    • Structure of NF-κB p50 homodimer bound to a κB site
    • Ghosh, G., G. Va Duyne, S. Ghosh, and P. Sigler. 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    Va Duyne, G.2    Ghosh, S.3    Sigler, P.4
  • 12
    • 0030043628 scopus 로고    scopus 로고
    • Regulated nuclear import of the Drosophila Rel protein dorsal: Structure-function analysis
    • Govind, S., E. Drier, L. H. Huang, and R. Steward. 1996. Regulated nuclear import of the Drosophila Rel protein dorsal: structure-function analysis. Mol. Cell. Biol. 16:1103-1114.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 1103-1114
    • Govind, S.1    Drier, E.2    Huang, L.H.3    Steward, R.4
  • 13
    • 0027165587 scopus 로고
    • Common structural constituents confer IκB activity to NF-KB p105 and IκB/MAD-3
    • Hatada, E. N., M. Naumann, and C. Scheidereit. 1993. Common structural constituents confer IκB activity to NF-KB p105 and IκB/MAD-3. EMBO J. 12:2781-2788.
    • (1993) EMBO J. , vol.12 , pp. 2781-2788
    • Hatada, E.N.1    Naumann, M.2    Scheidereit, C.3
  • 14
    • 0026600367 scopus 로고
    • Direct association of pp40/IκBβ with rel/NF-κB transcription factors: Role of ankyrin repeats in the inhibition of DNA binding activity
    • Inoue, J.-I., L. D. Kerr, D. Rashid, N. Davis, H. R. Bose, Jr., and I. M. Verma. 1992. Direct association of pp40/IκBβ with rel/NF-κB transcription factors: role of ankyrin repeats in the inhibition of DNA binding activity. Proc. Natl. Acad. Sci. USA 89:4333-4337.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 4333-4337
    • Inoue, J.-I.1    Kerr, L.D.2    Rashid, D.3    Davis, N.4    Bose Jr., H.R.5    Verma, I.M.6
  • 15
    • 0028303967 scopus 로고
    • Disulfide cross-linking in crude embryonic lysates reveals three complexes of the Drosophila morphogen dorsal and its inhibitor cactus
    • Isoda, K., and C. Nüsslein-Volhard. 1994. Disulfide cross-linking in crude embryonic lysates reveals three complexes of the Drosophila morphogen dorsal and its inhibitor cactus. Proc. Natl. Acad. Sci. USA 91:5350-5354.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 5350-5354
    • Isoda, K.1    Nüsslein-Volhard, C.2
  • 16
    • 0027437904 scopus 로고
    • IκBα-mediated inhibition of v-Rel DNA binding requires direct interaction with the RxxRxRxxC Rel/κB DNA-binding motif
    • Kumar, S., and C. Gelinas. 1993. IκBα-mediated inhibition of v-Rel DNA binding requires direct interaction with the RxxRxRxxC Rel/κB DNA-binding motif. Proc. Natl. Acad. Sci. USA 90:8962-8966.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 8962-8966
    • Kumar, S.1    Gelinas, C.2
  • 18
    • 0027759889 scopus 로고
    • Diverse molecular mechanisms of inhibition of NF-κB/DNA binding complexes by IκB proteins
    • Léveillard, T., and I. M. Verma. 1993. Diverse molecular mechanisms of inhibition of NF-κB/DNA binding complexes by IκB proteins. Gene Exp. 3:135-150.
    • (1993) Gene Exp. , vol.3 , pp. 135-150
    • Léveillard, T.1    Verma, I.M.2
  • 19
    • 0027374511 scopus 로고
    • The membrane-binding domain of ankyrin contains four independently folded subdomains, each comprised of six ankyrin repeats
    • Michaely, P., and V. Bennett. 1993. The membrane-binding domain of ankyrin contains four independently folded subdomains, each comprised of six ankyrin repeats. J. Biol. Chem. 268:22703-22709.
    • (1993) J. Biol. Chem. , vol.268 , pp. 22703-22709
    • Michaely, P.1    Bennett, V.2
  • 21
    • 0028979476 scopus 로고
    • Structure of the NF-κB p50 homodimer bound to DNA
    • Muller, C., F. Rey, M. Sodeoka, G. Verdine, and S. Harrison. 1995. Structure of the NF-κB p50 homodimer bound to DNA. Nature 373:311-317.
    • (1995) Nature , vol.373 , pp. 311-317
    • Muller, C.1    Rey, F.2    Sodeoka, M.3    Verdine, G.4    Harrison, S.5
  • 22
    • 0026742527 scopus 로고
    • The precursor of NF-κB has IκB-like functions
    • Rice, N. R., M. L. MacKichan, and A. Israël. 1992. The precursor of NF-κB has IκB-like functions. Cell 71:243-253.
    • (1992) Cell , vol.71 , pp. 243-253
    • Rice, N.R.1    MacKichan, M.L.2    Israël, A.3
  • 23
    • 0022971952 scopus 로고
    • Amino acid sequences common to rapidly degraded proteins: The PEST hypothesis
    • Rogers, S., R. Wells, and M. Rechsteiner. 1986. Amino acid sequences common to rapidly degraded proteins: the PEST hypothesis. Science 234: 364-368.
    • (1986) Science , vol.234 , pp. 364-368
    • Rogers, S.1    Wells, R.2    Rechsteiner, M.3
  • 24
    • 0029916228 scopus 로고    scopus 로고
    • PEST-dependent cytoplasmic retention of v-Rel by IκBα: Evidence that IκB-α regulates cellular localization of c-Rel and v-Rel by distinct mechanisms
    • Rottjakob, E. M., S. Sachdev, C. A. Leanna, T. A. McKinsey, and M. Hannink. 1996. PEST-dependent cytoplasmic retention of v-Rel by IκBα: evidence that IκB-α regulates cellular localization of c-Rel and v-Rel by distinct mechanisms. J. Virol. 70:3176-3188.
    • (1996) J. Virol. , vol.70 , pp. 3176-3188
    • Rottjakob, E.M.1    Sachdev, S.2    Leanna, C.A.3    McKinsey, T.A.4    Hannink, M.5
  • 25
    • 0026665460 scopus 로고
    • κB site-dependent activation of the interleukin-2 receptor a-chain gene promoter by human c-Rel
    • Tan, T.-H., G. P. Huang, A. Sica, P. Ghosh, H. A. Young, D. L. Longo, and N. R. Rice. 1992. κB site-dependent activation of the interleukin-2 receptor a-chain gene promoter by human c-Rel. Mol. Cell. Biol. 12:4067-4075.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 4067-4075
    • Tan, T.-H.1    Huang, G.P.2    Sica, A.3    Ghosh, P.4    Young, H.A.5    Longo, D.L.6    Rice, N.R.7
  • 26
    • 0029060770 scopus 로고
    • Specificity of rel-inhibitor interactions in Drosophila embryos
    • Tatei, K., and M. Levine. 1995. Specificity of rel-inhibitor interactions in Drosophila embryos. Mol. Cell. Biol. 15:3627-3634.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 3627-3634
    • Tatei, K.1    Levine, M.2
  • 27
    • 0028986194 scopus 로고
    • IκBβ regulates the persistent response in a biphasic activation of NF-κB
    • Thompson, J. E., R. J. Phillips, H. Erdjument-Bromage, P. Tempst, and S. Ghosh. 1995. IκBβ regulates the persistent response in a biphasic activation of NF-κB. Cell 80:573-582.
    • (1995) Cell , vol.80 , pp. 573-582
    • Thompson, J.E.1    Phillips, R.J.2    Erdjument-Bromage, H.3    Tempst, P.4    Ghosh, S.5
  • 28
    • 0028978032 scopus 로고
    • Phosphorylation of human IκBα on serines 32 and 36 controls IκBα proteolysis and NF-KB activation in response to diverse stimuli
    • Traenckner, E., H. Pahl, T. Henkel, K. Schmidt, S. Wilk, and P. Baeuerle. 1995. Phosphorylation of human IκBα on serines 32 and 36 controls IκBα proteolysis and NF-KB activation in response to diverse stimuli. EMBO J. 14:2876-2883.
    • (1995) EMBO J. , vol.14 , pp. 2876-2883
    • Traenckner, E.1    Pahl, H.2    Henkel, T.3    Schmidt, K.4    Wilk, S.5    Baeuerle, P.6
  • 29
    • 0030899121 scopus 로고    scopus 로고
    • I kappa B epsilon, a novel member of the IκB family, controls RelA and cRel NF-κB activity
    • Whiteside, S. T., J.-C. Epinat, N. R. Rice, and A. Israel. 1997. I kappa B epsilon, a novel member of the IκB family, controls RelA and cRel NF-κB activity. EMBO J. 16:1413-1426.
    • (1997) EMBO J. , vol.16 , pp. 1413-1426
    • Whiteside, S.T.1    Epinat, J.-C.2    Rice, N.R.3    Israel, A.4
  • 30
    • 0029122799 scopus 로고
    • N- and C-terminal sequences control degradation of MAD3/IκBα in response to inducers of NF-κB activity
    • Whiteside, S. T., M. K. Ernst, O. LeBail, C. Laurent-Winter, N. Rice, and A. Israël. 1995. 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) Mol. Cell. Biol. , vol.15 , pp. 5339-5345
    • Whiteside, S.T.1    Ernst, M.K.2    LeBail, O.3    Laurent-Winter, C.4    Rice, N.5    Israël, A.6
  • 31
    • 0030615020 scopus 로고    scopus 로고
    • Distinct domains of IκB-α inhibit human immunodeficiency virus type 1 replication through NF-κB and Rev
    • Wu, B.-Y., C. Woffendin, I. MacLachlan, and G. J. Nabel. 1997. Distinct domains of IκB-α inhibit human immunodeficiency virus type 1 replication through NF-κB and Rev. J. Virol. 71:3161-3167.
    • (1997) J. Virol. , vol.71 , pp. 3161-3167
    • Wu, B.-Y.1    Woffendin, C.2    MacLachlan, I.3    Nabel, G.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.