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Volumn 1, Issue 5, 1998, Pages 661-671

Phosphorylation of NF-κB p65 by PKA stimulates transcriptional activity by promoting a novel bivalent interaction with the coactivator CBP/p300

Author keywords

[No Author keywords available]

Indexed keywords

ACYLTRANSFERASE; CELL CYCLE PROTEIN; CREBBP PROTEIN, HUMAN; CYCLIC AMP DEPENDENT PROTEIN KINASE; CYCLIC AMP RESPONSIVE ELEMENT BINDING PROTEIN BINDING PROTEIN; GAL4 PROTEIN, S CEREVISIAE; HISTONE ACETYLTRANSFERASE; HISTONE ACETYLTRANSFERASE PCAF; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; NUCLEAR PROTEIN; NUCLEAR RECEPTOR COACTIVATOR 3; P300-CBP-ASSOCIATED FACTOR; PCAF PROTEIN, HUMAN; PEPTIDE FRAGMENT; SACCHAROMYCES CEREVISIAE PROTEIN; SERINE; TRANSACTIVATOR PROTEIN; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR RELA;

EID: 0032039076     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1097-2765(00)80066-0     Document Type: Article
Times cited : (1052)

References (36)
  • 2
    • 0029874138 scopus 로고    scopus 로고
    • The NF-κB and IκB proteins: New discoveries and insights
    • Baldwin, A.S. (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, A.S.1
  • 3
    • 0030480969 scopus 로고    scopus 로고
    • The CBP co-activator is a histone acetyltransferase
    • Bannister, A.J., and Kouzarides, T. (1996). The CBP co-activator is a histone acetyltransferase. Nature 384, 641-643.
    • (1996) Nature , vol.384 , pp. 641-643
    • Bannister, A.J.1    Kouzarides, T.2
  • 4
    • 0029585553 scopus 로고
    • Stimulation of c-Jun activity by CBP: c-Jun residues Ser63/ 73 are required for CBP-induced stimulation in vivo and CBP binding in vitro
    • Bannister, A.J., Oehler, T., Wilhelm, D., Angel, P., and Kouzarides, T. (1995). Stimulation of c-Jun activity by CBP: c-Jun residues Ser63/ 73 are required for CBP-induced stimulation in vivo and CBP binding in vitro. Oncogene 11, 2509-2514.
    • (1995) Oncogene , vol.11 , pp. 2509-2514
    • Bannister, A.J.1    Oehler, T.2    Wilhelm, D.3    Angel, P.4    Kouzarides, T.5
  • 6
    • 0028089315 scopus 로고
    • Interleukin 2 transcription factors as molecular targets of cAMP inhibition: Delayed inhibition kinetics and combinatorial transcription roles
    • Chen, D., and Rothenberg, E.V. (1994). Interleukin 2 transcription factors as molecular targets of cAMP inhibition: delayed inhibition kinetics and combinatorial transcription roles. J. Exp. Med. 179, 931-942.
    • (1994) J. Exp. Med. , vol.179 , pp. 931-942
    • Chen, D.1    Rothenberg, E.V.2
  • 8
    • 0031032594 scopus 로고    scopus 로고
    • Characterization of monoclonal antibodies raised against p300: Both p300 and CBP are present in intracellular TBP complexes
    • Dallas, P.B., Yaciuk, P., and Moran, E. (1997). Characterization of monoclonal antibodies raised against p300: both p300 and CBP are present in intracellular TBP complexes. J. Virol. 71, 1726-1731.
    • (1997) J. Virol. , vol.71 , pp. 1726-1731
    • Dallas, P.B.1    Yaciuk, P.2    Moran, E.3
  • 9
    • 0029786902 scopus 로고    scopus 로고
    • The EVES motif mediates both intermolecular and intramolecular regulation of c-Myb
    • Dash, A.B., Orrico, F.C., and Ness, S.A. (1996). The EVES motif mediates both intermolecular and intramolecular regulation of c-Myb. Genes Dev. 10, 1858-1869.
    • (1996) Genes Dev. , vol.10 , pp. 1858-1869
    • Dash, A.B.1    Orrico, F.C.2    Ness, S.A.3
  • 10
    • 0029825698 scopus 로고    scopus 로고
    • Interaction and functional collaboration of p300/CBP and bHLH proteins in muscle and B-cell differentiation
    • Eckner, R., Yao, T.P., Oldread, E., and Livingston, D.M. (1996). Interaction and functional collaboration of p300/CBP and bHLH proteins in muscle and B-cell differentiation. Genes Dev. 10, 2478-2490.
    • (1996) Genes Dev. , vol.10 , pp. 2478-2490
    • Eckner, R.1    Yao, T.P.2    Oldread, E.3    Livingston, D.M.4
  • 12
    • 0030797585 scopus 로고    scopus 로고
    • Activation of p53 sequence-specific DNA binding by acetylation of the p53 C-terminal domain
    • Gu, W., and Roeder, R.G. (1997). Activation of p53 sequence-specific DNA binding by acetylation of the p53 C-terminal domain. Cell 90, 595-606.
    • (1997) Cell , vol.90 , pp. 595-606
    • Gu, W.1    Roeder, R.G.2
  • 13
    • 0030570961 scopus 로고    scopus 로고
    • A growing coactivator network
    • Janknecht, R., and Hunter, T. (1996a). A growing coactivator network. Nature 383, 22-23.
    • (1996) Nature , vol.383 , pp. 22-23
    • Janknecht, R.1    Hunter, T.2
  • 14
    • 0030207894 scopus 로고    scopus 로고
    • Transcriptional control: Versatile molecular glue
    • Janknecht, R., and Hunter, T. (1996b). Transcriptional control: versatile molecular glue. Curr. Biol. 6, 951-954.
    • (1996) Curr. Biol. , vol.6 , pp. 951-954
    • Janknecht, R.1    Hunter, T.2
  • 15
    • 0029991520 scopus 로고    scopus 로고
    • Regulation of the c-fos promoter by the ternary complex factor Sap-1a and its coactivator CBP
    • Janknecht, R., and Nordheim, A. (1996). Regulation of the c-fos promoter by the ternary complex factor Sap-1a and its coactivator CBP. Oncogene 12, 1961-1969.
    • (1996) Oncogene , vol.12 , pp. 1961-1969
    • Janknecht, R.1    Nordheim, A.2
  • 16
    • 0027454228 scopus 로고
    • Association between proto-oncoprotein Rel and TATA-binding protein mediates transcriptional activation by NF-κB
    • Kerr, L.D., Ransone, L.J., Wamsley, P., Schmitt, M.J., Boyer, T.G., Zhou, Q., Berk, A.J., and Verma, I.M. (1993). Association between proto-oncoprotein Rel and TATA-binding protein mediates transcriptional activation by NF-κB. Nature 365, 412-419.
    • (1993) Nature , vol.365 , pp. 412-419
    • Kerr, L.D.1    Ransone, L.J.2    Wamsley, P.3    Schmitt, M.J.4    Boyer, T.G.5    Zhou, Q.6    Berk, A.J.7    Verma, I.M.8
  • 20
    • 0031126702 scopus 로고    scopus 로고
    • Rel/NF-κB and IκB proteins: An overview
    • May, M.J., and Ghosh, S. (1997). Rel/NF-κB and IκB proteins: an overview. Semin. Cancer Biol. 8, 63-73.
    • (1997) Semin. Cancer Biol. , vol.8 , pp. 63-73
    • May, M.J.1    Ghosh, S.2
  • 22
    • 0025975795 scopus 로고
    • DNA binding and IκB inhibition of the cloned p65 subunit of NF-κB, a rel-related polypeptide
    • Nolan, G., Ghosh, S., Liou, H.-C., Tempst, P., and Baltimore, D. (1991). DNA binding and IκB inhibition of the cloned p65 subunit of NF-κB, a rel-related polypeptide. Cell 64, 961-969.
    • (1991) Cell , vol.64 , pp. 961-969
    • Nolan, G.1    Ghosh, S.2    Liou, H.-C.3    Tempst, P.4    Baltimore, D.5
  • 23
    • 0029886810 scopus 로고    scopus 로고
    • Interaction of the co-activator CBP with Myb proteins: Effects on Myb-specific transactivatioon and on the cooperativity with NF-M
    • Oelgeschlager, M., Janknecht, R., Krieg, J., Schreek, S., and Luscher, B. (1996). Interaction of the co-activator CBP with Myb proteins: effects on Myb-specific transactivatioon and on the cooperativity with NF-M. EMBO J. 15, 2771-2780.
    • (1996) EMBO J. , vol.15 , pp. 2771-2780
    • Oelgeschlager, M.1    Janknecht, R.2    Krieg, J.3    Schreek, S.4    Luscher, B.5
  • 24
    • 0030606239 scopus 로고    scopus 로고
    • The transcriptional coactivators p300 and CBP are histone acetyltransferases
    • Ogryzko, V.V., Schiltz, R.L., Russanova, V., Howard, B.H., and Nakatani, Y. (1996). The transcriptional coactivators p300 and CBP are histone acetyltransferases. Cell 87, 953-959.
    • (1996) Cell , vol.87 , pp. 953-959
    • Ogryzko, V.V.1    Schiltz, R.L.2    Russanova, V.3    Howard, B.H.4    Nakatani, Y.5
  • 26
    • 0031040798 scopus 로고    scopus 로고
    • Distinct domains of adenovirus E1A interact with specific cellular factors to differentially modulate human immunodeficiency virus transcription
    • Parker, S.F., Felzien, L.K., Perkins, N.D., Imperiale, M.J., and Nabel, G.J. (1997). Distinct domains of adenovirus E1A interact with specific cellular factors to differentially modulate human immunodeficiency virus transcription. J. Virol. 71, 2004-2012.
    • (1997) J. Virol. , vol.71 , pp. 2004-2012
    • Parker, S.F.1    Felzien, L.K.2    Perkins, N.D.3    Imperiale, M.J.4    Nabel, G.J.5
  • 27
    • 0030614504 scopus 로고    scopus 로고
    • Regulation of NF-κB by cyclin-dependent kinases associated with the p300 coactivator
    • Perkins, N.D., Felzien, L.K., Betts, J.C., Leung, K., Beach, D.H., and Nabel, G.J. (1997). Regulation of NF-κB by cyclin-dependent kinases associated with the p300 coactivator. Science 275, 523-527.
    • (1997) Science , vol.275 , pp. 523-527
    • Perkins, N.D.1    Felzien, L.K.2    Betts, J.C.3    Leung, K.4    Beach, D.H.5    Nabel, G.J.6
  • 28
    • 0028116117 scopus 로고
    • Structural and functional analysis of the NF-κB p65 C terminus. An acidic and modular transactivation domain with the potential to adopt an alpha-helical conformation
    • Schmitz, M.L., dos Santos Silva, M.A., Altmann, H., Czisch, M., Holak, T.A., and Baeuerle, P.A. (1994). Structural and functional analysis of the NF-κB p65 C terminus. An acidic and modular transactivation domain with the potential to adopt an alpha-helical conformation. J. Biol. Chem. 269, 25613-25620.
    • (1994) J. Biol. Chem. , vol.269 , pp. 25613-25620
    • Schmitz, M.L.1    Dos Santos Silva, M.A.2    Altmann, H.3    Czisch, M.4    Holak, T.A.5    Baeuerle, P.A.6
  • 29
    • 0029058962 scopus 로고
    • Transactivation domain 2 (TA2) of p65 NF-κB. Similarity to TA1 and phorbol ester-stimulated activity and phosphorylation in intact cells
    • Schmitz, M.L., dos Santos Silva, M.A., and Baeuerle, P.A. (1995a). Transactivation domain 2 (TA2) of p65 NF-κB. Similarity to TA1 and phorbol ester-stimulated activity and phosphorylation in intact cells. J. Biol. Chem. 270, 15576-15584.
    • (1995) J. Biol. Chem. , vol.270 , pp. 15576-15584
    • Schmitz, M.L.1    Dos Santos Silva, M.A.2    Baeuerle, P.A.3
  • 30
    • 0028960452 scopus 로고
    • Interaction of the COOH-terminal transactivation domain of p65 NF-κB with TATA-binding protein, transcription factor IIB, and coactivators
    • Schmitz, M.L., Stelzer, G., Altmann, H., Meisterernst, M., and Baeuerle, P.A. (1995b). Interaction of the COOH-terminal transactivation domain of p65 NF-κB with TATA-binding protein, transcription factor IIB, and coactivators. J. Biol. Chem. 270, 7219-7226.
    • (1995) J. Biol. Chem. , vol.270 , pp. 7219-7226
    • Schmitz, M.L.1    Stelzer, G.2    Altmann, H.3    Meisterernst, M.4    Baeuerle, P.A.5
  • 31
    • 0029904571 scopus 로고    scopus 로고
    • CREB-binding protein activates transcription through multiple domains
    • Swope, D.L., Mueller, C.L., and Chrivia, J.C. (1996). CREB-binding protein activates transcription through multiple domains. J. Biol. Chem. 277, 28138-28145.
    • (1996) J. Biol. Chem. , vol.277 , pp. 28138-28145
    • Swope, D.L.1    Mueller, C.L.2    Chrivia, J.C.3
  • 32
    • 0026489365 scopus 로고
    • The high mobility group protein HMG I(Y) is required for NF-κB-dependent virus induction of the human IFN-β gene
    • Thanos, D., and Maniatis, T. (1992).The high mobility group protein HMG I(Y) is required for NF-κB-dependent virus induction of the human IFN-β gene. Cell 71, 777-789.
    • (1992) Cell , vol.71 , pp. 777-789
    • Thanos, D.1    Maniatis, T.2
  • 33
    • 0028986194 scopus 로고
    • IκB-β regulates the persistent response in a biphasic activation of NF-κB
    • Thompson, J., Phillips, R., Erdjument-Bromage, H., Tempst, P., and Ghosh, S. (1995). IκB-β regulates the persistent response in a biphasic activation of NF-κB. Cell 80, 573-582.
    • (1995) Cell , vol.80 , pp. 573-582
    • Thompson, J.1    Phillips, R.2    Erdjument-Bromage, H.3    Tempst, P.4    Ghosh, S.5
  • 34
    • 0029665857 scopus 로고    scopus 로고
    • A p300/CBP-associated factor that competes with the adenoviral oncoprotein E1A
    • Yang, X.J., Ogryzko, V.V., Nishikawa, J., Howard, B.H., and Nakatani, Y. (1996). A p300/CBP-associated factor that competes with the adenoviral oncoprotein E1A. Nature 382, 319-324.
    • (1996) Nature , vol.382 , pp. 319-324
    • Yang, X.J.1    Ogryzko, V.V.2    Nishikawa, J.3    Howard, B.H.4    Nakatani, Y.5
  • 35
    • 0029968939 scopus 로고    scopus 로고
    • Human p300 protein is a coactivator for the transcription factor MyoD
    • Yuan, W., Condorelli, G., Caruso, M., Felsani, A., and Giordano, A. (1996). Human p300 protein is a coactivator for the transcription factor MyoD. J. Biol. Chem. 277, 9009-9013.
    • (1996) J. Biol. Chem. , vol.277 , pp. 9009-9013
    • Yuan, W.1    Condorelli, G.2    Caruso, M.3    Felsani, A.4    Giordano, A.5
  • 36
    • 0030991201 scopus 로고    scopus 로고
    • The transcriptional activity of NF-κB is regulated by the IκB-associated PKAc subunit through a cyclic AMP-independent mechanism
    • Zhong, H., SuYang, H., Erdjument-Bromage, H., Tempst, P., and Ghosh, S. (1997). The transcriptional activity of NF-κB is regulated by the IκB-associated PKAc subunit through a cyclic AMP-independent mechanism. Cell 89, 413-424.
    • (1997) Cell , vol.89 , pp. 413-424
    • Zhong, H.1    Suyang, H.2    Erdjument-Bromage, H.3    Tempst, P.4    Ghosh, S.5


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