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Abstract:

We have previously shown that nuclear receptor coactivator overexpression significantly enhanced NF-κB activity in a dose response manner. We studied the mechanism by which TIF2 regulates NF-κB activity. We determined that: 1) the p38 specific inhibitor reduces 50% NF-κB transcriptional activity, even in cells that overexpress distinct TIF2 deletions; 2) there is a physical interaction between TIF2 and p38 and RelA determined through in vitro translated protein bindind assays; 3) TIF2 is a p38 substrate; 4) there is a physical interaction between TIF2 and IKK in TNF-α 20 ng/ml stimulated or not HEK 293 cell protein extract, and IκB only in basal conditions, determined by binding pull down assays. This NF-κ B complex regulates its activity and targets gene expression in a determined physiologic context depending on the coactivator complex content.

Registro:

Documento: Artículo
Título:Different enzymatic activities recruitment by specific domains of TIF2 are involved in NF-κB transactivation
Autor:Nojek, I.M.; Werbajh, S.E.; Colo, G.P.; Rubio, F.M.; Franco, L.D.; Nahmod, V.E.; Costas, M.A.
Filiación:Inst. de Invest. Med. Alfredo Lanari, Universidad de Buenos Aires, Combatientes de Malvinas 3150, 1427 Buenos Aires, Argentina
Fundación Instituto Leloir, Universidad de Buenos Aires, Buenos Aires, Argentina
Fac. de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Buenos Aires, Argentina
Palabras clave:MAPK; NF-κB; Nuclear receptor coactivators; TIF2; cell protein; I kappa B; immunoglobulin enhancer binding protein; mitogen activated protein kinase; nuclear receptor coactivator 2; synaptophysin; transcription factor RelA; tumor necrosis factor alpha; immunoglobulin enhancer binding protein; mitogen activated protein kinase p38; NCOA2 protein, human; nuclear receptor coactivator 2; transcription factor; article; dose response; enzyme activity; gene overexpression; human; human cell; protein binding; protein determination; protein expression; protein interaction; transactivation; transcription regulation; cell nucleus; cytoplasm; drug antagonism; enzyme activation; metabolism; phosphorylation; physiology; Cell Nucleus; Cytoplasm; Enzyme Activation; Humans; NF-kappa B; Nuclear Receptor Coactivator 2; p38 Mitogen-Activated Protein Kinases; Phosphorylation; Trans-Activation (Genetics); Transcription Factors
Año:2004
Volumen:64
Número:2
Página de inicio:135
Página de fin:138
Título revista:Medicina
Título revista abreviado:Medicina (Argentina)
ISSN:00257680
CODEN:MEDCA
CAS:mitogen activated protein kinase, 142243-02-5; NCOA2 protein, human; NF-kappa B; Nuclear Receptor Coactivator 2; p38 Mitogen-Activated Protein Kinases, EC 2.7.1.37; Transcription Factors
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00257680_v64_n2_p135_Nojek

Referencias:

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  • Finco, T.S., Baldwin, A.S., Mechanistic aspects of NF-kappa B regulation: The emerging role of phosphorylation and proteolysis (1995) Immunity, 3, pp. 263-272
  • Kopp, E.B., Ghosh, S., NF-kappa B and Rel proteins in innate immunity (1995) Adv. Immunol., 58, pp. 1-27
  • Carter, A.B., Knudtson, K.L., Monick, M.M., Hunninghake, G.W., The p38 mitogen-activated protein kinase is required for NF-kappaB-dependent gene expression. The role of TATA-binding protein (TBP) (1999) J. Biol. Chem., 274, pp. 30858-30863
  • Rosenfeld, M.G., Glass, C.K., Coregulator codes of transcriptional regulation by nuclear receptors (2001) J. Biol. Chem., 276, pp. 36865-36868
  • Xu, J., O'Malley, B.W., Molecular mechanisms and cellular biology of the steroid receptor coactivator (SRC) family in steroid receptor function (2002) Rev. Endocr. Metab. Disord., 3, pp. 185-192
  • Lee, S.K., Kim, H.J., Na, S.Y., Kim, T.S., Choi, H.S., Im, S.Y., Lee, J.W., Steroid receptor coactivator-1 coactivates activating protein-1-mediated transactivations through interaction with the c-Jun and c-Fos subunits (1998) J. Biol. Chem., 273, pp. 16651-16654
  • Na, S.Y., Lee, S.K., Han, S.J., Choi, H.S., Im, S.Y., Lee, J.W., Steroid receptor coactivator-1 interacts with the p50 subunit and coactivates nuclear factor kappaB-mediated transactiva-tions (1998) J. Biol. Chem., 273, pp. 10831-10834
  • Torchia, J., Rose, D.W., Inostroza, J., Kamei, Y., Westin, S., Glass, C.K., Rosenfeld, M.G., The transcriptional co-activator p/CIP binds CBP and mediates nuclear-receptor function (1997) Nature, 387, pp. 677-684
  • Werbajh, S., Nojek, I., Lanz, R., Costas, M.A., RAC-3 is a NF-kappa B coactivator (2000) FEBS Lett., 485, pp. 195-199
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Citas:

---------- APA ----------
Nojek, I.M., Werbajh, S.E., Colo, G.P., Rubio, F.M., Franco, L.D., Nahmod, V.E. & Costas, M.A. (2004) . Different enzymatic activities recruitment by specific domains of TIF2 are involved in NF-κB transactivation . Medicina, 64(2), 135-138.
Recuperado de https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00257680_v64_n2_p135_Nojek [ ]
---------- CHICAGO ----------
Nojek, I.M., Werbajh, S.E., Colo, G.P., Rubio, F.M., Franco, L.D., Nahmod, V.E., et al. "Different enzymatic activities recruitment by specific domains of TIF2 are involved in NF-κB transactivation " . Medicina 64, no. 2 (2004) : 135-138.
Recuperado de https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00257680_v64_n2_p135_Nojek [ ]
---------- MLA ----------
Nojek, I.M., Werbajh, S.E., Colo, G.P., Rubio, F.M., Franco, L.D., Nahmod, V.E., et al. "Different enzymatic activities recruitment by specific domains of TIF2 are involved in NF-κB transactivation " . Medicina, vol. 64, no. 2, 2004, pp. 135-138.
Recuperado de https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00257680_v64_n2_p135_Nojek [ ]
---------- VANCOUVER ----------
Nojek, I.M., Werbajh, S.E., Colo, G.P., Rubio, F.M., Franco, L.D., Nahmod, V.E., et al. Different enzymatic activities recruitment by specific domains of TIF2 are involved in NF-κB transactivation . Medicina (Argentina). 2004;64(2):135-138.
Available from: https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00257680_v64_n2_p135_Nojek [ ]