Different enzymatic activities recruitment by specific domains of TIF2 are involved in NF-κB transactivation
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, ev...
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2004
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| Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00257680_v64_n2_p135_Nojek http://hdl.handle.net/20.500.12110/paper_00257680_v64_n2_p135_Nojek |
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paper:paper_00257680_v64_n2_p135_Nojek2023-06-08T14:53:35Z Different enzymatic activities recruitment by specific domains of TIF2 are involved in NF-κB transactivation Nojek, Ignacio Martín Coló, Georgina Pamela Rubio, María Fernanda Franco, Diana Lorena Costas, Mónica Alejandra 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 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. Fil:Nojek, I.M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Colo, G.P. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Rubio, F.M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Franco, L.D. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Costas, M.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 2004 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00257680_v64_n2_p135_Nojek http://hdl.handle.net/20.500.12110/paper_00257680_v64_n2_p135_Nojek |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
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 |
| spellingShingle |
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 Nojek, Ignacio Martín Coló, Georgina Pamela Rubio, María Fernanda Franco, Diana Lorena Costas, Mónica Alejandra Different enzymatic activities recruitment by specific domains of TIF2 are involved in NF-κB transactivation |
| topic_facet |
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 |
| description |
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. |
| author |
Nojek, Ignacio Martín Coló, Georgina Pamela Rubio, María Fernanda Franco, Diana Lorena Costas, Mónica Alejandra |
| author_facet |
Nojek, Ignacio Martín Coló, Georgina Pamela Rubio, María Fernanda Franco, Diana Lorena Costas, Mónica Alejandra |
| author_sort |
Nojek, Ignacio Martín |
| title |
Different enzymatic activities recruitment by specific domains of TIF2 are involved in NF-κB transactivation |
| title_short |
Different enzymatic activities recruitment by specific domains of TIF2 are involved in NF-κB transactivation |
| title_full |
Different enzymatic activities recruitment by specific domains of TIF2 are involved in NF-κB transactivation |
| title_fullStr |
Different enzymatic activities recruitment by specific domains of TIF2 are involved in NF-κB transactivation |
| title_full_unstemmed |
Different enzymatic activities recruitment by specific domains of TIF2 are involved in NF-κB transactivation |
| title_sort |
different enzymatic activities recruitment by specific domains of tif2 are involved in nf-κb transactivation |
| publishDate |
2004 |
| url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00257680_v64_n2_p135_Nojek http://hdl.handle.net/20.500.12110/paper_00257680_v64_n2_p135_Nojek |
| work_keys_str_mv |
AT nojekignaciomartin differentenzymaticactivitiesrecruitmentbyspecificdomainsoftif2areinvolvedinnfkbtransactivation AT cologeorginapamela differentenzymaticactivitiesrecruitmentbyspecificdomainsoftif2areinvolvedinnfkbtransactivation AT rubiomariafernanda differentenzymaticactivitiesrecruitmentbyspecificdomainsoftif2areinvolvedinnfkbtransactivation AT francodianalorena differentenzymaticactivitiesrecruitmentbyspecificdomainsoftif2areinvolvedinnfkbtransactivation AT costasmonicaalejandra differentenzymaticactivitiesrecruitmentbyspecificdomainsoftif2areinvolvedinnfkbtransactivation |
| _version_ |
1768546384835772416 |