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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Autores principales: Nojek, I.M., Werbajh, S.E., Colo, G.P., Rubio, F.M., Franco, L.D., Nahmod, V.E., Costas, M.A.
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Acceso en línea:http://hdl.handle.net/20.500.12110/paper_00257680_v64_n2_p135_Nojek
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spelling todo:paper_00257680_v64_n2_p135_Nojek2023-10-03T14:36:39Z Different enzymatic activities recruitment by specific domains of TIF2 are involved in NF-κB transactivation Nojek, I.M. Werbajh, S.E. Colo, G.P. Rubio, F.M. Franco, L.D. Nahmod, V.E. Costas, M.A. 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. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar 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, I.M.
Werbajh, S.E.
Colo, G.P.
Rubio, F.M.
Franco, L.D.
Nahmod, V.E.
Costas, M.A.
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.
format JOUR
author Nojek, I.M.
Werbajh, S.E.
Colo, G.P.
Rubio, F.M.
Franco, L.D.
Nahmod, V.E.
Costas, M.A.
author_facet Nojek, I.M.
Werbajh, S.E.
Colo, G.P.
Rubio, F.M.
Franco, L.D.
Nahmod, V.E.
Costas, M.A.
author_sort Nojek, I.M.
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
url http://hdl.handle.net/20.500.12110/paper_00257680_v64_n2_p135_Nojek
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AT rubiofm differentenzymaticactivitiesrecruitmentbyspecificdomainsoftif2areinvolvedinnfkbtransactivation
AT francold differentenzymaticactivitiesrecruitmentbyspecificdomainsoftif2areinvolvedinnfkbtransactivation
AT nahmodve differentenzymaticactivitiesrecruitmentbyspecificdomainsoftif2areinvolvedinnfkbtransactivation
AT costasma differentenzymaticactivitiesrecruitmentbyspecificdomainsoftif2areinvolvedinnfkbtransactivation
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