RAC-3 is a NF-κB coactivator

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It has been shown that the molecular mechanism by which cytokines and glucocorticoids mutually antagonize their functions involves a mutual glucocorticoid receptor (GR)/nuclear factor-κB (NF-κB) transrepression. Here we report a role for the nuclear receptor coactivator RAC3, in modulating NF-κB tra...

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Detalles Bibliográficos
Autores principales: Werbajh, S., Nojek, I., Lanz, R., Costas, M.A.
Formato: JOUR
Materias:
Glucocorticoid receptor
Nuclear factor-κB
Nuclear receptor coactivator
Tumor necrosis factor
glucocorticoid receptor
immunoglobulin enhancer binding protein
transcription factor
transcription factor rac 3
tumor necrosis factor
unclassified drug
article
competitive inhibition
genetic transfection
human
human cell
modulation
molecular biology
priority journal
protein analysis
protein binding
protein expression
transactivation
transcription regulation
Binding, Competitive
Glucocorticoids
Hela Cells
Humans
Immunosorbent Techniques
NF-kappa B
Receptors, Glucocorticoid
Response Elements
Trans-Activators
Transcription Factor RelA
Transcription Factors
Transcription, Genetic
Transfection
Tumor Necrosis Factor-alpha
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_00145793_v485_n2-3_p195_Werbajh
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires
Descripción
Sumario:It has been shown that the molecular mechanism by which cytokines and glucocorticoids mutually antagonize their functions involves a mutual glucocorticoid receptor (GR)/nuclear factor-κB (NF-κB) transrepression. Here we report a role for the nuclear receptor coactivator RAC3, in modulating NF-κB transactivation. We found that RAC3 functions as a coactivator by binding to the active form of NF-κB and that overexpression of RAC3 restores GR-dependent transcription neglecting GR/NF-κB transrepression. The competition between GR and NF-κB for binding to RAC3 may represent a general mechanism by which both transcription factors mutually antagonize their activity. (C) 2000 Federation of European Biochemical Societies.

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