Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

RAC-3 is a NF-kappa B coactivator.

S Werbajh1, I Nojek, R Lanz

  • 1Deparmento de Cs. Biológicas, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Ciudad Universitaria, Pabellón II, Argentina.

FEBS Letters
|November 30, 2000
PubMed
Summary
This summary is machine-generated.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

RAC3 more than a nuclear receptor coactivator: a key inhibitor of senescence that is downregulated in aging.

Cell death & disease·2015
Same author

The p160 nuclear receptor co-activator RAC3 exerts an anti-apoptotic role through a cytoplasmatic action.

Oncogene·2007
Same author

Glaucoma phenotype in a large Swiss pedigree with the myocilin Gly367Arg mutation.

Eye (London, England)·2007
Same author

TNF-alpha enhances estrogen-induced cell proliferation of estrogen-dependent breast tumor cells through a complex containing nuclear factor-kappa B.

Oncogene·2005
Same author

Efficacy and safety of ketotifen eye drops in the treatment of seasonal allergic conjunctivitis.

The British journal of ophthalmology·2003
Same author

Osmotic stress sensitizes naturally resistant cells to TNF-alpha-induced apoptosis.

Cell death and differentiation·2002
Same journal

Investigating transcription factor dynamics in health and disease using FRAP.

FEBS letters·2026
Same journal

Regulation of CFTR stability at the plasma membrane-Mechanisms and therapeutic opportunities in cystic fibrosis.

FEBS letters·2026
Same journal

Identification of a Shiga toxin A-derived peptide internalized into Gb3 receptor-bearing cells via interaction with the Shiga toxin B subunit.

FEBS letters·2026
Same journal

The dual role of lectins in cancer-immunotherapy tools and therapeutic targets.

FEBS letters·2026
Same journal

Decoding the dynamic extracellular matrix in cancer-3D models and bioscaffolds rewire the rules of tumor progression.

FEBS letters·2026
Same journal

Extending the classical sequence-structure-function paradigm through protein dynamics and context-dependent behavior.

FEBS letters·2026
See all related articles

Nuclear receptor coactivator RAC3 modulates NF-kappa B activity, impacting cytokine and glucocorticoid signaling. Competition for RAC3 between glucocorticoid receptor (GR) and NF-kappa B offers a new mechanism for their functional antagonism.

Area of Science:

  • Molecular biology
  • Cellular signaling
  • Gene transcription regulation

Background:

  • Cytokines and glucocorticoids exhibit mutual antagonism in cellular functions.
  • This antagonism is partly mediated by glucocorticoid receptor (GR)/nuclear factor-kappa B (NF-kappa B) transrepression.

Purpose of the Study:

  • To investigate the role of nuclear receptor coactivator RAC3 in modulating NF-kappa B transactivation.
  • To elucidate the mechanism of RAC3 in the context of GR/NF-kappa B cross-regulation.

Main Methods:

  • Investigated RAC3's interaction with the active form of NF-kappa B.
  • Assessed the effect of RAC3 overexpression on GR-dependent transcription under conditions of GR/NF-kappa B transrepression.

Main Results:

Related Experiment Videos

  • RAC3 functions as a coactivator by directly binding to the active form of NF-kappa B.
  • Overexpression of RAC3 rescued GR-dependent transcription, overcoming the inhibitory effects of GR/NF-kappa B transrepression.

Conclusions:

  • RAC3 plays a crucial role in modulating NF-kappa B transactivation.
  • The competition between GR and NF-kappa B for binding to RAC3 represents a novel mechanism for their mutual functional antagonism.