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ING4 — RELA

Protein-Protein interactions - manually collected from original source literature:

Studies that report less than 10 interactions are marked with *

• IRef Bind Interaction: RELA — ING4 Garkavtsev et al., Nature 2004*
• IRef Bind_translation Interaction: RELA — ING4 (coimmunoprecipitation) Garkavtsev et al., Nature 2004*
• IRef Bind_translation Interaction: RELA — ING4 (two hybrid) Garkavtsev et al., Nature 2004*
• IRef Biogrid Interaction: ING4 — RELA (physical association, affinity chromatography technology) Nozell et al., Mol Cell Biol 2008*
• IRef Biogrid Interaction: ING4 — RELA (physical association, affinity chromatography technology) Garkavtsev et al., Nature 2004*
• IRef Biogrid Interaction: ING4 — RELA (physical association, affinity chromatography technology) Hou et al., Oncogene 2014*
• IRef Biogrid Interaction: ING4 — RELA (direct interaction, two hybrid) Garkavtsev et al., Nature 2004*
• IRef Biogrid Interaction: ING4 — RELA (direct interaction, enzymatic study) Hou et al., Oncogene 2014*
• IRef Biogrid Interaction: ING4 — RELA (direct interaction, pull down) Nozell et al., Mol Cell Biol 2008*
• IRef Hprd Interaction: RELA — ING4 (in vivo) Garkavtsev et al., Nature 2004*
• IRef Hprd Interaction: RELA — ING4 (two hybrid) Garkavtsev et al., Nature 2004*
• IRef Ophid Interaction: ING4 — RELA (aggregation, interologs mapping) Brown et al., Bioinformatics 2005

Text-mined interactions from Literome

Contzler et al., Biochem Biophys Res Commun 2006 : Histone acetyltransferase HBO1 inhibits NF-kappaB activity by coactivator sequestration ... Since the androgen receptor and NF-kappaB transcription factors crossmodulate their transcriptional activity, we investigated whether HBO1 regulates NF-kappaB signaling ... Here, we report that in 293T cells HBO1 reduced dose-dependently NF-kappaB activity stimulated by TNFalpha, or by overexpressing p65/RelA, RelB, or cRel ... Electrophoretic mobility-shift assays demonstrated that HBO1 was neither perturbing the formation of p65/RelA DNA complexes nor binding itself to the kappaB consensus sequence or to p65/RelA, suggesting that HBO1 reduced NF-kappaB activity by squelching a cofactor
Nozell et al., Mol Cell Biol 2008 (Glioma) : We demonstrate that an ING4 and NF-kappaB interaction exists but does not prevent NF-kappaB activation, nuclear translocation, or DNA binding
Coles et al., Proc Natl Acad Sci U S A 2010 (Inflammation) : We have generated Ing4-deficient mice to explore the role of Ing4 in development, tumorigenesis, and in NF-kappaB signaling ... However, increased promoter occupancy by RelA in LPS stimulated, Ing4-null cells does not always correlate with increased NF-kappaB target-gene expression, as RelA activation of a subset of cytokine promoters also requires Ing4 for proper histone H4 acetylation ... Furthermore, activation of the IkappaB alpha promoter by RelA is also Ing4 dependent , and LPS stimulated, Ing4-null cells have reduced levels of IkappaB alpha promoter H4 acetylation and IkappaB gene expression ... Thus, Ing4 negatively regulates the cytokine mediated inflammatory response in mice by facilitating NF-kappaB activation of IkappaB promoters, thereby suppressing nuclear RelA levels and the activation of select NF-kappaB target cytokines
Byron et al., PloS one 2012 (Breast Neoplasms...) : Conversely, ectopic expression of ING4 inhibited p65/RelA phosphorylation in T47D and MCF7 breast cancer cells