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EGR1 — RELA
Protein-Protein interactions - manually collected from original source literature:
Studies that report less than 10 interactions are marked with *
Text-mined interactions from Literome
Chapman et al., J Biol Chem 2000
:
In this study we demonstrate that the early growth response transcription factor
Egr-1 , whose DNA binding domain shares a high degree of homology with that of Sp1, can also interact with RelA in vitro and
regulate NF-kappaB transcriptional activity in vivo ... Surprisingly, and in contrast to Sp1,
Egr-1 specifically
represses RelA transcriptional activity through its zinc finger domain
Thyss et al., EMBO J 2005
:
Furthermore, we demonstrate that
Egr-1 is
induced upon UVB irradiation through
NF-kappaB activation and the binding of p65/RelA within the Egr-1 promoter
Ma et al., J Biol Chem 2009
(Neoplasm Invasiveness...) :
Furthermore, silencing
EGR-1 suppressed a synergistically functional interaction between EGR-1 and
NF-kappaB
Cogswell et al., J Exp Med 1997
:
Characterization of the NF-kappa B1 promoter identified an
Egr-1 site which was found to be
essential for both the PMA/PHA mediated induction as well as the synergistic activation observed after the expression of the RelA subunit of
NF-kappa B and Egr-1 ... Furthermore,
Egr-1 induction was
required for endogenous
NF-kappa B1 gene expression, since PMA/PHA stimulated T cell lines expressing antisense Egr-1 RNA were inhibited in their ability to upregulate NF-kappa B1 transcription