C/EBPα, C/EBPα oncoproteins, or C/EBPβ preferentially bind NF-κB p50 compared with p65, focusing therapeutic targeting on the C/EBP:p50 interaction.

ABSTRACT: Canonical nuclear factor kappaB (NF-κB) activation signals stimulate nuclear translocation of p50:p65, replacing inhibitory p50:p50 with activating complexes on chromatin. C/EBP interaction with p50 homodimers provides an alternative pathway for NF-κB target gene activation, and interaction with p50:p65 may enhance gene activation. We previously found that C/EBPα cooperates with p50, but not p65, to induce Bcl-2 transcription and that C/EBPα induces Nfkb1/p50, but not RelA/p65, transcription. Using p50 and p65 variants containing the FLAG epitope at their N- or C-termini, we now show that C/EBPα, C/EBPα myeloid oncoproteins, or the LAP1, LAP2, or LIP isoforms of C/EBPβ have markedly higher affinity for p50 than for p65. Deletion of the p65 transactivation domain did not increase p65 affini

SUBMITTER: Dooher JE 

PROVIDER: S-EPMC3196798 | biostudies-literature | 2011 Oct

REPOSITORIES: biostudies-literature