CCAAT-enhancer-binding proteins

This domain is involved in dimerization and DNA binding, as are other transcription factors of the leucine zipper domain-containing family (c-Fos and c-jun).

Members of the C/EBP family can form homodimers or heterodimers with other C/EBPs and with other transcription factors, which may or may not contain the leucine zipper domain.

Their expression is regulated at multiple levels, including through hormones, mitogens, cytokines, nutrients, and other factors.

This protein is expressed in the mammalian nervous system and plays a significant role in the development and function of nerve cells.

C/EBPβ function is regulated by multiple mechanisms, including phosphorylation, acetylation, activation, autoregulation, and repression via other transcription factors, oncogenic elements, or chemokines.

It was shown in C. elegans that multiple cis elements of cebp-1 mRNA 3'UTR interact with mak-2 to upregulate expression of CEBP-1 in neuronal development.

For example, Murine Embryonic Fibroblasts (MEFs) from mice lacking both C/EBPβ and C/EBPδ show impaired adipocyte differentiation in response to adipogenic stimuli.

[6][7] C/EBPβ and δ promote adipogenesis, at least in part by inducing the expression of the "master" adipogenic transcription factors C/EBPα and PPARγ.

However, CCAAT/enhancer-binding protein over-expression correlates with poor prognosis in glioblastoma and promotes genomic instability in cervical cancer, hinting at an oncogenic role.

[13] Cell culture studies in mice and human microglia lines also find increased C/EBPβ activity associated with pathogenic inflammation and cytokine responses.

[14] Genetic and molecular pathways with degenerative implications involving C/EBPβ and its homologs are conserved across multiple model organisms including Mus musculus, Drosophila melanogaster, Caenorhabditis elegans, and Danio rerio.