[6] The protein functions as a dominant-negative inhibitor by forming heterodimers with other C/EBP members, preventing their DNA binding activity.

[8] Due to a variety of upstream and downstream regulatory interactions, CHOP plays an important role in ER stress-induced apoptosis caused by a variety of stimuli such as pathogenic microbial or viral infections, amino acid starvation, mitochondrial stress, neurological diseases, and neoplastic diseases.

[9] However, under overwhelming ER stress conditions, the expression of CHOP rises sharply along with the activation of apoptotic pathways in a wide variety of cells.

CHOP also interacts with the phosphorylated transcription factor JUN to form a complex that binds to the promoter region of DR4 in lung cancer cells.

The highly oxidized state of the ER results in H2O2 leakage into the cytoplasm, inducing the production of reactive oxygen species (ROS) and a series of apoptotic and inflammatory reactions.

Identified CHOP-p21 relationship may play a role in changing the cell state from adapting to ER stress towards pre-apoptotic activity.

[53] In general, the downstream targets of CHOP regulate the activation of apoptotic pathways, however, the molecular interaction mechanisms behind those processes remain to be discovered.

DNA damage-inducible transcript 3 has been shown to interact with [proteins]: Chop gene deletion has been demonstrated protective against diet induced metabolic syndromes in mice.

[62] Furthermore, Chop depletion by a GLP1-ASO delivery system[63] was shown to have therapeutic effects of insulin reduction and fatty liver correction,[64] in preclinical mouse models.

For example, small molecule inhibitors of CHOP expression may act as therapeutic options to prevent ER stress and microbial infections.

[65] The regulation of CHOP expression plays an important role in metabolic diseases and in some cancers through its function in mediating apoptosis.