Download Full Text (3.3 MB)

Presentation date

Summer 8-10-2022

College, Institute, or Department

Eppley Institute for Research in Cancer

Faculty Mentor

Hamid Band

Research Mentor

Bhopal Mohapatra


ECD, Ecdysoneless protein, is evolutionarily conserved. It was identified as a human homologue of Drosophila ecdysoneless, interacting with HPV16 E6 in a yeast two-hybrid assay. ECD has been proven to be essential for cell cycle progression from G1 to S phase, mitigating endoplasmic reticulum (ER) stress, and embryogenesis. ECD KO mice are embryonic lethal as it halts the cell cycle at G1. ECD interacts with p53 and Rb. ECD also associates with pre-mRNA splicing factor PRPF8. ECD is over-expressed in breast, pancreatic, gastric, and Human Papilloma-driven cancers and is correlated with shorter patient survival. ECD interacts with co-chaperone complex R2TP involved in protein assembly and folding. ECD over-expression has been proven to increase oncogenesis regulated by c-MYC in a recent mice model. Biochemical analyses showed ECD to have a role in mRNA splicing and nucleus to cytoplasm export. The purpose was to determine if there is an interaction between ECD and EIF4A1 and determine ECD’s effect on global translation using HEK293T (human embryonic kidney) and SUM159 (breast cancer) cell lines. Overall, the interaction between ECD and EIF4A1 supports a novel mechanism by which ECD protein regulates eukaryotic mRNA translation. This mechanism may contribute to the resistance of cancer cells over-expressing ECD to the translation-inhibitory effect of endoplasmic reticulum stress prevalent in tumors.


ECD, Ecdysoneless protein, EIF4A1, eukaryotic translational regulation

Novel Interaction Between ECD and EIF4A1 Indicates ECD Regulates Eukaryotic Translation