Anti-eRF1 antibody

Supplementary info

Activity summary

The eukaryotic release factor 1 (eRF1) also known as ETF1 plays a critical role in translation termination during protein synthesis. eRF1 recognizes stop codons on mRNA and helps facilitate the release of the newly synthesized polypeptide chain from the ribosome. This protein has a molecular weight of approximately 48 kDa. Researchers have detected eRF1 in various tissues across eukaryotic organisms highlighting its extensive expression and importance in maintaining cellular function.

Biological function summary

ERF1 functions as a component of the eRF1/eRF3 complex which is essential for the accurate termination of translation. This interaction with eRF3 enhances GTPase activity driving the release process. By binding to stop codons UAA UAG and UGA eRF1 ensures the fidelity of protein synthesis maintaining cellular protein pools correctly. The complex machinery involving eRF1 therefore sustains cellular homeostasis by ensuring proteins are accurately built according to genetic instructions.

Pathways

ERF1 is an important player in the mRNA surveillance and translation termination pathways. The protein's cooperation with eRF3 and SMG1 enables detection and resolution of premature termination codons contributing to nonsense-mediated mRNA decay. Besides eRF1 interacts with ribosomal proteins forming a bridge in the translation machinery allowing it to perform its termination role effectively.

Associated diseases and disorders

Mutations or dysregulation of eRF1 have potential connections to cancer and neurodegenerative diseases. Abnormal eRF1 levels may lead to faulty translation termination causing the synthesis of aberrant proteins which can contribute to cancer progression. Additionally changes in eRF1 function or expression may have implications in Huntington's disease where protein synthesis disruptions play a role in disease pathogenesis. These associations highlight eRF1's relevance in both cancer biology and neurodegenerative disorders.