Eukaryotic Translation Initiation Factor 5A2 (eIF5A2) is a crucial protein involved in the process of translation initiation in eukaryotic cells. It is one of the two isoforms of eIF5A, the other being eIF5A1. Both isoforms are unique due to their post-translational modification known as hypusination, which is essential for their function .
The gene encoding eIF5A2, known as EIF5A2, was isolated and sequenced in 2001 and is located on chromosome 3q26.2 . This gene is distinct from EIF5A1, which is located on chromosome 17p13.1 . The discovery of eIF5A2 has provided significant insights into its role in cellular processes and its implications in various diseases.
eIF5A2 primarily acts as an elongation factor during the mRNA translation process . It promotes the formation of the first peptide bond during protein synthesis and is involved in the translation elongation of specific mRNAs . The hypusination of eIF5A2 is critical for its function, as it facilitates the translation of polyproline motifs, which are challenging to translate .
eIF5A2 is frequently overexpressed in various human cancers, including ovarian cancer, lung adenocarcinoma, and other malignancies . Its overexpression is associated with enhanced cell proliferation, migration, and invasion, making it a potential oncogene . Studies have shown that silencing eIF5A2 leads to significant reductions in cellular proliferation and migration, highlighting its role in cancer progression .
Due to its involvement in cancer, eIF5A2 has been studied as a potential prognostic marker and therapeutic target. Its expression levels can provide insights into the prognosis of cancer patients, and targeting eIF5A2 could offer new avenues for cancer treatment . Additionally, the role of eIF5A2 in translation elongation and its interaction with other cellular pathways make it a critical factor in understanding cancer biology .