The mechanism by which protein elongation factor eEF1A2 enhances cell growth and oncogenicity

Abstract

EEF1A2 is a putative ovarian and breast oncogene that encodes protein elongation factor eEF1A2. During protein translation, eEF1A2 binds amino-acylated tRNA and recruits it to the ribosome. eEF1A2 also regulates the translocation of the growing polypeptide from the acceptor (A) site to the peptidyl (P) site of the ribosome. Human EEF1A2 is one of two isoforms of eukaryotic elongation factor 1alpha(EEF1A). EEF1A1 and EEF1A2 share more than 90% DNA and amino acid sequence homology. eEF1A proteins from several species and genera associate with the cellular actin network by binding actin filaments and depolymerizing alpha-tubulin microtubules. This suggests that eEF1A proteins may contribute to the regulation of cytoskeletal organization in addition to controlling protein translation. EEF1A2 is increased in copy number in about 25% of primary ovarian tumors and highly expressed in approximately 30% of ovarian tumors and established cell lines. (Abstract shortened by UMI.)