Eef1akmt2, also known as METTL10, is a lysine methyltransferase that specifically methylates the translation elongation factor eEF1A1 [2]. eEF1A1 is essential for protein synthesis in eukaryotes, and thus Eef1akmt2 plays a crucial role in this fundamental biological process. Understanding its function can be facilitated through genetic models like gene knockout (KO) mouse models for in-vivo functional studies.

In clear cell renal cell carcinoma, SETD2-mutated tumors with loss of SET domain function show decreased progression-free survival and loss of Eef1AKMT2 gene expression. EEF1AKMT2 and EEF1AKMT3, which methylate eEF1A1, have their expression dependent on the SET-domain function of SETD2. This indicates that SETD2-mutated ccRCC may display dysregulation of protein translation via loss of Eef1akmt2 expression [1]. In in vitro studies, a unique beta-hairpin motif in human eEF1A-KMT2 (METTL10) is important for its activity towards eEF1A1, and phosphorylation of eEF1A1 at S314 negatively crosstalks with Eef1akmt2-mediated methylation of K316 [2].

In conclusion, Eef1akmt2 is vital for the methylation of eEF1A1, an essential factor in protein synthesis. Model-based research, especially in the context of clear cell renal cell carcinoma, reveals its significance in disease-related protein translation dysregulation. Understanding Eef1akmt2 provides insights into the molecular mechanisms underlying certain diseases and may offer potential targets for therapeutic intervention.