A small chemical modification to a protein involved in making other proteins changes how efficiently some genetic messages are read. Peer-reviewed experiments connect this selectivity with cancer-related protein production and drug resistance in laboratory models. The findings offer a possible research target, while effectiveness and safety of treatment in people remain unestablished.
A chemical mark on eEF1A, a protein that helps cells assemble other proteins, influences which genetic messages are efficiently decoded. A peer-reviewed study found that this modification selectively affects production of some cancer-related proteins. The mark is added by METTL13, an enzyme. Adding a methyl group is a small chemical change, but its consequences were uneven across the messages the cellular machinery reads.[1], [2]
Researchers combined measurements of proteins with observations of individual molecules and experiments in cells. Differences in the amount of messenger ribonucleic acid, the material carrying genetic instructions for protein production, did not fully track the results. The decoding step also changed. This provides a mechanism for differences in how cancer cells depend on machinery shared with other cells.[1]
Reducing the enzyme’s activity restrained growth in some lung-tumour models resistant to sotorasib, a targeted cancer drug. Those findings came from cells, mice and preclinical systems containing patient-derived tumours. An association between inferred enzyme activity and poorer treatment response also appeared in patient data. These results leave the safety and clinical benefit of blocking the enzyme in people unestablished; the patient association does not demonstrate a treatment effect.[1]
