Enzyme Modification Stalls Resistant Tumor Growth

St. Jude researchers link a METTL13-driven protein change to KRAS-inhibitor-resistant tumors, a finding that remains in pre-clinical research.

Updated on Nov. 3, 2026 in Life Sciences

Bold flat-color editorial illustration of a glass culture dish with amber droplets beside a microscope objective, evoking laboratory cancer research.
St. Jude Children's Research Hospital scientists found that the METTL13 enzyme modifies the protein eEF1A, a change linked to tumors resistant to KRAS inhibitors in pre-clinical research published November 3, 2026. AI Illustration. Upload story photo >

St. Jude Children's Research Hospital scientists identified how the translation factor eEF1A is altered by the METTL13 enzyme, which methylates eEF1A at lysine 55 to form eEF1AK55me2. The findings, published November 3, 2026, in Nature Cell Biology, are research-stage and have not been tested as a treatment.

Why it matters

The work links a specific protein modification to the efficient translation of codons enriched in oncogenes such as KRAS, a driver present in many tumor types. Researchers observed that disrupting METTL13 stymied growth of KRAS-inhibitor-resistant tumors in animal models.

The study used animal models and single-molecule imaging of recombinantly expressed eEF1A, with and without METTL13-mediated methylation, to measure decoding kinetics. Two related codons were shown to decode at very similar rates when METTL13 was present and K55 was methylated, but no human clinical measurement has been reported.

The players

St. Jude Children's Research Hospital

A Memphis, Tennessee pediatric cancer research center whose labs study translation biology, ribosome structure and oncogenic drivers such as KRAS.

The details

eEF1A is a translation elongation factor that helps ribosomes read messenger RNA, the instruction strand that cells use to build proteins, by influencing how fast and accurately each three-nucleotide codon is decoded. METTL13 attaches two methyl groups to lysine 55 on eEF1A, creating a modified form the team called eEF1AK55me2, which speeds efficient translation of a subset of codons common in oncogenes. The researchers built cell lines lacking METTL13 and used parallelized single-molecule imaging to show the modification changes decoding kinetics and protein structure.

Timeline

  1. St. Jude's team published a cryo-EM ribosome structure study in Nature in 2023.

  2. The METTL13 findings were published November 3, 2026, in Nature Cell Biology.

The Tech Race

The finding positions translation regulation as a research target alongside KRAS inhibitor development, where resistance has limited current therapies. It builds on St. Jude's 2023 ribosome structure work and remains at the pre-clinical stage.

No treatment based on METTL13 is available, and no timeline for human testing has been announced. For patients with KRAS-driven tumors, the finding is a research direction, not a usable therapy.

The takeaway

Watch for whether follow-up work tests METTL13 inhibition in tumor models beyond the current study and whether the patient-data link to poor prognosis is tested in additional cohorts. Any published follow-up in Nature Cell Biology would be the next checkpoint.

Further reading

Explore more Life Sciences coverage for context on how translation biology connects to cancer research.