Back

Genetic identification of the RAS proteostatic machinery and its failure to regulate oncogenic variants

Bigenzahn, J. W.; Kartnig, F.; Vollert, M.; Sedlyarov, V.; Superti-Furga, G.

2025-12-11 cell biology
10.64898/2025.12.10.693430 bioRxiv
Show abstract

The regulation of cellular homeostasis, differentiation, and proliferation is safeguarded by proteostatic mechanisms, which are crucial for maintaining cellular function. We used endogenously affinity-tagged KRAS cells in a fluorescence-activated cell sorting (FACS)-based CRISPR knockout screen to map genome-wide genetic requirements for proteostatic KRAS regulation. Three regulatory modules emerged, specifically cullin E3 ligase activity (CUL3, NAE1, UBE2M, CAND1, and UBE2L3), LZTR1 protein function (LZTR1, NUDCD3, and ZRSR2), and RAS GTPase modulation and processing (NRAS, HRAS, FNTB, RCE1, ICMT, and GOLGA7), all critical for regulating KRAS abundance. This expands our knowledge on the machinery controlling ubiquitin-meditated RAS family member regulation. Combining endogenous affinity tagging with genetic variant introduction, we found that the oncogenic KRAS G12D mutant exhibits reduced regulation by CRL3LZTR1, potentially contributing to oncogenic transformation and proliferation. In summary, our study genetically defines the machinery regulating RAS GTPase protein abundance, providing a foundation for a deeper molecular understanding and potential therapeutic exploitation of CRL3LZTR1-RAS GTPase regulation in human disease.

Matching journals

The top 7 journals account for 50% of the predicted probability mass.

50% of probability mass above

"Similar papers" are the closest papers from that journal in the model's embedding space. They show what the match is built on, but the ranking comes mostly from a classifier over the whole training set, not from these examples alone.