Giron P, Eggermont C, Noeparast A, et al. - Since sensitivity to epidermal growth factor receptor (EGFR) tyrosine kinase inhibitors in non‐small cell lung cancer (NSCLC) is induced by activating mutations in the EGFR, researchers investigated proteins that abrogate the response of EGFR mutant NSCLC to EGFR targeted therapy. For this purpose, they conducted an unbiased high‐throughput siRNA screen. The deubiquitinase USP13 was a top hit resulting from this screen. As a result of targeting USP13, there was an increase in the sensitivity to EGFR inhibition with small molecules in vitro and in vivo. USP13, by counteracting the action of members of the Cbl family of E3 ubiquitin ligases, resulted in selective stabilization of mutant EGFR in a peptidase‐independent manner. Based on these data, USP13 was concluded to be a strong mutant EGFR‐specific co‐target that could enhance the therapeutic efficacy of EGFR targeted therapies.