Shanye Yin

Abstract Ribosomal protein mutations are increasingly associated with cancer risk and thought to perturb ribosome function. At the same time, they reportedly activate p53, a critical anti-cancer barrier. To determine how these mutations overcome this protective block to enable tumorigenesis, we generate an in vivo model of the hotspot ribosomal protein RPS15-S138F mutation identified as a putative driver of chronic lymphocytic leukemia.

Abstract Targeted protein degradation is a promising therapeutic strategy to tackle disease-causing proteins that lack binding pockets for traditional small-molecule inhibitors. Its first step is to trigger the proximity between a ubiquitin ligase complex and a target protein through a heterobifunctional molecule, such as proteolysis targeting chimeras (PROTACs), leading to the formation of a ternary complex.

1 Introduction Cancer is still a major burden of disease worldwide despite the development of new therapeutic strategies. An estimated 19.3 million new cases and almost 10 million deaths have reportedly occurred due to cancer in 2020 (1). Further efforts are needed to prolong the survival time of patients with cancer, especially at the advanced stages.