Gspt1, also known as G1 to S phase transition 1, is a key translation termination factor [2,3]. It interacts with eRF1 to facilitate the translation termination process, which is crucial for normal protein synthesis and thus for various biological processes [3].

In leukemia research, drugs that degrade Gspt1 via the CRL4CRBN ubiquitin ligase have shown potential as a new class of cancer therapy [1]. Gspt1 degradation leads to impaired translation termination, activation of the integrated stress response pathway, and TP53-independent cell death in leukemia cells [1]. A Nuclease technology screen suggested that cells with higher translation levels are more susceptible to Gspt1 degradation [1].

In addition, in glioblastoma, administration of CC-885, which degrades Gspt1, prolonged the survival period of nude mice with transplanted U87 glioblastoma cells. Gspt1-knockout U87 cells showed enhanced apoptosis, indicating Gspt1 is essential for glioblastoma growth [4].

In conclusion, Gspt1 is vital for translation termination in normal biological processes. Studies using gene-knockout models in leukemia and glioblastoma have revealed its significance in cancer cell survival and growth, suggesting that targeting Gspt1 could be a promising therapeutic strategy for these diseases.