GSPT1 is a GTPase that functions as a critical translation termination factor, forming part of the eRF1-eRF3-GTP ternary complex that mediates protein synthesis termination at stop codons UAA, UAG, and UGA 1. The protein facilitates delivery of eRF1 to stop codons, where GTP hydrolysis by GSPT1 induces conformational changes leading to proper translation termination 1. GSPT1 is significantly overexpressed in various cancer tissues and plays a key role in cancer cell progression 2. The protein has emerged as an attractive therapeutic target through the development of molecular glue degraders, particularly cereblon modulators like CC-885 and CC-90009, which recruit GSPT1 to the CRL4(CRBN) ubiquitin ligase for proteasomal degradation 13. These degraders demonstrate potent anti-tumor activity against acute myeloid leukemia (AML) cells, including leukemia stem cells 3. Clinical studies show that GSPT1 degradation rapidly induces apoptosis in AML blasts and reduces leukemia engraftment in patient-derived xenograft models 3. Several selective GSPT1 degraders, including the orally bioavailable SJ6986, have entered clinical trials, representing a promising therapeutic strategy for GSPT1-related cancers 45.