SRP72 is a critical component of the signal recognition particle (SRP) complex, a ribonucleoprotein assembly mediating cotranslational targeting of secretory and membrane proteins to the endoplasmic reticulum 1. As one of the two largest SRP proteins, SRP72 forms a heterodimer with SRP68 through its N-terminal tetratricopeptide repeat (TPR) domain, enabling stable interaction even at elevated salt concentrations 23. The SRP72 RNA-binding domain flexibly engages the SRP RNA S domain, forming a novel K+-turn structure that remodels regulatory RNA loops and facilitates ribosome interaction during protein translocation 4. Cancer-associated mutations disrupt the SRP68-SRP72 interaction and ER localization, impairing translocation function 3. Clinically, SRP72 mutations are recognized as germline determinants of hereditary myeloid malignancies, conferring specific increased risk for myelodysplastic syndrome (MDS) and acute myeloid leukemia, particularly in pediatric populations 567. Beyond hematologic disease, SRP72 depletion increases cellular radiosensitivity by elevating apoptosis rather than impairing DNA repair, suggesting potential therapeutic applications in radiation oncology 8.