The SFR1 protein was initially discovered in the context of DNA homologous recombination repair, and its name originates from "Swi6-interacting recombination repair protein 1." However, subsequent research has revealed its central role in the field of cell death, particularly in the process of **necroptosis**. In the classical necroptosis signaling pathway, when cells receive death signals such as tumor necrosis factor, SFR1 is recruited and phosphorylated by the upstream kinase RIPK3 as a key adaptor protein. Phosphorylated SFR1 specifically binds to and stabilizes MLKL, the core executioner protein of necroptosis, significantly promoting the phosphorylation and subsequent activation of MLKL by RIPK3. This process ultimately leads to plasma membrane rupture and inflammatory cell death. Therefore, SFR1 is considered a critical molecule that precisely regulates the amplification and execution of necroptosis signaling. The study of its function is of great importance for understanding pathological processes such as infections, inflammatory diseases, and tissue damage.