Smarcal1, an ATP-dependent DNA annealing helicase, belongs to the SNF2-family DNA translocase. It is crucial for maintaining genome stability as it functions in DNA damage repair, especially in reannealing stalled replication forks. It is involved in pathways like cGAS-STING-dependent signaling and also impacts transcriptional regulation [2,3].

In a mouse melanoma model, Smarcal1 loss enhances anti-tumor immune responses. It does so by hindering the ability of tumor cells to induce PD-L1 in response to genomic instability, thus sensitizing tumors to immune checkpoint blockade. This reveals its role in tumor immune evasion [1]. In telomerase-negative glioblastoma cells, Smarcal1 deficiency promotes alternative lengthening of telomeres and tumorigenesis, highlighting its significance in cancer-related processes [4].

In conclusion, Smarcal1 is essential for maintaining genome stability, with key roles in DNA damage repair and transcriptional regulation. Studies using gene knockout models have revealed its importance in tumor immune evasion and tumorigenesis in specific cancer types, providing potential targets for cancer immunotherapy and new insights into cancer mechanisms.