Polm, also known as DNA polymerase mu, is a member of the DNA polymerase family. It is involved in DNA repair processes and plays a role in maintaining genomic stability. It has been associated with pathways such as the NF-κB signaling pathway, and is of biological importance in processes like tumorigenesis and host-virus interactions [1,2].

In ovarian cancer, the POLM G312R mutation promotes tumorigenesis. It increases the ribonucleotide insertion capability of POLM, leading to genomic instability. It also upregulates COL11A1, activates the NF-κB signaling pathway, and contributes to tumor progression and chemoresistance, identifying the POLM-COL11A1-NF-κB axis as a novel oncogenic pathway [1]. In porcine epidemic diarrhea virus (PEDV) infection, POLM expression increases, regulated by the transcription factor FOXA1. POLM targets and degrades PEDV structural proteins (N, S2, and M) via the autophagy pathway, inhibiting PEDV proliferation [2].

In conclusion, Polm is crucial for maintaining genomic stability and is involved in important biological processes related to cancer development and host-virus interactions. Studies on its role in ovarian cancer and PEDV infection using genetic models help understand its functions in these disease conditions, potentially providing new therapeutic targets for treatment [1,2].