PCMT1, also known as protein-L-isoaspartate (D-aspartate) O-methyltransferase, is a repair enzyme. It catalyzes the conversion of isomerized aspartic acid (iso-Asp) residues into their normal structure, restoring the configuration and function of proteins. It has been associated with pathways like PI3K/AKT in multiple cancer-related processes [2,3].

Genome-wide Nuclease technology knockout screen identified PCMT1 as a critical driver of anoikis resistance in ovarian cancer, with PCMT1 enhancing cell migration, adhesion, and spheroid formation in vitro, and its overexpression leading to increased ascites formation and distant metastasis in vivo [1]. In prostate cancer, knockdown/overexpression experiments showed that PCMT1 promotes proliferation, migration, and invasion while inhibiting apoptosis through the PI3K/AKT/GSK-3β pathway [2]. In liver cancer, in vitro and in vivo experiments indicated that PCMT1 knockdown inhibits cancer cell proliferation and migration, promotes apoptosis, and reduces tumor growth rate, enhancing CD8+T cell infiltration [3]. In breast cancer, knockdown of PCMT1 in TNBC cells inhibited proliferation, migration, and invasion, and in MCF-7/PR cells, silencing PCMT1 enhanced sensitivity to paclitaxel through the PI3K/Akt/STMN1 pathway [4,5]. In bladder cancer, PCMT1 regulated cell migration and invasion through modulating epithelial-mesenchymal transition (EMT)-associated genes [6].

In conclusion, PCMT1 plays a significant role in cancer-related biological processes such as cell migration, invasion, proliferation, and apoptosis, across various cancer types including ovarian, prostate, liver, breast, and bladder cancers. Studies using gene knockout or knockdown models have been crucial in revealing its oncogenic functions, suggesting PCMT1 as a potential therapeutic target in these malignancies.