KAT2B, also known as PCAF (lysine acetyltransferase 2B), is a histone acetyltransferase. It plays a crucial role in gene expression regulation at the post-transcriptional level through acetylation. It is involved in multiple biological processes, such as autophagy regulation, where acetylation events controlled by KAT2B target key components of autophagy-related complexes [2]. It is also associated with cancer-related pathways, including those related to epithelial-mesenchymal transition (EMT) in breast cancer [1].

In breast cancer, loss-of-function studies suggest that inactivation of KAT2B can ameliorate the expression of EMT markers, mimicking the effects of NELF-E ablation. The NELF-E-SLUG-KAT2B epigenetic axis is crucial in breast cancer carcinogenesis, as elevated expression of NELF-E and KAT2B is linked to poorer prognosis [1]. In cholangiocarcinoma, downregulation of KAT2B is associated with disease progression and poor prognosis, while overexpression of KAT2B suppresses cancer cell proliferation and growth, acting through the NF2-YAP signaling pathway [3]. In non-small cell lung cancer, low KAT2B expression is related to unsatisfactory immune checkpoint blockade efficacy and poor prognosis, and KAT2B expression is positively correlated with immune cell infiltration levels and immune checkpoint gene expression [4].

In conclusion, KAT2B is an important regulator in multiple biological and disease-related processes. Loss-of-function studies in various cancer models have revealed its significance in cancer development and progression, as well as its association with immune-related responses in non-small cell lung cancer. Understanding KAT2B's function provides insights into disease mechanisms and potential therapeutic targets in cancer.