Gliomas represent the most common primary malignant intracranial tumors in adults. Despite recent advances in treatment, the prognosis of patients with glioblastoma remains poor. Epigenetic abnormalities, the hallmarks of various types of cancer, contribute to the dysregulated expression of cancer-related genes. Post-translational modification of histones plays a pivotal role in cancer development and progression by modulating gene transcription, chromatin remodeling, and nuclear structure. Therefore, further exploration of the molecular mechanisms of epigenetic regulation in gliomas and the identification of superior therapeutic targets are required. High-mobility group nucleosomal-binding domain 2 (HMGN2) participates in the epigenetic regulation of genes through histone modification and exhibits significant differential expression between glioma and normal tissues. However, the effect of HMGN2 on gliomas and its underlying mechanisms remain unclear. This study aimed to elucidate these uncertainties by demonstrating that HMGN2 significantly promotes the proliferation of glioma cells. HMGN2 binds to histones and promotes the stability of H3K27ac acetylation in the cell division cycle 20 (CDC20) promoter region, enhancing the transcriptional activity of CDC20 and increasing the proliferation of glioma cells. Moreover, we found that CDC20 expression was negatively correlated with the survival time of patients with glioma. These results suggest that targeting epigenetic regulation, such as the HMGN2/CDC20 axis, may provide a novel direction for the treatment of gliomas.

Protein arginine methyltransferase 1 (PRMT1), a type I PRMT, is overexpressed in gastric cancer (GC) cells. To elucidate the function of PRMT1 in GC, PRMT1 expression in HGC-27 and MKN-45 cells was knocked down by short hairpin RNA (shRNA) or inhibited by PRMT1 inhibitors (AMI-1 or DCLX069), which resulted in inhibition of GC cell proliferation, migration, invasion, and tumorigenesis in vitro and in vivo. MLX-interacting protein (MLXIP) and Kinectin 1 (KTN1) were identified as PRMT1-binding proteins. PRMT1 recruited MLXIP to the promoter of β-catenin, which induced β-catenin transcription and activated the β-catenin signaling pathway, promoting GC cell migration and metastasis. Furthermore, KTN1 inhibited the K48-linked ubiquitination of PRMT1 by decreasing the interaction between TRIM48 and PRMT1. Collectively, our findings reveal a mechanism by which PRMT1 promotes cell proliferation and metastasis mediated by the β-catenin signaling pathway.

Gene therapy holds great promise for curing cancer by editing the deleterious genes of tumor cells, but the lack of vector systems for efficient delivery of genetic material into specific tumor sites in vivo has limited its full therapeutic potential in cancer gene therapy. Over the past two decades, increasing studies have shown that lentiviral vectors (LVs) modified with different glycoproteins from a donating virus, a process referred to as pseudotyping, have altered tropism and display cell-type specificity in transduction, leading to selective tumor cell killing. This feature of LVs together with their ability to enable high efficient gene delivery in dividing and non-dividing mammalian cells in vivo make them to be attractive tools in future cancer gene therapy. This review is intended to summarize the status quo of some typical pseudotypings of LVs and their applications in basic anti-cancer studies across many malignancies. The opportunities of translating pseudotyped LVs into clinic use in cancer therapy have also been discussed.