Kinesin family member 20A (KIF20A) is a member of the kinesin family. It transports chromosomes during mitosis, plays a key role in cell division. Recently, studies proved that KIF20A was highly expressed in cancer. High expression of KIF20A was correlated with poor overall survival (OS). In this review, we summarized all the cancer that highly expressed KIF20A, described the role of KIF20A in cancer. We also organized phase I and phase II clinical trials of KIF20A peptides vaccine. All results indicated that KIF20A was a promising therapeutic target for multiple cancer.

TRIM59 is a member of the tripartite motif containing (TRIM) protein family. It functions as an E3 ubiquitin ligase through its RING domain and is expressed by multiple types of cells. Physiogically, TRIM59 is involved in development, immune response, and the invasion and metastasis of tumors. In this review, we first describe the structure, expression, and subcellular location of TRIM59. Then, we summarize emerging evidence for TRIM59 in immunological diseases including infection, vascular diseases, autoimmunity, and tumor immunity. Additionally, we discuss important molecular signaling pathways that mediate TRIM59 activity. Altogether, the accumulating evidence suggests that manipulating TRIM59 levels and activity may open an avenue for innovative therapies for immune diseases and tumors. The immune system plays an important role in maintaining physiology. When immune system is in disorder, there are a series of diseases such as allergy, immune deficiency diseases and persistent infections. Immune system is composed of a large number of immune cells, which plays a major role in fighting bacteria, viruses, parasites fungi, or cancer cells. There are many molecules involved in the regulation of immune balance, including TRIM59. Like other TRIM proteins, TRIM59 is important in tumor invasion and metastasis, immune response and thus pathogenesis of various immune diseases. In this study, we summarized the structure and expression regulation of TRIM59, expounded its effect and mechanism on immunity and immune-related diseases, and discussed the possibility of TRIM59 as a therapeutic target.

The 3D structure and functions of ENPP4, a protein expressed on the surface of Bacillus Calmette–Guerin (BCG)-activated macrophages, are unknown. In this study, we analyzed the 3D structure of ENPP4 and determined its tumoricidal effects on MCA207 cells. Homology modeling showed that Arg305, Tyr341, Asn291, and Asn295 are important residues in substrate, adenosine triphosphate (ATP), binding. A molecular dynamics study was also carried out to study the stability of ENPP4 (including zinc atoms) as well as its ligand–enzyme complex. BCG increased ENPP4 expression in macrophages, and specific blocking of ENPP4 in BCG-activated macrophages (BAMs) significantly reduced their cytotoxicity against MCA207 cells. These results indicate that zinc remains inside the ENPP4 protein, a BCG activated tumoricidal macrophage protein, throughout the simulation. Important information for the design of new inhibitors was obtained.

Objective: This study presented a comprehensive characterization of the osteomyelitis immune microenvironment, identified driver genes and pathogenic cell populations underlying disease progression, and uncovered potential therapeutic targets through single-cell and bulk transcriptomic analysis. Methods: We analyzed time-series transcriptomic sequencing data from mouse osteomyelitis samples in the dataset GSE168896. Fuzzy c-means clustering was applied to reveal gene sets linked to disease progression. Immune cell infiltration analysis was conducted through the online tool ImmuCellAI-mouse. Furthermore, by leveraging single-cell sequencing data, we characterized immune cell subpopulations and pinpointed the key cell subtypes that were present in the osteomyelitis mice. Results: We identified six gene clusters exhibiting distinct temporal expression patterns and functional roles in osteomyelitis, such as leukocyte and lymphocyte activation and ossification. Single-cell sequencing analysis further showed seven distinct cellular subpopulations. Among these, macrophages demonstrated a significant increase following osteomyelitis, and the infiltration of Mif ⁺ Cd63 ⁺ , Arg1 ⁺ Sdc4 ⁺ , and Cxcl1 ⁺ Ccl4 ⁺ macrophages significantly increased. Moreover, Ccl3–Ccr1 and Cxcl2–Cxcr2 ligand–receptors contributed mostly in immune cells. Conclusion: Our findings tracked the transcriptional dynamics and evolving immune landscape of osteomyelitis, highlighting macrophages as central regulators of disease progression. We identified that significant infiltration of Arg1 ⁺ Sdc4 ⁺ , Cxcl1 ⁺ Ccl4 ⁺ , and Mif ⁺ Cd63 ⁺ macrophages may affect osteomyelitis through the Ccl3–Ccr1 and Cxcl2–Cxcr2 signaling pathways. These findings offer a new perspective on immune regulation in osteomyelitis.

Allergic asthma, known for its airway hyperresponsiveness and remodeling, is a prevalent chronic respiratory disease. Recent investigations have emphasized the crucial role of ubiquitination, a post-translational modification, in the pathogenesis of allergic asthma. Ubiquitination involves the addition of ubiquitin molecules to substrates, caused their degradation or alteration in activity. Ubiquitination affects various aspects of immune cell function, such as activation of Th2 cells, B cells, and antigen-presenting cells, which are vital to allergic asthma. In this review, we explore the role of ubiquitination in modulating immune responses during allergic asthma. We discuss the interplay between ubiquitin ligases, their substrates, and the impact on immune cell function, including Th2 differentiation and Th2 cytokines production. Our study also considers the potential therapeutic outcomes of targeting ubiquitination in asthma management. By understanding the complex interplay between ubiquitination, immune cells and immune responses, we can identify new molecules for treating allergic asthma, potentially leading to more effective therapies that modulate immune responses and ameliorate disease symptoms.