H2AT120蛋白磷酸化致癌的动力学特性.

In this paper, based on Hill kinetics and Michaelis-Menten equation, we built a theoretical model to study the kinetics of H2 AT120 protein phosphorylation promoting the oncogenic transformation. We found that in H2 AubK119-H2 AT120 D-H2 AT120 P signaling pathway, the vaccinia-related kinase 1(VRK1) regulates the kinetic behavior of H2 AT120 protein phosphorylation. Overexpression or underexpression of VRK will cause abnormalities in the phosphorylation process of H2 AT120, which leads to improper gene expression and oncogenic transformation. By investigating the dynamic stability of the H2 AubK119-H2 AT120 D-H2 AT120 P signaling pathway system, we found that the H2 AubK119, H2 AT120 D, and H2 AT120 P present Hopf bifurcation. It confirms the transition characteristics of the system’s evolutionary dynamics over time. This shows that the phosphorylation of H2 AT120 protein promotes the complexity of cancer occurrence and development. Based on the model in this article, we explained the carcinogenic regulation characteristics of VRK, H2 AT12 ubiquitination and [H2 AT120 D] mutation. The results can be used to further understand the carcinogenic mechanism induced by the H2 AubK119-H2 AT120 D-H2 AT120 P signaling circuit. The theoretical results are consistent with the experiment, revealing a carcinogenic mechanism of epigenetic changes caused by phosphorylation of H2 AT120 protein, which can provide a theoretical basis for the design to prevent cancers induced by histone mutations. [ABSTRACT FROM AUTHOR]