Molecular structure of polysaccharide mediated autophagy markers KIF23 and PRC1 proteins and their regulatory role in triple negative cancer through the p53 signaling pathway

As a process of intracellular degradation and recycling of its own components, abnormal regulation of autophagy has been strongly associated with the development of multiple cancer types, including triple-negative breast cancer. The amino acid sequences of KIF23 and PRC1 proteins were analyzed by bioinformatics method, their three-dimensional structures were predicted, and their interactions with polysaccharides were studied by molecular docking technology. The localization and expression patterns of KIF23 and PRC1 in cells were studied by cell biology techniques. By constructing breast cancer cell lines that stably overexpress or knock down KIF23 and PRC1, we evaluated the effect of these proteins on autophagy activity. Finally, molecular biological methods such as Western blot and real-time quantitative PCR were used to detect the expression changes of proteins related to p53 signaling pathway and the levels of autophagy markers such as LC3 and p62, thereby revealing the regulatory effects of KIF23 and PRC1 on autophagy of triple-negative breast cancer cells through p53 signaling pathway. The study found that the KIF23 and PRC1 proteins have complex three-dimensional structures, and their interactions with polysaccharides may affect their function during cell division and autophagy. In triple-negative breast cancer cells, overexpression of KIF23 and PRC1 significantly enhanced autophagy activity, while knockdown of these proteins inhibited autophagy. Further experiments showed that KIF23 and PRC1 regulate the expression of autophagy related proteins by influencing the activity of p53 signaling pathway. Overexpression of KIF23 and PRC1 led to inhibition of the p53 signaling pathway, while knocking down these proteins activated the p53 signaling pathway, which was consistent with reduced autophagy activity.