On February 20th, the internationally renowned academic journal Nature Cell Biology published the results of a collaborative study of Professor Wu Mian from the School of Life Sciences, University of Science and Technology of China and Professor Yang Xiaolu from the University of Pennsylvania School of Medicine: p53 regulates biosynthesis through direct inactivation of glucose-6-phosphate dehydrogenase. The magazine published a long-term review titled p53 guards the metabolic pathway less travelled in the form of News and Views.
The tumor suppressor p53 plays an important role in regulating the pentose phosphate pathway (PPP). p53 is one of the most important tumor suppressors in cells to date. It plays a key role in important cell processes such as cell cycle regulation, DNA repair, and apoptosis. In recent years, scientists have discovered that p53 also plays an important role in cell metabolism, especially in sugar metabolism.
The latest work of the Wu Myanmar research group and Yang Xiaolu's laboratory proves that p53 can react with the key enzyme of the first step in the pentose phosphate pathway, glucose-6-phosphate dehydrogenase (G6PD). Combine and inhibit its activity. Under normal circumstances, p53 is involved in preventing this pathway, and the glucose in the cell is mainly used for glycolysis and tricarboxylic acid cycle; in tumor cells with p53 mutation or deletion, it is lost due to p53 mutation The ability to bind to G6PD and inhibit G6PD, another metabolic pathway for glucose utilization in cells, the pentose phosphate pathway, is therefore accelerated and consumes a lot of glucose, which partially explains the Warburg phenomenon proposed by scientists since the late 1920s . In addition, due to the acceleration of PPP, a large amount of NADDH and pentose (component materials of DNA) are produced, which can meet the large amount of DNA replication required for the rapid growth of tumor cells. In addition, the study also proposed for the first time that p53 not only has transcriptional activity, but also has a catalytic function. It can reduce the activity of G6PD enzyme in a "hit-and-run" mode by transiently binding to substrate.
The first authors of the paper are Jiang Peng and Du Wenjing, PhD students in the research group of Professor Wu Mian. Currently, they are engaged in postdoctoral research at the University of Pennsylvania School of Medicine. The research was supported by the National Natural Science Foundation of China, the Chinese Academy of Sciences and the Ministry of Science and Technology.
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