Nature reveals new discovery of proteasome research Scientists from Kansas State University have discovered new details of the complex process of assembling protein degradation machinery in cells in new research. Their research found that it is possible to advance the treatment of cancer and neurological diseases. The research was published in the journal Nature on May 5. The new research focuses on the proteasome (proteasome), a protein complex that exists in humans and other biological cells to help maintain cell health. Kaneros State University Assistant Professor Jeroen Roelofs said: "Proteasome is a large molecular machine responsible for protein degradation in cells. It is essential for protein quality control and rapid removal of specific proteins by cells, ensuring the health and normal function of cells. "The purpose of the new research is to better understand the mechanism by which various particles in the proteasome work synergistically to function as a proteasome-what transmission devices and components are needed? In what order are the working machines constructed? Scientists have discovered that the destruction of two important particles can affect the normal function of protein lysosomes, which is of great significance for cancer and various neurodegenerative diseases such as Parkinson's disease and Huntington's disease. Nature ’s new research is based on Roelofs ’2009 work as a postdoctoral fellow at Harvard Medical School. At the time, he discovered that chaperone played an important role in the assembly of the two particles. When these two particles are combined, they give the proteasome the ability to remove unnecessary proteins in the cell. The chaperone protein acts as two particles. "The new research of the supervisor found that in addition to acting as a molecular supervisor for the two particles, the chaperone protein also controls the time for the two particles to bind together. At the same time, the scientists also discovered more about Information on these two particles. They found that the core particle has 7 pockets, and the 6 tails of the control particles all enter these pockets. When docked together, they turn on the function of the proteasome. Roelofs said: " In the assembly process, in fact, only one tail determines the combination of core particles and control particles. Because there are six tails, and only one tail is necessary to confer specificity, and docking in the pocket is controlled by chaperone proteins, this research finding is surprising. "Roelofs believes that these research findings may reveal new targets for anti-cancer drugs. In addition, it also provides scientists with new research and manipulation of signaling pathways, which may promote cancer and neurological research. Roelofs said:" This is Very basic research. Understanding this basic mechanics can often lead to new ways of improvement, which is extremely important for human health. "
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