On September 16th, the prestigious international academic journal *Cell Research* published a groundbreaking study led by Professor Hu Ronggui’s team from the Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences. The research introduces a novel proteomic-level technique called ProTA (Protein Turnover Assay), which enables the detection of protein stability using a dual-fluorescence approach. This method provides new insights into the mechanism of action of the chemotherapy drug Bortezomib (BTZ) and its associated drug resistance in cancer cells.
Maintaining stable yet dynamic protein levels is essential for cellular function and survival. Protein homeostasis involves processes such as translation, folding, post-translational modifications, and degradation. Among these, protein degradation plays a critical role in regulating the abundance and activity of proteins. Dysregulation of this process has been linked to various diseases, including cancer, neurodegenerative disorders, and drug resistance. Understanding how proteins are degraded not only deepens our knowledge of fundamental biological mechanisms but also opens up new possibilities for disease diagnosis and treatment. However, current tools for studying protein degradation at the omics level remain limited, with mass spectrometry being one of the few available methods.
In this study, lead author Yu Tao and colleagues developed ProTA, a powerful technique that combines flow cytometry (FACS) and DNA chip technology to quantitatively assess protein stability across the entire proteome. Unlike traditional mass spectrometry, which often fails to detect low-abundance but functionally important proteins, ProTA can monitor the stability of over 15,000 proteins simultaneously in living cells. As a proof of concept, the researchers applied ProTA to investigate BTZ, a widely used anti-cancer drug. Their findings revealed that BTZ treatment alters intracellular fatty acid metabolism and activates the interleukin-6 signaling pathway, potentially contributing to drug resistance. These results suggest that targeted therapeutic strategies based on these pathways could help overcome resistance.
Additionally, the study uncovered a previously unknown mechanism involved in the regulation of key cellular organelles. ProTA, as a new tool for studying protein degradation, holds great promise when combined with mass spectrometry and other omics technologies. It allows for a comprehensive analysis of changes in protein stability and molecular networks under various conditions, such as drug exposure, infection, or developmental transitions.
The research was conducted under the guidance of Professor Hu Ronggui and involved collaboration with several leading institutions, including the Kang Kangcheng Laboratory, the Wang Hongyan Laboratory, the Zhangye Laboratory, and the Houjian Laboratory. Valuable contributions were also made by experts from Fudan University, the Chinese Academy of Sciences, Goethe University, and Caltech. The project was supported by the Chinese Academy of Sciences, the Ministry of Science and Technology, and the National Natural Science Foundation. Ongoing applications of ProTA continue to expand, with promising results already emerging.
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