On September 16, the prestigious international journal *Cell Research* published a groundbreaking study led by Hu Ronggui’s research group from the Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences. The paper introduces a novel technique called ProTA (Protein Turnover Assay), which enables the detection of protein stability at the proteome level using a dual-fluorescence approach. This method sheds light on the mechanisms of action and resistance development of Bortezomib (BTZ), a widely used chemotherapy drug targeting the proteasome.
Maintaining stable yet dynamic protein levels is essential for cellular function and survival. Protein homeostasis involves multiple processes, including translation, folding, post-translational modifications, and degradation. Among these, protein degradation plays a crucial role in regulating the abundance and functionality of proteins. It influences key cellular processes such as signal transduction, cell survival, and proliferation, and also affects how cells respond to drugs and external stressors. Disruptions in this process are linked to various diseases, including cancer and neurodegenerative disorders. Therefore, understanding protein degradation is vital for both basic biological research and the development of new therapeutic strategies.
However, current tools for studying protein degradation at an omics scale remain limited, with mass spectrometry being one of the few available methods. To address this gap, Yu Tao and colleagues developed ProTA, integrating flow cytometry (FACS) and DNA chip technology. This innovative approach allows for the relative quantification of protein stability across thousands of proteins in living cells. Unlike traditional mass spectrometry, ProTA can detect low-abundance but functionally important proteins, overcoming previous limitations.
As a proof of concept, the team applied ProTA to investigate BTZ’s effects and the emergence of resistance in tumor cells. Their findings revealed that BTZ treatment alters intracellular fatty acid metabolism and activates the interleukin-6 signaling pathway, potentially contributing to drug resistance. These insights suggest that designing combination therapies targeting these pathways could help overcome resistance. Additionally, the researchers uncovered a previously unknown mechanism of organelle homeostasis regulation, further highlighting the versatility of ProTA.
This technology holds great promise for future studies, especially when combined with other omics approaches. It can be used to systematically analyze changes in protein stability under various conditions, such as drug treatment, infection, or developmental transitions. Ongoing work aims to expand the application of ProTA in diverse biological contexts.
The study was conducted under the guidance of Hu Ronggui and involved collaboration with several leading laboratories, including the Kang Kangcheng Laboratory, Wang Hongyan Laboratory, Zhangye Laboratory, and Houjian Laboratory. Valuable contributions came from experts such as Chen Zi, Dr. Zhang Tao, Yan Xueqi, Wu Jiarui, Li Dangsheng, Wang Wei, Ivan Dikic, and Shirley Diamond. The research was supported by the Chinese Academy of Sciences, the Ministry of Science and Technology, and the National Natural Science Foundation.
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