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Dalian Institute of Chemicals reveals a network of deubiquitination and ubiquitination molecular interactions
[ Instrument Network Instrument Research and Development ] Recently, the team of bio-molecular function research group, Park Hailong, of the Institute of Biotechnology Research, Dalian Institute of Chemical Physics, Chinese Academy of Sciences, based on bioinformatics methods, revealed the key deubiquitination and ubiquitination molecules in cancer. Function network.
Deubiquitination and ubiquitination are vital post-transcriptional modifications in life, involving almost all biological pathways such as cell cycle, immune regulation, and signaling. At the same time, this system of action also plays an important role in the occurrence and development of cancer. Among them, deubiquitination and ubiquitination rely on deubiquitinating enzyme and E3 ubiquitin ligase to achieve specific recognition of substrates. However, whether it is deubiquitinating enzyme or E3 ubiquitin ligase, its protein species are diverse and exhibit a "many-to-many" complex interaction relationship with the substrate. At present, there are many "deubiquitinating enzyme-substrate" interactions and "E3 ubiquitin link-substrate" interactions have not been revealed.
The team built the bio-molecular structure information, proteomic expression profiling, genomic expression profiling, molecular network and other biological big data resources to construct a deubiquitinating enzyme-substrate and E3 ubiquitin linkage. A predictive model of the enzyme-substrate interaction enables the identification of potentially unknown substrates and validates the results with molecular biology experiments. At the same time, in the study of the "deubiquitinating enzyme-substrate" interaction, further fusion of cancer multi-omics data resources reveals a "deubiquitinating enzyme-substrate with cancer-specific functions in various cancers. "interaction. The relevant research results will provide a favorable reference for the study of ubiquitination and deubiquitination systems, and promote the discovery of new cancer therapeutic targets targeting ubiquitination and deubiquitination systems.
The two projects were funded by the National Natural Science Foundation, the Postdoctoral Fund, the Dalian Institute of Chemicals Innovation Fund and the Chinese Academy of Sciences Hundred Talents Program, and were published in Oncogene and iScience magazine respectively.