Office Address
420 Washington Avenue SE
Minneapolis, MN 55455
United States
Yue Chen
Associate Professor
Biochemistry, Molecular Biology, and Biophysics
Our long-term goal is to discover and characterize novel posttranslational modification (PTM) pathways that are involved in protein homeostasis, cellular signaling and epigenetic regulation. To achieve this goal, we develop and apply mass spectrometry-based quantitative and chemical proteomics technology as well as bioinformatic analysis tools for system-wide characterization of protein modification networks. Our study employs both cellular and animal-based models that involve diverse biological applications including cancer, metabolic diseases, nutrition and aging.
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Mission statement
Posttranslational modifications (PTMs) serve as direct chemical links between changes in metabolic environment, such as nutrients, oxygen, and cellular response signaling. A dysregulated PTM pathway is one of the major causes in the pathological development of cancer, aging, and metabolic diseases. Our research aims to discover and characterize novel PTM pathways as regulatory mechanisms in organismal development and diseases with cutting-edge technologies. These studies benefit society by mapping the foundational framework of molecular interactions in PTM pathways for the future development of new therapeutic approaches with improved clinical outcomes. With these efforts, I will also provide systematic scientific trainings with state-of-the-art facilities for future scientists, teachers, and healthcare professionals.
Research statement
Covalent posttranslational modifications (PTMs) of proteins represent one of the fundamental regulatory mechanisms in the cell with enzyme families encoded by more than 5% of the genome in higher eukaryotes. Extensive studies in the past twenty years established the functional roles of some well-known PTMs, including protein phosphorylation, glycosylation, ubiquitination, lysine acetylation and methylation in signal transduction, cell cycle, protein-protein interactions and epigenetic memories.
We have developed highly efficient mass-spectrometry based technology for system-wide identification and quantification of PTM sites and established the bioinformatics platform for understanding the functional relevance of the PTMs in protein structure and cellular physiology.
Our future research aims to develop and apply powerful proteomic technologies in combination with biochemistry, cell biology and computational analysis to understand the dynamic profiles of the PTM networks in various diseases, and reveal the correlation between cellular metabolism and diverse PTM pathways.