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Human cells orchestrate up to ~20,687 proteins to maintain cell growth and survival. Upon environmental change, cells dynamically remodel their proteomic landscape by two simultaneous processes: enhancing the synthesis of proteins that respond to the altered cellular conditions and degrading a subset of the pre-existing proteome. Any defect in this nature’s fine-tuned system hampers regulated cell growth as exemplified by cancer and neurodegenerative disorders. To fully understand the underlying pathology of the dysregulated proteostasis system, Heeseon An’s lab studies the regulatory mechanisms of protein translation (ribosome) and degradation processes (the ubiquitin proteasome system and autophagy) in health and disease. Importantly, we develop chemical, biological, and proteomics tools to enable quantitative analyses of the cell biological events.
An, H.*; Ordureau, A.*; Koerner, M.; Paulo, J.A.; Harper, J.W. (2020) Systematic Quantitative Analysis of Ribosome Inventory During Nutrient Stress. Nature, 583, 303-309. * equal contribution
An, H.; Ordureau, A.; Paulo, J.A.; Shoemaker, C.J.; Denic, V.; Harper, J.W. (2019) TEX264 Is an Endoplasmic Reticulum-Resident ATG8-Interacting Protein Critical for ER Remodeling during Nutrient Stress, Molecular Cell, 74, 891-908.
An, H.; Harper, J.W. (2018) Systematic Analysis of Ribophagy in Human Cells Reveals Bystander Flux During Selective Autophagy,Nat. Cell Biol., 20, 135-143.