Asst. Prof. Choe, Young-Jun

Our lab investigates the mechanisms that maintain cellular proteostasis—the delicate balance of protein synthesis, folding, and degradation. Proteostasis declines with aging, leading to the accumulation of toxic protein aggregates that underlie neurodegenerative diseases. Central to our research are molecular chaperones, which assist in protein folding, prevent aggregation, and promote the degradation of damaged proteins. We are particularly interested in novel forms of protein aggregates and protein condensates, and how they interact with molecular chaperones.

Our interests also extend to ribosome-associated quality control (RQC), a critical pathway that monitors and resolves errors during translation. Translation of messenger RNAs damaged by endogenous or exogenous insults can cause ribosome stalling. By studying how cells manage stalled ribosomes and aberrant nascent polypeptides, we aim to uncover how RQC safeguards proteome integrity under stress conditions. Using a combination of molecular biology, biochemistry, and imaging approaches, we seek to provide new insights into cellular proteostasis. Through these efforts, we aim to contribute to a broader understanding of the molecular basis of age-related disorders, particularly neurodegenerative and skin diseases.

Research Areas

Proteostasis, Molecular chaperone, Ribosome-associated quality control (RQC), Protein aggregation, Phase separation