Our research focuses on protein quality control process in the endoplasmic reticulum, which is an important hub for protein production in the cells. —Shengyi Iris Sun, PhD, Associate Professor, Department of Pharmacology
ER Protein Folding and Degradation
In eukaryotes, approximately 30% of all newly synthesized proteins pass through the endoplasmic reticulum (ER), where they undergo folding and maturation. A significant fraction of nascent proteins may fail to fold properly, which if not cleared efficiently may contribute to disease pathogenesis. These misfolded proteins in the ER are disposed of by a quality-control process known as ER-associated degradation (ERAD). ERAD is the first line of defense to recruit and retrotranslocate misfolded ER proteins for cytosolic proteasomal degradation. ERAD helps maintain a favorable folding environment for wildtype ER proteins, and has been implicated in over 70 human diseases. The long-term goal of our research program is to gain a comprehensive understanding of the cellular and physiological functions of mammalian ERAD.
Watch the Research in Motion video on Dr. Sun’s research here, and read more about her research on her lab website here
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