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John Christianson


My lab’s principal focus is on ER-associated degradation (ERAD), a multifaceted process responsible for clearing non-functional and orphan translation products from the early secretory pathway. Ensuring the highest level of fidelity for the transiting protein load is essential, as unabated accumulation or exposure to the extracellular environment of misfolded proteins can negatively impact cellular homeostasis and viability. More than 40 unique proteins have been implicated in ERAD, many as part of transiently forming macromolecular complexes. Yet despite their implied role in ERAD, many of these factors remain poorly characterized. ERAD plays a central role in inherited disorders such as cystic fibrosis and α1-antitrypsin disease. Many studies have linked ERAD genes to various forms of cancer and recent evidence also suggests a novel role for ERAD in regulating tumor suppressor protein levels.

Our interests lie in characterizing essential components of the ERAD mechanism and identifying novel substrates of this pathway. We employ proteomic, cell biological, functional genomic and biochemical techniques to identify factors, characterize the complexes they function in, and understand the substrate-specificity with which they operate. We are keenly interested in understanding the role that quality control at the level of the ER plays in the expression of proteins responsible for tumor progression and metastasis. Our long term goals are to explore quality control mechanisms as a novel point of intervention for cancer therapies.

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