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Glucose on the sugar side chains of proteins keeps unfolded proteins in the ER. Mannoses on sugar side chains act as a timer for protein folding. Unfolded proteins in the ER are threaded through a retrotranslocon into the cytosol where they are ubiquitylated and digested. IRE1, ATF6 and PERK sense the amount of unfolded protein and generates several responses to reduce the effects and amount of unfolded protein.
Work in our lab covers a broad range of topics unified by one theme: the protein-folding problem. Through biochemistry and genetics we investigate the mechanisms of protein folding and the consequences of misfolding. Because protein-folding problems are universal, we move back and forth between simple and complex organisms (yeast, rodents, and human cells).