Research overview

　About one-third of all proteins are synthesized in the endoplasmic reticulum (ER). Newly synthesized membrane and secretory proteins are co-translationally translocated into the ER and undergo posttranslational modification there such as attachment of N-glycan and disulfide bond formation. They attain their correct conformation with the assistance of ER chaperones, and then go to the next compartment, the Golgi apparatus. Proteins that cannot fold properly are transported back into the cytosol through the retrotranslocation complex with simultaneous ubiquitination, extracted by AAA-ATPase and degraded by the proteasome in the cytosol. This sequential process is referred to as ER-associated degradation. Using cultured human cells, we are trying to elucidate the molecular mechanisms of these phenomena, which are essential for the maintenance of ER homeostasis.

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