Retrograde protein translocation: ERADication of secretory proteins in health and disease

RK Plemper, DH Wolf - Trends in biochemical sciences, 1999 - cell.com
RK Plemper, DH Wolf
Trends in biochemical sciences, 1999cell.com
Eukaryotic cells have a complex degradation machinery that eliminates misfolded or
unassembled secretory proteins from the endoplasmic reticulum (ER). The proteins are
retained in an ER/pre-Golgi compartment and then hydrolysed by the cytosolic ubiquitin-
proteasome system. This requires retrograde translocation of proteins from the ER back to
the cytoplasm, which is mediated by Sec61, the central component of the ER protein-import
channel. This proteolytic pathway prevents a potentially lethal aggregation of secretory …
Abstract
Eukaryotic cells have a complex degradation machinery that eliminates misfolded or unassembled secretory proteins from the endoplasmic reticulum (ER). The proteins are retained in an ER/pre-Golgi compartment and then hydrolysed by the cytosolic ubiquitin-proteasome system. This requires retrograde translocation of proteins from the ER back to the cytoplasm, which is mediated by Sec61, the central component of the ER protein-import channel. This proteolytic pathway prevents a potentially lethal aggregation of secretory proteins; however, several viruses misuse it to escape detection, and bacterial and plant toxins might also exploit it. Underactive or overactive ER degradation machinery contributes to the pathogenesis of several severe human diseases.
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