In and out of the ER: protein folding, quality control, degradation, and related human diseases

DN Hebert, M Molinari - Physiological reviews, 2007 - journals.physiology.org
Physiological reviews, 2007journals.physiology.org
A substantial fraction of eukaryotic gene products are synthesized by ribosomes attached at
the cytosolic face of the endoplasmic reticulum (ER) membrane. These polypeptides enter
cotranslationally in the ER lumen, which contains resident molecular chaperones and
folding factors that assist their maturation. Native proteins are released from the ER lumen
and are transported through the secretory pathway to their final intra-or extracellular
destination. Folding-defective polypeptides are exported across the ER membrane into the …
A substantial fraction of eukaryotic gene products are synthesized by ribosomes attached at the cytosolic face of the endoplasmic reticulum (ER) membrane. These polypeptides enter cotranslationally in the ER lumen, which contains resident molecular chaperones and folding factors that assist their maturation. Native proteins are released from the ER lumen and are transported through the secretory pathway to their final intra- or extracellular destination. Folding-defective polypeptides are exported across the ER membrane into the cytosol and destroyed. Cellular and organismal homeostasis relies on a balanced activity of the ER folding, quality control, and degradation machineries as shown by the dozens of human diseases related to defective maturation or disposal of individual polypeptides generated in the ER.
American Physiological Society