GSBS Student Publications


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

GSBS Program

Biochemistry & Molecular Pharmacology

UMMS Affiliation

Graduate School of Biomedical Sciences



Document Type


Medical Subject Headings

Endoplasmic Reticulum; Humans; Metabolic Diseases; Molecular Chaperones; Protein Biosynthesis; *Protein Folding


Life Sciences | Medicine and Health Sciences


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.

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Citation: Physiol Rev. 2007 Oct;87(4):1377-408. Link to article on publisher's site

DOI of Published Version


Related Resources

Link to Article in PubMed

Journal Title

Physiological reviews

PubMed ID