Title
In and out of the ER: protein folding, quality control, degradation, and related human diseases
UMMS Affiliation
Graduate School of Biomedical Sciences
Publication Date
2007-10-12
Document Type
Article
Disciplines
Life Sciences | Medicine and Health Sciences
Abstract
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.
DOI of Published Version
10.1152/physrev.00050.2006
Source
Physiol Rev. 2007 Oct;87(4):1377-408. Link to article on publisher's site
Journal/Book/Conference Title
Physiological reviews
Related Resources
PubMed ID
17928587
Repository Citation
Hebert DN, Molinari M. (2007). In and out of the ER: protein folding, quality control, degradation, and related human diseases. GSBS Student Publications. https://doi.org/10.1152/physrev.00050.2006. Retrieved from https://escholarship.umassmed.edu/gsbs_sp/380