201. Versatility of the endoplasmic reticulum protein folding factory.
- Author
-
van Anken E and Braakman I
- Subjects
- Glycoproteins metabolism, Glycosylation, Hydrophobic and Hydrophilic Interactions, Models, Biological, Molecular Chaperones biosynthesis, Molecular Chaperones chemistry, Molecular Chaperones metabolism, Protein Denaturation, Quality Control, Signal Transduction physiology, Ubiquitin metabolism, Endoplasmic Reticulum metabolism, Protein Folding
- Abstract
The endoplasmic reticulum (ER) is dedicated to import, folding and assembly of all proteins that travel along or reside in the secretory pathway of eukaryotic cells. Folding in the ER is special. For instance, newly synthesized proteins are N-glycosylated and by default form disulfide bonds in the ER, but not elsewhere in the cell. In this review, we discuss which features distinguish the ER as an efficient folding factory, how the ER monitors its output and how it disposes of folding failures.
- Published
- 2005
- Full Text
- View/download PDF