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Protein folding includes oligomerization - examples from the endoplasmic reticulum and cytosol.
- Source :
-
The FEBS journal [FEBS J] 2008 Oct; Vol. 275 (19), pp. 4700-27. Date of Electronic Publication: 2008 Aug 01. - Publication Year :
- 2008
-
Abstract
- A correct three-dimensional structure is a prerequisite for protein functionality, and therefore for life. Thus, it is not surprising that our cells are packed with proteins that assist protein folding, the process in which the native three-dimensional structure is formed. In general, plasma membrane and secreted proteins, as well as those residing in compartments along the endocytic and exocytic pathways, fold and oligomerize in the endoplasmic reticulum. The proteins residing in the endoplasmic reticulum are specialized in the folding of this subset of proteins, which renders this compartment a protein-folding factory. This review focuses on protein folding in the endoplasmic reticulum, and discusses the challenge of oligomer formation in the endoplasmic reticulum as well as the cytosol.
- Subjects :
- Apoptosis Regulatory Proteins physiology
DNA-Directed RNA Polymerases physiology
Deoxyribonucleases physiology
Dimerization
Globins physiology
Glycoproteins physiology
Immunoglobulin M biosynthesis
Lectins physiology
Membrane Glycoproteins physiology
Molecular Chaperones physiology
Oxidoreductases Acting on Sulfur Group Donors
Peptidylprolyl Isomerase physiology
Protein Disulfide-Isomerases physiology
Protein Transport physiology
Receptors, Antigen, T-Cell physiology
Saccharomyces cerevisiae Proteins physiology
Thyroglobulin biosynthesis
beta-Crystallin A Chain physiology
Cytosol physiology
Endoplasmic Reticulum physiology
HSP70 Heat-Shock Proteins physiology
Polymers
Protein Folding
Subjects
Details
- Language :
- English
- ISSN :
- 1742-464X
- Volume :
- 275
- Issue :
- 19
- Database :
- MEDLINE
- Journal :
- The FEBS journal
- Publication Type :
- Academic Journal
- Accession number :
- 18680510
- Full Text :
- https://doi.org/10.1111/j.1742-4658.2008.06590.x