Protein folding includes oligomerization – examples from the endoplasmic reticulum and cytosol
- 11 September 2008
- journal article
- review article
- Published by Wiley in The FEBS Journal
- Vol. 275 (19), 4700-4727
- https://doi.org/10.1111/j.1742-4658.2008.06590.x
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.Keywords
This publication has 118 references indexed in Scilit:
- Characterization of an ERAD Pathway for Nonglycosylated BiP Substrates, which Require HerpMolecular Cell, 2007
- Structures of GRP94-Nucleotide Complexes Reveal Mechanistic Differences between the hsp90 ChaperonesMolecular Cell, 2007
- Hsp70 Chaperone Ligands Control Domain Association via an Allosteric Mechanism Mediated by the Interdomain LinkerMolecular Cell, 2007
- Substrate-Specific Translocational Attenuation during ER Stress Defines a Pre-Emptive Quality Control PathwayCell, 2006
- The Structure of the ζζ Transmembrane Dimer Reveals Features Essential for Its Assembly with the T Cell ReceptorCell, 2006
- Distinct Ubiquitin-Ligase Complexes Define Convergent Pathways for the Degradation of ER ProteinsCell, 2006
- Molecular Chaperones and Protein Quality ControlCell, 2006
- Structure of an LDLR-RAP Complex Reveals a General Mode for Ligand Recognition by Lipoprotein ReceptorsMolecular Cell, 2006
- A transmembrane protein with a cdc2+CDC28-related kinase activity is required for signaling from the ER to the nucleusCell, 1993
- Transcriptional induction of genes encoding endoplasmic reticulum resident proteins requires a transmembrane protein kinaseCell, 1993