Chaperones in control of protein disaggregation
- 23 January 2008
- journal article
- review article
- Published by Springer Science and Business Media LLC in The EMBO Journal
- Vol. 27 (2), 328-335
- https://doi.org/10.1038/sj.emboj.7601970
Abstract
The chaperone protein network controls both initial protein folding and subsequent maintenance of proteins in the cell. Although the native structure of a protein is principally encoded in its amino‐acid sequence, the process of folding in vivo very often requires the assistance of molecular chaperones. Chaperones also play a role in a post‐translational quality control system and thus are required to maintain the proper conformation of proteins under changing environmental conditions. Many factors leading to unfolding and misfolding of proteins eventually result in protein aggregation. Stress imposed by high temperature was one of the first aggregation‐inducing factors studied and remains one of the main models in this field. With massive protein aggregation occurring in response to heat exposure, the cell needs chaperones to control and counteract the aggregation process. Elimination of aggregates can be achieved by solubilization of aggregates and either refolding of the liberated polypeptides or their proteolysis. Here, we focus on the molecular mechanisms by which heat‐shock protein 70 (Hsp70), Hsp100 and small Hsp chaperones liberate and refold polypeptides trapped in protein aggregates.Keywords
This publication has 86 references indexed in Scilit:
- Folding versus aggregation: Polypeptide conformations on competing pathwaysArchives of Biochemistry and Biophysics, 2008
- Processing of Proteins by the Molecular Chaperone Hsp104Journal of Molecular Biology, 2007
- Collaboration between the ClpB AAA+ remodeling protein and the DnaK chaperone systemProceedings of the National Academy of Sciences of the United States of America, 2007
- Asymmetric deceleration of ClpB or Hsp104 ATPase activity unleashes protein-remodeling activityNature Structural & Molecular Biology, 2007
- Visualizing the ATPase Cycle in a Protein Disaggregating Machine: Structural Basis for Substrate Binding by ClpBMolecular Cell, 2007
- The Cytoplasmic Hsp70 Chaperone Machinery Subjects Misfolded and Endoplasmic Reticulum Import-incompetent Proteins to Degradation via the Ubiquitin–Proteasome SystemMolecular Biology of the Cell, 2007
- A camel passes through the eye of a needle: protein unfolding activity of Clp ATPasesMolecular Microbiology, 2006
- Missense meanderings in sequence space: a biophysical view of protein evolutionNature Reviews Genetics, 2005
- Folding properties of the nucleotide exchange factor GrpE from Thermus thermophilus: GrpE is a thermosensor that mediates heat shock responseJournal of Molecular Biology, 2001
- Identification of thermolabile Escherichia coli proteins: prevention and reversion of aggregation by DnaK and ClpBThe EMBO Journal, 1999