Related Experiment Video
Updated: May 29, 2026
06:55
Using Caenorhabditis elegans to Screen for Tissue-Specific Chaperone Interactions
Published on: June 7, 2020
Expanding the cellular molecular chaperone network through the ubiquitous cochaperones
Frank J Echtenkamp1, Brian C Freeman
1Department of Cell and Development Biology, University of Illinois, Urbana, IL, USA.
Biochimica Et Biophysica Acta
|September 6, 2011
Summary
Molecular chaperone networks maintain cellular order. This review highlights Heat Shock Protein 90 (HSP90) cochaperones, showing how they diversify protein regulation and expand chaperone network reach.
Area of Science:
- Cellular biology
- Molecular biology
- Biochemistry
Background:
- Cells require complex protein networks for homeostasis.
- Molecular chaperones and cochaperones maintain cellular order.
- Heat Shock Protein 90 (HSP90) is a key chaperone.
Purpose of the Study:
- To review HSP90-associated cochaperones.
- To present a model for cochaperone function.
- To explore cochaperone roles in protein regulation.
Main Methods:
- Literature review of HSP90 and cochaperone studies.
- Analysis of existing data on cochaperone-client interactions.
- Synthesis of evidence supporting a functional model.
Main Results:
- HSP90 cochaperones possess inherent chaperoning abilities.
- Select cochaperones differentially modulate target proteins.
- Cochaperones contribute to combinatorial client regulation.
- Cochaperones expand the reach of chaperone networks.
Conclusions:
- HSP90 cochaperones are crucial for cellular regulation.
- Cochaperones enhance the versatility of chaperone networks.
- Understanding cochaperone function is key to cellular homeostasis.
Related Concept Videos
03:00Molecular Chaperones and Protein Folding
The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
The...
03:00Molecular Chaperones and Protein Folding
The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
The...
01:26Bacterial Protein Maturation
Bacterial protein maturation is a tightly regulated process that ensures newly synthesized polypeptides achieve correct functional conformations. This maturation involves a series of modifications, folding events, and quality control steps, often assisted by specialized chaperone proteins.N-Terminal ModificationsThe maturation of bacterial polypeptides begins cotranslationally as the polypeptide exits the ribosome. The first amino acid, N-formylmethionine (fMet), is typically modified at the...
01:31Regulation of the Unfolded Protein Response
Inositol-requiring kinase one or IRE1 is the most conserved eukaryotic unfolded protein response (UPR) receptor. It is a type I transmembrane protein kinase receptor with a distinctive site-specific RNase activity. As the binding mechanics of the misfolded proteins with the N-terminal domain of IRE-1 are unclear, three binding models — direct, indirect, and allosteric -- are proposed for receptor activation. Nevertheless, it is known that once a misfolded protein associates with IRE1, it...
02:04Covalently Linked Protein Regulators
Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein.
These groups modify specific amino acids in a protein.
02:04Covalently Linked Protein Regulators
Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein.
These groups modify specific amino acids in a protein.