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Updated: Jun 2, 2026

Detection of the pH-dependent Activity of Escherichia coli Chaperone HdeB In Vitro and In Vivo

Detection of the pH-dependent Activity of Escherichia coli Chaperone HdeB In Vitro and In Vivo

Published on: October 23, 2016

Extracellular Chaperones.

Rebecca A Dabbs, Amy R Wyatt, Justin J Yerbury

Topics in Current Chemistry

|April 26, 2011

Summary

This summary is machine-generated.

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Molecular Chaperones and Protein Folding

Molecular 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...

Molecular Chaperones and Protein Folding

Molecular 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...

Bacterial Protein Maturation

Bacterial 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...

Mitochondrial Precursor Proteins

Mitochondrial Precursor Proteins

Mitochondrial precursors are partially unfolded or loosely folded polypeptide chains. Newly synthesized precursors are inhibited from spontaneously folding into their native conformation by the cytosolic chaperones, heat shock proteins 70 (Hsp70), and mitochondrial import stimulation factors (MSFs). Precursors bound to MSFs are guided to the TOM70-TOM37 receptors, while precursors bound to Hsp70 chaperones are targetted to TOM20-TOM22 receptor complexes.
Most of the mitochondrial precursors...

Protein Folding Quality Check in the RER

Protein Folding Quality Check in the RER

ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...

Export of Misfolded Proteins out of the ER

Export of Misfolded Proteins out of the ER

After folding, the ER assesses the quality of secretory and membrane proteins. The correctly folded proteins are cleared by the calnexin cycle for transport to their final destination, while misfolded proteins are held back in the ER lumen. The ER chaperones attempt to unfold and refold the misfolded proteins but sometimes fail to achieve the correct native conformation. Such terminally misfolded proteins are then exported to the cytosol by ER-associated degradation or ERAD pathway for...

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Extracellular chaperones maintain protein homeostasis (proteostasis) in body fluids by preventing toxic protein aggregation. These proteins also aid in clearing misfolded proteins and may influence immune responses, offering new therapeutic avenues.

Area of Science:

Biochemistry
Cell Biology
Immunology

Background:

Proteostasis, the maintenance of protein levels and folding, is crucial for life.
Cellular proteostasis is well-understood, but extracellular mechanisms remain less clear.
Protein aggregation in extracellular fluids is linked to diseases like Alzheimer's, type II diabetes, and prion diseases.

Purpose of the Study:

To investigate the role of extracellular chaperones in maintaining proteostasis.
To understand how extracellular chaperones prevent and clear misfolded protein aggregates.
To explore the potential immunological functions of extracellular chaperones.

Main Methods:

Identification and characterization of extracellular chaperone families.
Assays to study chaperone binding to misfolded proteins.

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Using Caenorhabditis elegans to Screen for Tissue-Specific Chaperone Interactions

Using Caenorhabditis elegans to Screen for Tissue-Specific Chaperone Interactions

Published on: June 7, 2020

Intracellular Refolding Assay

Intracellular Refolding Assay

Published on: January 24, 2012

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Last Updated: Jun 2, 2026

Detection of the pH-dependent Activity of Escherichia coli Chaperone HdeB In Vitro and In Vivo

Detection of the pH-dependent Activity of Escherichia coli Chaperone HdeB In Vitro and In Vivo

Published on: October 23, 2016

Using Caenorhabditis elegans to Screen for Tissue-Specific Chaperone Interactions

Using Caenorhabditis elegans to Screen for Tissue-Specific Chaperone Interactions

Published on: June 7, 2020

Intracellular Refolding Assay

Intracellular Refolding Assay

Published on: January 24, 2012

Investigation of chaperone-mediated clearance pathways (e.g., endocytosis).

Exploration of chaperone interactions with immune components.

Main Results:

Extracellular chaperones selectively bind hydrophobic regions of misfolded proteins.
Chaperones inhibit protein toxicity and prevent aggregation into insoluble deposits.
Chaperones facilitate the clearance of soluble misfolded proteins via receptor-mediated endocytosis and lysosomal degradation.
Emerging evidence suggests extracellular chaperones modulate immune responses.

Conclusions:

Extracellular chaperones are key players in maintaining extracellular proteostasis.
These chaperones offer novel therapeutic targets for protein misfolding diseases.
Further research into extracellular chaperones could advance treatments for proteostasis and immune-related disorders.