Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Molecular Chaperones and Protein Folding03:00

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 Folding03:00

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 Maturation01:26

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...
The Proteasome01:13

The Proteasome

Eukaryotic cells can degrade proteins through several pathways. One of the most important among these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. This involves participation of a series of enzymes including— E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3 (ubiquitin...
The Proteasome02:18

The Proteasome

Eukaryotic cells can degrade proteins through several pathways. One of the most important amongst these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. A series of enzymes carry out the ubiquitination of the target proteins - E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
Export of Misfolded Proteins out of the ER01:32

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...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Quantitative prediction of oil-water interfacial tension in surfactant systems using dissipative particle dynamics.

Soft matter·2026
Same author

Assessment and Optimization of Force Fields for Glycine Polymorphism and Solution Properties.

Journal of chemical theory and computation·2026
Same author

Small heat shock proteins HspB1 and HspB5 differentially alter the condensation and aggregation of the TDP-43 low-complexity domain.

Protein science : a publication of the Protein Society·2026
Same author

Differential inclusion formation of an aggregation-prone protein reveals differences in the proteostasis capacity of neuronal cell lines.

Biochimica et biophysica acta. Molecular cell research·2026
Same author

Clusterin reverses epitheliopathy, reduces inflammation, and restores goblet cells and corneal nerves in a mouse model of autoimmune dry eye.

Scientific reports·2026
Same author

Clusterin: A clinical translation spearhead for extracellular chaperones that promotes neural regeneration.

Neural regeneration research·2026
Same journal

Lactate as a Chemical Modification on Proteins and Metabolites.

Annual review of biochemistry·2026
Same journal

Nucleocytoplasmic Transport.

Annual review of biochemistry·2026
Same journal

Packaging of Single-Stranded RNA in Viruses and Virus-Like Particles.

Annual review of biochemistry·2026
Same journal

Shaping of the Infant Gut Microbiome by Milk Oligosaccharides.

Annual review of biochemistry·2026
Same journal

Proteostasis Deregulation by Metabolism Drives the Hallmarks of Cancer.

Annual review of biochemistry·2026
Same journal

JoAnne Stubbe's Radical Path: A Story of Passion, Curiosity, and Persistence.

Annual review of biochemistry·2026
See all related articles

Related Experiment Video

Updated: May 14, 2026

Using Caenorhabditis elegans to Screen for Tissue-Specific Chaperone Interactions
06:55

Using Caenorhabditis elegans to Screen for Tissue-Specific Chaperone Interactions

Published on: June 7, 2020

Extracellular chaperones and proteostasis.

Amy R Wyatt1, Justin J Yerbury, Heath Ecroyd

  • 1School of Biological Sciences, University of Wollongong, Wollongong, New South Wales 2522, Australia. mrw@uow.edu.au

Annual Review of Biochemistry
|January 29, 2013
PubMed
Summary
This summary is machine-generated.

Extracellular chaperones sense and clear misfolded proteins, protecting against serious diseases. Further understanding proteostasis mechanisms is key to developing therapies for currently untreatable conditions.

More Related Videos

Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry
10:24

Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry

Published on: June 7, 2018

Intracellular Refolding Assay
07:18

Intracellular Refolding Assay

Published on: January 24, 2012

Related Experiment Videos

Last Updated: May 14, 2026

Using Caenorhabditis elegans to Screen for Tissue-Specific Chaperone Interactions
06:55

Using Caenorhabditis elegans to Screen for Tissue-Specific Chaperone Interactions

Published on: June 7, 2020

Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry
10:24

Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry

Published on: June 7, 2018

Intracellular Refolding Assay
07:18

Intracellular Refolding Assay

Published on: January 24, 2012

Area of Science:

  • Molecular Biology
  • Cellular Biology
  • Biochemistry

Background:

  • Untreatable diseases stem from misfolded and aggregated extracellular proteins.
  • Limited understanding of extracellular proteostasis mechanisms hinders therapeutic development.

Purpose of the Study:

  • Investigate the role of extracellular chaperones in maintaining proteostasis.
  • Elucidate mechanisms for sensing and clearing misfolded proteins in extracellular fluids.

Main Methods:

  • Discovery of constitutively secreted extracellular chaperones.
  • Analysis of chaperone function in sensing and disposal of misfolded proteins.

Main Results:

  • Extracellular chaperones identified as key players in proteostasis.
  • Evidence suggests chaperones act as sensors and disposal mediators for misfolded proteins.

Conclusions:

  • Extracellular chaperones are crucial for preventing disease pathologies.
  • Further research into extracellular proteostasis is essential for developing novel therapies for debilitating diseases.